BindingDB Reactant_set_id Ligand SMILES Ligand InChI Ligand InChI Key BindingDB MonomerID BindingDB Ligand Name Target Name Target Source Organism According to Curator or DataSource Ki (nM) IC50 (nM) Kd (nM) EC50 (nM) kon (M-1-s-1) koff (s-1) pH Temp (C) Curation/DataSource Article DOI BindingDB Entry DOI PMID PubChem AID Patent Number Authors Institution Link to Ligand in BindingDB Link to Target in BindingDB Link to Ligand-Target Pair in BindingDB Ligand HET ID in PDB PDB ID(s) for Ligand-Target Complex PubChem CID of Ligand PubChem SID of Ligand ChEBI ID of Ligand ChEMBL ID of Ligand DrugBank ID of Ligand IUPHAR_GRAC ID of Ligand KEGG ID of Ligand ZINC ID of Ligand Number of Protein Chains in Target (>1 implies a multichain complex) BindingDB Target Chain Sequence PDB ID(s) of Target Chain UniProt (SwissProt) Recommended Name of Target Chain UniProt (SwissProt) Entry Name of Target Chain UniProt (SwissProt) Primary ID of Target Chain UniProt (SwissProt) Secondary ID(s) of Target Chain UniProt (SwissProt) Alternative ID(s) of Target Chain UniProt (TrEMBL) Submitted Name of Target Chain UniProt (TrEMBL) Entry Name of Target Chain UniProt (TrEMBL) Primary ID of Target Chain UniProt (TrEMBL) Secondary ID(s) of Target Chain UniProt (TrEMBL) Alternative ID(s) of Target Chain 34206 CC(C=CC(=O)NO)C=C(C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20) ALCVRKZFLFWUAZ-UHFFFAOYSA-N 19130 (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide::CHEMBL99::TSA::Trichostatin A (TSA) Histone deacetylase 4 Homo sapiens 34 Curated from the literature by BindingDB 10.1021/jm7009217 10.7270/Q2XK8CT6 17929798 aid1797824 Itoh, Y; Suzuki, T; Kouketsu, A; Suzuki, N; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19130 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19130&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 91895926 46519165 46024 CHEMBL99 7005 ZINC05579377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34207 SCCCCCCC(=O)Nc1nc(cs1)-c1ccccc1 InChI=1S/C16H20N2OS2/c19-15(10-6-1-2-7-11-20)18-16-17-14(12-21-16)13-8-4-3-5-9-13/h3-5,8-9,12,20H,1-2,6-7,10-11H2,(H,17,18,19) LUXAHBUKMVESIS-UHFFFAOYSA-N 19131 CHEMBL419758::JMC505425 Compound 7::N-(4-phenyl-1,3-thiazol-2-yl)-7-sulfanylheptanamide::NCH-31 Histone deacetylase 4 Homo sapiens 32 Curated from the literature by BindingDB 10.1021/jm7009217 10.7270/Q2XK8CT6 17929798 aid1797824 Itoh, Y; Suzuki, T; Kouketsu, A; Suzuki, N; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19131 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19131&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11427204 46519166 CHEMBL419758 ZINC13609382 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34208 CC(C)(C)OC(=O)N[C@@H](CCCCCS)C(=O)Nc1cccc(c1)-c1ccccc1 InChI=1S/C24H32N2O3S/c1-24(2,3)29-23(28)26-21(15-8-5-9-16-30)22(27)25-20-14-10-13-19(17-20)18-11-6-4-7-12-18/h4,6-7,10-14,17,21,30H,5,8-9,15-16H2,1-3H3,(H,25,27)(H,26,28)/t21-/m0/s1 JITODBYUQIXPEO-NRFANRHFSA-N 19132 tert-butyl N-[(1S)-1-[(3-phenylphenyl)carbamoyl]-6-sulfanylhexyl]carbamate::thiolate analogue, 13a Histone deacetylase 4 Homo sapiens 38 Curated from the literature by BindingDB 10.1021/jm7009217 10.7270/Q2XK8CT6 17929798 aid1797824 Itoh, Y; Suzuki, T; Kouketsu, A; Suzuki, N; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19132 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19132&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23648185 46519167 ZINC14969966 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34209 CC(C)(C)OC(=O)N[C@@H](CCCCCS)C(=O)Nc1cnc2ccccc2c1 InChI=1S/C21H29N3O3S/c1-21(2,3)27-20(26)24-18(11-5-4-8-12-28)19(25)23-16-13-15-9-6-7-10-17(15)22-14-16/h6-7,9-10,13-14,18,28H,4-5,8,11-12H2,1-3H3,(H,23,25)(H,24,26)/t18-/m0/s1 ULIPYSGEVHHKMB-SFHVURJKSA-N 19133 tert-butyl N-[(1S)-1-(quinolin-3-ylcarbamoyl)-6-sulfanylhexyl]carbamate::thiolate analogue, 15a Histone deacetylase 4 Homo sapiens 33 Curated from the literature by BindingDB 10.1021/jm7009217 10.7270/Q2XK8CT6 17929798 aid1797824 Itoh, Y; Suzuki, T; Kouketsu, A; Suzuki, N; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19133 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19133&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23634769 46519168 ZINC14969971 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34210 CC(C)(C)OC(=O)N[C@@H](CCCCCS)C(=O)NC1CCCC1 InChI=1S/C17H32N2O3S/c1-17(2,3)22-16(21)19-14(11-5-4-8-12-23)15(20)18-13-9-6-7-10-13/h13-14,23H,4-12H2,1-3H3,(H,18,20)(H,19,21)/t14-/m0/s1 IKSFNOMXHPMYIQ-AWEZNQCLSA-N 19134 CHEMBL213934::tert-butyl N-[(1S)-1-(cyclopentylcarbamoyl)-6-sulfanylhexyl]carbamate::thiolate analogue, 16a Histone deacetylase 4 Homo sapiens 1030 Curated from the literature by BindingDB 10.1021/jm7009217 10.7270/Q2XK8CT6 17929798 aid1797824 Itoh, Y; Suzuki, T; Kouketsu, A; Suzuki, N; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19134 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19134&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11844891 46519169 CHEMBL213934 ZINC14969975 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34211 CC(C)(C)OC(=O)N[C@@H](CCCCCS)C(=O)NC1CCCCC1 InChI=1S/C18H34N2O3S/c1-18(2,3)23-17(22)20-15(12-8-5-9-13-24)16(21)19-14-10-6-4-7-11-14/h14-15,24H,4-13H2,1-3H3,(H,19,21)(H,20,22)/t15-/m0/s1 NREURQUIJSGJMZ-HNNXBMFYSA-N 19135 CHEMBL209551::tert-butyl N-[(1S)-1-(cyclohexylcarbamoyl)-6-sulfanylhexyl]carbamate::thiolate analogue, 17a Histone deacetylase 4 Homo sapiens 1140 Curated from the literature by BindingDB 10.1021/jm7009217 10.7270/Q2XK8CT6 17929798 aid1797824 Itoh, Y; Suzuki, T; Kouketsu, A; Suzuki, N; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19135 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19135&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11844892 46519170 CHEMBL209551 ZINC14969979 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34212 CC(C)(C)OC(=O)N[C@@H](CCCCCS)C(=O)NC1CCCCCC1 InChI=1S/C19H36N2O3S/c1-19(2,3)24-18(23)21-16(13-9-6-10-14-25)17(22)20-15-11-7-4-5-8-12-15/h15-16,25H,4-14H2,1-3H3,(H,20,22)(H,21,23)/t16-/m0/s1 RTVMPAGMFUPGRI-INIZCTEOSA-N 19136 CHEMBL379049::tert-butyl N-[(1S)-1-(cycloheptylcarbamoyl)-6-sulfanylhexyl]carbamate::thiolate analogue, 18a Histone deacetylase 4 Homo sapiens 840 Curated from the literature by BindingDB 10.1021/jm7009217 10.7270/Q2XK8CT6 17929798 aid1797824 Itoh, Y; Suzuki, T; Kouketsu, A; Suzuki, N; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19136 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19136&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11844893 46519171 CHEMBL379049 ZINC14969983 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34213 CC(C)(C)NC(=O)[C@H](CCCCCS)NC(=O)OC(C)(C)C InChI=1S/C16H32N2O3S/c1-15(2,3)18-13(19)12(10-8-7-9-11-22)17-14(20)21-16(4,5)6/h12,22H,7-11H2,1-6H3,(H,17,20)(H,18,19)/t12-/m0/s1 FYJYSSQDWGZNHS-LBPRGKRZSA-N 19137 tert-butyl N-[(1S)-1-(tert-butylcarbamoyl)-6-sulfanylhexyl]carbamate::thiolate analogue, 19a Histone deacetylase 4 Homo sapiens 1900 Curated from the literature by BindingDB 10.1021/jm7009217 10.7270/Q2XK8CT6 17929798 aid1797824 Itoh, Y; Suzuki, T; Kouketsu, A; Suzuki, N; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19137 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19137&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23634770 46519172 ZINC14969987 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34214 CC(C)(C)OC(=O)N[C@@H](CCCCCS)C(=O)NC12CC3CC(CC(C3)C1)C2 InChI=1S/C22H38N2O3S/c1-21(2,3)27-20(26)23-18(7-5-4-6-8-28)19(25)24-22-12-15-9-16(13-22)11-17(10-15)14-22/h15-18,28H,4-14H2,1-3H3,(H,23,26)(H,24,25)/t15?,16?,17?,18-,22?/m0/s1 NKBMBTJJIYPODH-XDHFQJGLSA-N 19138 tert-butyl N-[(1S)-1-(adamantan-1-ylcarbamoyl)-6-sulfanylhexyl]carbamate::thiolate analogue, 20a Histone deacetylase 4 Homo sapiens 4200 Curated from the literature by BindingDB 10.1021/jm7009217 10.7270/Q2XK8CT6 17929798 aid1797824 Itoh, Y; Suzuki, T; Kouketsu, A; Suzuki, N; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19138 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19138&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23634771 46519173 ZINC14969991 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34215 N[C@@H](CCCCCS)C(=O)NC1CCCC1 InChI=1S/C12H24N2OS/c13-11(8-2-1-5-9-16)12(15)14-10-6-3-4-7-10/h10-11,16H,1-9,13H2,(H,14,15)/t11-/m0/s1 BNEXTTBMNDFSSZ-NSHDSACASA-N 19139 (2S)-2-amino-N-cyclopentyl-7-sulfanylheptanamide::thiolate analogue, 26a Histone deacetylase 4 Homo sapiens 31200 Curated from the literature by BindingDB 10.1021/jm7009217 10.7270/Q2XK8CT6 17929798 aid1797824 Itoh, Y; Suzuki, T; Kouketsu, A; Suzuki, N; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19139 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19139&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23634888 46519174 ZINC14969995 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34216 SCCCCC[C@H](NC(=O)c1ccccc1)C(=O)NC1CCCC1 InChI=1S/C19H28N2O2S/c22-18(15-9-3-1-4-10-15)21-17(13-5-2-8-14-24)19(23)20-16-11-6-7-12-16/h1,3-4,9-10,16-17,24H,2,5-8,11-14H2,(H,20,23)(H,21,22)/t17-/m0/s1 IKSCZYXAUUPGHW-KRWDZBQOSA-N 19140 (2S)-N-cyclopentyl-2-(phenylformamido)-7-sulfanylheptanamide::thiolate analogue, 27a Histone deacetylase 4 Homo sapiens 280 Curated from the literature by BindingDB 10.1021/jm7009217 10.7270/Q2XK8CT6 17929798 aid1797824 Itoh, Y; Suzuki, T; Kouketsu, A; Suzuki, N; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19140 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19140&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23634889 46519175 ZINC14969999 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34217 SCCCCC[C@H](NC(=O)c1ccc(Cl)cc1)C(=O)NC1CCCC1 InChI=1S/C19H27ClN2O2S/c20-15-11-9-14(10-12-15)18(23)22-17(8-2-1-5-13-25)19(24)21-16-6-3-4-7-16/h9-12,16-17,25H,1-8,13H2,(H,21,24)(H,22,23)/t17-/m0/s1 JYRNZXYEKQYJDP-KRWDZBQOSA-N 19141 (2S)-2-[(4-chlorophenyl)formamido]-N-cyclopentyl-7-sulfanylheptanamide::thiolate analogue, 28a Histone deacetylase 4 Homo sapiens 650 Curated from the literature by BindingDB 10.1021/jm7009217 10.7270/Q2XK8CT6 17929798 aid1797824 Itoh, Y; Suzuki, T; Kouketsu, A; Suzuki, N; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19141 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19141&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23634890 46519176 ZINC14970004 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34218 OCC(=O)N[C@@H](CCCCCS)C(=O)NC1CCCC1 InChI=1S/C14H26N2O3S/c17-10-13(18)16-12(8-2-1-5-9-20)14(19)15-11-6-3-4-7-11/h11-12,17,20H,1-10H2,(H,15,19)(H,16,18)/t12-/m0/s1 YFJMWUCZDQRYEZ-LBPRGKRZSA-N 19142 (2S)-N-cyclopentyl-2-(2-hydroxyacetamido)-7-sulfanylheptanamide::thiolate analogue, 30a Histone deacetylase 4 Homo sapiens 970 Curated from the literature by BindingDB 10.1021/jm7009217 10.7270/Q2XK8CT6 17929798 aid1797824 Itoh, Y; Suzuki, T; Kouketsu, A; Suzuki, N; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19142 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19142&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23634891 46519177 ZINC14970008 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34219 CC(C)(C)C(=O)N[C@@H](CCCCCS)C(=O)NC1CCCC1 InChI=1S/C17H32N2O2S/c1-17(2,3)16(21)19-14(11-5-4-8-12-22)15(20)18-13-9-6-7-10-13/h13-14,22H,4-12H2,1-3H3,(H,18,20)(H,19,21)/t14-/m0/s1 CSQHTINQZNDANL-AWEZNQCLSA-N 19143 (2S)-N-cyclopentyl-2-(2,2-dimethylpropanamido)-7-sulfanylheptanamide::thiolate analogue, 33a Histone deacetylase 4 Homo sapiens 730 Curated from the literature by BindingDB 10.1021/jm7009217 10.7270/Q2XK8CT6 17929798 aid1797824 Itoh, Y; Suzuki, T; Kouketsu, A; Suzuki, N; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19143 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19143&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23634892 46519178 ZINC14970012 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34220 CC(C)(C)NC(=O)N[C@@H](CCCCCS)C(=O)NC1CCCC1 InChI=1S/C17H33N3O2S/c1-17(2,3)20-16(22)19-14(11-5-4-8-12-23)15(21)18-13-9-6-7-10-13/h13-14,23H,4-12H2,1-3H3,(H,18,21)(H2,19,20,22)/t14-/m0/s1 CBRFYHIFCHDUDU-AWEZNQCLSA-N 19144 (2S)-2-[(tert-butylcarbamoyl)amino]-N-cyclopentyl-7-sulfanylheptanamide::thiolate analogue, 35a Histone deacetylase 4 Homo sapiens 310 Curated from the literature by BindingDB 10.1021/jm7009217 10.7270/Q2XK8CT6 17929798 aid1797824 Itoh, Y; Suzuki, T; Kouketsu, A; Suzuki, N; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19144 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19144&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23634893 46519179 ZINC14970016 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34221 CC(C)(C)NC(=S)N[C@@H](CCCCCS)C(=O)NC1CCCC1 InChI=1S/C17H33N3OS2/c1-17(2,3)20-16(23)19-14(11-5-4-8-12-22)15(21)18-13-9-6-7-10-13/h13-14,22H,4-12H2,1-3H3,(H,18,21)(H2,19,20,23)/t14-/m0/s1 VXMHHEQJZJBMRW-AWEZNQCLSA-N 19145 (2S)-2-[(tert-butylcarbamothioyl)amino]-N-cyclopentyl-7-sulfanylheptanamide::thiolate analogue, 36a Histone deacetylase 4 Homo sapiens 220 Curated from the literature by BindingDB 10.1021/jm7009217 10.7270/Q2XK8CT6 17929798 aid1797824 Itoh, Y; Suzuki, T; Kouketsu, A; Suzuki, N; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19145 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19145&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23634894 46519180 ZINC14970020 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34222 COC(=O)N[C@@H](CCCCCS)C(=O)NC1CCCC1 InChI=1S/C14H26N2O3S/c1-19-14(18)16-12(9-3-2-6-10-20)13(17)15-11-7-4-5-8-11/h11-12,20H,2-10H2,1H3,(H,15,17)(H,16,18)/t12-/m0/s1 JTOYXAPQCNRTSP-LBPRGKRZSA-N 19146 methyl N-[(1S)-1-(cyclopentylcarbamoyl)-6-sulfanylhexyl]carbamate::thiolate analogue, 37a Histone deacetylase 4 Homo sapiens 1160 Curated from the literature by BindingDB 10.1021/jm7009217 10.7270/Q2XK8CT6 17929798 aid1797824 Itoh, Y; Suzuki, T; Kouketsu, A; Suzuki, N; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19146 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19146&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23634895 46519181 ZINC14970024 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34223 SCCCCC[C@H](NC(=O)OC1CCCCC1)C(=O)NC1CCCC1 InChI=1S/C19H34N2O3S/c22-18(20-15-9-6-7-10-15)17(13-5-2-8-14-25)21-19(23)24-16-11-3-1-4-12-16/h15-17,25H,1-14H2,(H,20,22)(H,21,23)/t17-/m0/s1 FCXNEJOVTQTYLD-KRWDZBQOSA-N 19147 cyclohexyl N-[(1S)-1-(cyclopentylcarbamoyl)-6-sulfanylhexyl]carbamate::thiolate analogue, 38a Histone deacetylase 4 Homo sapiens 580 Curated from the literature by BindingDB 10.1021/jm7009217 10.7270/Q2XK8CT6 17929798 aid1797824 Itoh, Y; Suzuki, T; Kouketsu, A; Suzuki, N; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19147 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19147&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23635016 46519182 ZINC14970028 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34224 SCCCCC[C@H](NC(=O)OCc1ccccc1)C(=O)NC1CCCC1 InChI=1S/C20H30N2O3S/c23-19(21-17-11-6-7-12-17)18(13-5-2-8-14-26)22-20(24)25-15-16-9-3-1-4-10-16/h1,3-4,9-10,17-18,26H,2,5-8,11-15H2,(H,21,23)(H,22,24)/t18-/m0/s1 TYBDKDNZVXAQGQ-SFHVURJKSA-N 19148 benzyl N-[(1S)-1-(cyclopentylcarbamoyl)-6-sulfanylhexyl]carbamate::thiolate analogue, 40a Histone deacetylase 4 Homo sapiens 130 Curated from the literature by BindingDB 10.1021/jm7009217 10.7270/Q2XK8CT6 17929798 aid1797824 Itoh, Y; Suzuki, T; Kouketsu, A; Suzuki, N; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19148 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19148&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23635017 46519183 ZINC14970032 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34245 CC(C=CC(=O)NO)C=C(C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20) ALCVRKZFLFWUAZ-UHFFFAOYSA-N 19130 (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide::CHEMBL99::TSA::Trichostatin A (TSA) Histone deacetylase 4 Homo sapiens 20 8 37.00 C Curated from the literature by BindingDB 10.1016/j.bmc.2005.12.063 10.7270/Q2P55KRB 16439135 aid1797827 Bhuiyan, MP; Kato, T; Okauchi, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Kyushu Institute of Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19130 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19130&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 91895926 46519165 46024 CHEMBL99 7005 ZINC05579377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34246 CC1(C)NC(=O)[C@H](CCCCCC=C)NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC1=O InChI=1S/C27H38N4O4/c1-4-5-6-7-11-15-20-23(32)30-27(2,3)26(35)29-21(18-19-13-9-8-10-14-19)25(34)31-17-12-16-22(31)24(33)28-20/h4,8-10,13-14,20-22H,1,5-7,11-12,15-18H2,2-3H3,(H,28,33)(H,29,35)(H,30,32)/t20-,21-,22+/m0/s1 JGLNPLYOZKFHDE-FDFHNCONSA-N 19156 (3S,9S,14aR)-9-benzyl-3-(hept-6-en-1-yl)-6,6-dimethyl-tetradecahydropyrrolo[1,2-a][,,,]cyclododecane-1,4,7,10-tetrone::cyclo(-L-Ae9-Aib-L-Phe-D-Pro-), 1 Histone deacetylase 4 Homo sapiens >100000 8 37.00 C Curated from the literature by BindingDB 10.1016/j.bmc.2005.12.063 10.7270/Q2P55KRB 16439135 aid1797827 Bhuiyan, MP; Kato, T; Okauchi, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Kyushu Institute of Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19156 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19156&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23648188 46519190 ZINC14970052 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34247 CC1(C)NC(=O)[C@H](CCCCCC2CO2)NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC1=O InChI=1S/C27H38N4O5/c1-27(2)26(35)29-21(16-18-10-5-3-6-11-18)25(34)31-15-9-14-22(31)24(33)28-20(23(32)30-27)13-8-4-7-12-19-17-36-19/h3,5-6,10-11,19-22H,4,7-9,12-17H2,1-2H3,(H,28,33)(H,29,35)(H,30,32)/t19?,20-,21-,22+/m0/s1 QKELJHBCMVDGRQ-GEIYVISESA-N 19157 (3S,9S,14aR)-9-benzyl-6,6-dimethyl-3-[5-(oxiran-2-yl)pentyl]-tetradecahydropyrrolo[1,2-a][,,,]cyclododecane-1,4,7,10-tetrone::chlamydocin-epoxide analog, 2 Histone deacetylase 4 Homo sapiens 4050 8 37.00 C Curated from the literature by BindingDB 10.1016/j.bmc.2005.12.063 10.7270/Q2P55KRB 16439135 aid1797827 Bhuiyan, MP; Kato, T; Okauchi, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Kyushu Institute of Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19157 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19157&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23648189 46519191 ZINC14970061 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34248 CC1(C)NC(=O)[C@H](CCCCCC(=O)CBr)NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC1=O InChI=1S/C27H37BrN4O5/c1-27(2)26(37)30-21(16-18-10-5-3-6-11-18)25(36)32-15-9-14-22(32)24(35)29-20(23(34)31-27)13-8-4-7-12-19(33)17-28/h3,5-6,10-11,20-22H,4,7-9,12-17H2,1-2H3,(H,29,35)(H,30,37)(H,31,34)/t20-,21-,22+/m0/s1 JVGKFKCLINQLIO-FDFHNCONSA-N 19158 (3S,9S,14aR)-9-benzyl-3-(7-bromo-6-oxoheptyl)-6,6-dimethyl-tetradecahydropyrrolo[1,2-a][,,,]cyclododecane-1,4,7,10-tetrone::chlamydocin-bromomethylketone analog, 4 Histone deacetylase 4 Homo sapiens 59.5 8 37.00 C Curated from the literature by BindingDB 10.1016/j.bmc.2005.12.063 10.7270/Q2P55KRB 16439135 aid1797827 Bhuiyan, MP; Kato, T; Okauchi, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Kyushu Institute of Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19158 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19158&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23648190 46519192 ZINC14970066 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34249 CC(=O)CCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC(=O)C(C)(C)NC1=O InChI=1S/C27H38N4O5/c1-18(32)11-6-4-9-14-20-23(33)30-27(2,3)26(36)29-21(17-19-12-7-5-8-13-19)25(35)31-16-10-15-22(31)24(34)28-20/h5,7-8,12-13,20-22H,4,6,9-11,14-17H2,1-3H3,(H,28,34)(H,29,36)(H,30,33)/t20-,21-,22+/m0/s1 LROHGDHXLCJFFJ-FDFHNCONSA-N 19159 (3S,9S,14aR)-9-benzyl-6,6-dimethyl-3-(6-oxoheptyl)-tetradecahydropyrrolo[1,2-a][,,,]cyclododecane-1,4,7,10-tetrone::chlamydocin-methylketone analog, 5 Histone deacetylase 4 Homo sapiens 290 8 37.00 C Curated from the literature by BindingDB 10.1016/j.bmc.2005.12.063 10.7270/Q2P55KRB 16439135 aid1797827 Bhuiyan, MP; Kato, T; Okauchi, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Kyushu Institute of Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19159 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19159&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23648191 46519193 ZINC14970071 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34250 CC1(C)NC(=O)[C@H](CCCCCC(O)CO)NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC1=O InChI=1S/C27H40N4O6/c1-27(2)26(37)29-21(16-18-10-5-3-6-11-18)25(36)31-15-9-14-22(31)24(35)28-20(23(34)30-27)13-8-4-7-12-19(33)17-32/h3,5-6,10-11,19-22,32-33H,4,7-9,12-17H2,1-2H3,(H,28,35)(H,29,37)(H,30,34)/t19?,20-,21-,22+/m0/s1 NNQJJGWQFNOJGP-GEIYVISESA-N 19160 (3S,9S,14aR)-9-benzyl-3-(6,7-dihydroxyheptyl)-6,6-dimethyl-tetradecahydropyrrolo[1,2-a][,,,]cyclododecane-1,4,7,10-tetrone::chlamydocin-diol analog, 6 Histone deacetylase 4 Homo sapiens >100000 8 37.00 C Curated from the literature by BindingDB 10.1016/j.bmc.2005.12.063 10.7270/Q2P55KRB 16439135 aid1797827 Bhuiyan, MP; Kato, T; Okauchi, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Kyushu Institute of Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19160 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19160&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23648192 46519194 ZINC14970079 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34251 CC1(C)NC(=O)[C@H](CCCCCC=O)NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC1=O InChI=1S/C26H36N4O5/c1-26(2)25(35)28-20(17-18-11-6-5-7-12-18)24(34)30-15-10-14-21(30)23(33)27-19(22(32)29-26)13-8-3-4-9-16-31/h5-7,11-12,16,19-21H,3-4,8-10,13-15,17H2,1-2H3,(H,27,33)(H,28,35)(H,29,32)/t19-,20-,21+/m0/s1 UYAIPFJESUYYPF-PCCBWWKXSA-N 19161 6-[(3S,9S,14aR)-9-benzyl-6,6-dimethyl-1,4,7,10-tetraoxo-tetradecahydropyrrolo[1,2-a][,,,]cyclododecan-3-yl]hexanal::chlamydocin-aldehyde analog, 7 Histone deacetylase 4 Homo sapiens 1290 8 37.00 C Curated from the literature by BindingDB 10.1016/j.bmc.2005.12.063 10.7270/Q2P55KRB 16439135 aid1797827 Bhuiyan, MP; Kato, T; Okauchi, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Kyushu Institute of Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19161 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19161&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 10896194 46519195 C00609 ZINC14970082 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 34252 CC1(C)NC(=O)[C@H](CCCCCC(=O)CO)NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC1=O InChI=1S/C27H38N4O6/c1-27(2)26(37)29-21(16-18-10-5-3-6-11-18)25(36)31-15-9-14-22(31)24(35)28-20(23(34)30-27)13-8-4-7-12-19(33)17-32/h3,5-6,10-11,20-22,32H,4,7-9,12-17H2,1-2H3,(H,28,35)(H,29,37)(H,30,34)/t20-,21-,22+/m0/s1 XXRCTSZBEZSWSN-FDFHNCONSA-N 19162 (3S,9S,14aR)-9-benzyl-3-(7-hydroxy-6-oxoheptyl)-6,6-dimethyl-tetradecahydropyrrolo[1,2-a][,,,]cyclododecane-1,4,7,10-tetrone::chlamydocin-hydroxymethylketone analog, 10 Histone deacetylase 4 Homo sapiens 60.4 8 37.00 C Curated from the literature by BindingDB 10.1016/j.bmc.2005.12.063 10.7270/Q2P55KRB 16439135 aid1797827 Bhuiyan, MP; Kato, T; Okauchi, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Kyushu Institute of Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19162 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19162&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11964530 46519196 ZINC14970086 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 44663 Nc1ccccc1NC(=O)c1ccc(CNc2nccc(n2)-c2cccnc2)cc1 InChI=1S/C23H20N6O/c24-19-5-1-2-6-21(19)28-22(30)17-9-7-16(8-10-17)14-27-23-26-13-11-20(29-23)18-4-3-12-25-15-18/h1-13,15H,14,24H2,(H,28,30)(H,26,27,29) HRNLUBSXIHFDHP-UHFFFAOYSA-N 24624 CHEMBL272980::MGCD-0103::MGCD0103::N-(2-aminophenyl)-4-({[4-(pyridin-3-yl)pyrimidin-2-yl]amino}methyl)benzamide::US10227295, Compound MGCD0103::US11377423, MGCD-0103::US9409858, MGCD0103::US9751832, MGCD0103::US9956192, Compound MGCD0103 Histone deacetylase 4 Homo sapiens >10000 8 37.00 C Curated from the literature by BindingDB 10.1021/jm800251w 10.7270/Q28P5XTT 18570366 aid1798452 Zhou, N; Moradei, O; Raeppel, S; Leit, S; Frechette, S; Gaudette, F; Paquin, I; Bernstein, N; Bouchain, G; Vaisburg, A; Jin, Z; Gillespie, J; Wang, J; Fournel, M; Yan, PT; Trachy-Bourget, MC; Kalita, A; Lu, A; Rahil, J; MacLeod, AR; Li, Z; Besterman, JM; Delorme, D MethylGene Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=24624 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=24624&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 9865515 56269575 CHEMBL272980 7008 ZINC13986811 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45585 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >10000 8 37.00 C Curated from the literature by BindingDB 10.1021/jm800079s 10.7270/Q2W957H9 18370373 aid1798524 Jones, P; Altamura, S; De Francesco, R; Paz, OG; Kinzel, O; Mesiti, G; Monteagudo, E; Pescatore, G; Rowley, M; Verdirame, M; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45586 Nc1ccccc1NC(=O)c1ccc(CNC(=O)OCc2cccnc2)cc1 InChI=1S/C21H20N4O3/c22-18-5-1-2-6-19(18)25-20(26)17-9-7-15(8-10-17)13-24-21(27)28-14-16-4-3-11-23-12-16/h1-12H,13-14,22H2,(H,24,27)(H,25,26) INVTYAOGFAGBOE-UHFFFAOYSA-N 19410 CHEMBL27759::MS-275::US11377423, MS-275::US11672788, Compound Entinostat::US9265734, MS-275::US9796664, Compound MS-275::benzamide-type inhibitor, 3::pyridin-3-ylmethyl N-({4-[(2-aminophenyl)carbamoyl]phenyl}methyl)carbamate Histone deacetylase 4 Homo sapiens >10000 8 37.00 C Curated from the literature by BindingDB 10.1021/jm800079s 10.7270/Q2W957H9 18370373 aid1798524 Jones, P; Altamura, S; De Francesco, R; Paz, OG; Kinzel, O; Mesiti, G; Monteagudo, E; Pescatore, G; Rowley, M; Verdirame, M; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19410 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19410&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4261 46519433 CHEMBL27759 7007 ZINC01488870 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45587 COc1ccc2[nH]c(C)c(CC(=O)N[C@@H](CCCCCC(C)=O)c3nc(c[nH]3)-c3ccccc3)c2c1 InChI=1S/C29H34N4O3/c1-19(34)10-6-4-9-13-26(29-30-18-27(33-29)21-11-7-5-8-12-21)32-28(35)17-23-20(2)31-25-15-14-22(36-3)16-24(23)25/h5,7-8,11-12,14-16,18,26,31H,4,6,9-10,13,17H2,1-3H3,(H,30,33)(H,32,35)/t26-/m0/s1 DBOGSXSBFWKDRX-SANMLTNESA-N 25146 2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)octyl]acetamide::4-phenylimidazole, 17::CHEMBL407959 Histone deacetylase 4 Homo sapiens >10000 8 37.00 C Curated from the literature by BindingDB 10.1021/jm800079s 10.7270/Q2W957H9 18370373 aid1798524 Jones, P; Altamura, S; De Francesco, R; Paz, OG; Kinzel, O; Mesiti, G; Monteagudo, E; Pescatore, G; Rowley, M; Verdirame, M; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25146 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25146&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 24853793 56374287 CHEMBL407959 ZINC29054657 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45588 COc1ccc2[nH]c(C)c(CC(=O)N[C@@H](CCCCCC(C)=O)c3nc4ccc(Cl)cc4[nH]3)c2c1 InChI=1S/C27H31ClN4O3/c1-16(33)7-5-4-6-8-24(27-31-23-11-9-18(28)13-25(23)32-27)30-26(34)15-20-17(2)29-22-12-10-19(35-3)14-21(20)22/h9-14,24,29H,4-8,15H2,1-3H3,(H,30,34)(H,31,32)/t24-/m0/s1 AURHBCXEYHGOLZ-DEOSSOPVSA-N 25147 N-[(1S)-1-(6-chloro-1H-1,3-benzodiazol-2-yl)-7-oxooctyl]-2-(5-methoxy-2-methyl-1H-indol-3-yl)acetamide::benzimidazole analogue, 18 Histone deacetylase 4 Homo sapiens >10000 8 37.00 C Curated from the literature by BindingDB 10.1021/jm800079s 10.7270/Q2W957H9 18370373 aid1798524 Jones, P; Altamura, S; De Francesco, R; Paz, OG; Kinzel, O; Mesiti, G; Monteagudo, E; Pescatore, G; Rowley, M; Verdirame, M; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25147 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25147&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 24853792 56374288 ZINC29054662 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45589 CCC(=O)CCCCC[C@H](NC(=O)Cc1c(C)[nH]c2ccc(OC)cc12)c1nc(c[nH]1)-c1ccccc1 InChI=1S/C30H36N4O3/c1-4-22(35)13-9-6-10-14-27(30-31-19-28(34-30)21-11-7-5-8-12-21)33-29(36)18-24-20(2)32-26-16-15-23(37-3)17-25(24)26/h5,7-8,11-12,15-17,19,27,32H,4,6,9-10,13-14,18H2,1-3H3,(H,31,34)(H,33,36)/t27-/m0/s1 IJGAWXDUIJWLTQ-MHZLTWQESA-N 25148 2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)nonyl]acetamide::4-phenylimidazole, 19 Histone deacetylase 4 Homo sapiens >10000 8 37.00 C Curated from the literature by BindingDB 10.1021/jm800079s 10.7270/Q2W957H9 18370373 aid1798524 Jones, P; Altamura, S; De Francesco, R; Paz, OG; Kinzel, O; Mesiti, G; Monteagudo, E; Pescatore, G; Rowley, M; Verdirame, M; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25148 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25148&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11700059 56374289 ZINC29054529 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45639 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.025 10.7270/Q2RJ4GSK 18308563 aid1798526 Jones, P; Altamura, S; De Francesco, R; Gallinari, P; Lahm, A; Neddermann, P; Rowley, M; Serafini, S; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45640 OCCN(CCc1c[nH]c2ccccc12)Cc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C22H25N3O3/c26-14-13-25(12-11-19-15-23-21-4-2-1-3-20(19)21)16-18-7-5-17(6-8-18)9-10-22(27)24-28/h1-10,15,23,26,28H,11-14,16H2,(H,24,27)/b10-9+ BWDQBBCUWLSASG-MDZDMXLPSA-N 19428 (2E)-N-hydroxy-3-(4-{[(2-hydroxyethyl)[2-(1H-indol-3-yl)ethyl]amino]methyl}phenyl)prop-2-enamide::(E)-N-hydroxy-3-[4-[[2-hydroxyethyl-[2-(1H-indol-3-yl)ethyl]amino]methyl]phenyl]prop-2-enamide::CHEMBL356066::Dacinostat::LAQ-824::NVP-LAQ824 Histone deacetylase 4 Homo sapiens 420 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.025 10.7270/Q2RJ4GSK 18308563 aid1798526 Jones, P; Altamura, S; De Francesco, R; Gallinari, P; Lahm, A; Neddermann, P; Rowley, M; Serafini, S; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19428 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19428&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6445533 46519450 CHEMBL356066 ZINC01494627 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45641 ONC(=O)\C=C\c1cccc(c1)S(=O)(=O)Nc1ccccc1 InChI=1S/C15H14N2O4S/c18-15(16-19)10-9-12-5-4-8-14(11-12)22(20,21)17-13-6-2-1-3-7-13/h1-11,17,19H,(H,16,18)/b10-9+ NCNRHFGMJRPRSK-MDZDMXLPSA-N 25150 (2E)-N-hydroxy-3-[3-(phenylsulfamoyl)phenyl]prop-2-enamide::Belinosta::Belinostat::PXD-101::PXD101 Histone deacetylase 4 Homo sapiens 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.025 10.7270/Q2RJ4GSK 18308563 aid1798526 Jones, P; Altamura, S; De Francesco, R; Gallinari, P; Lahm, A; Neddermann, P; Rowley, M; Serafini, S; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25150 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25150&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5OG 5EEN 6918638 56374291 61076 ZINC03818726 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45642 Nc1ccccc1NC(=O)c1ccc(CNC(=O)OCc2cccnc2)cc1 InChI=1S/C21H20N4O3/c22-18-5-1-2-6-19(18)25-20(26)17-9-7-15(8-10-17)13-24-21(27)28-14-16-4-3-11-23-12-16/h1-12H,13-14,22H2,(H,24,27)(H,25,26) INVTYAOGFAGBOE-UHFFFAOYSA-N 19410 CHEMBL27759::MS-275::US11377423, MS-275::US11672788, Compound Entinostat::US9265734, MS-275::US9796664, Compound MS-275::benzamide-type inhibitor, 3::pyridin-3-ylmethyl N-({4-[(2-aminophenyl)carbamoyl]phenyl}methyl)carbamate Histone deacetylase 4 Homo sapiens 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.025 10.7270/Q2RJ4GSK 18308563 aid1798526 Jones, P; Altamura, S; De Francesco, R; Gallinari, P; Lahm, A; Neddermann, P; Rowley, M; Serafini, S; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19410 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19410&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4261 46519433 CHEMBL27759 7007 ZINC01488870 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45643 Nc1ccccc1NC(=O)c1ccc(CNc2nccc(n2)-c2cccnc2)cc1 InChI=1S/C23H20N6O/c24-19-5-1-2-6-21(19)28-22(30)17-9-7-16(8-10-17)14-27-23-26-13-11-20(29-23)18-4-3-12-25-15-18/h1-13,15H,14,24H2,(H,28,30)(H,26,27,29) HRNLUBSXIHFDHP-UHFFFAOYSA-N 24624 CHEMBL272980::MGCD-0103::MGCD0103::N-(2-aminophenyl)-4-({[4-(pyridin-3-yl)pyrimidin-2-yl]amino}methyl)benzamide::US10227295, Compound MGCD0103::US11377423, MGCD-0103::US9409858, MGCD0103::US9751832, MGCD0103::US9956192, Compound MGCD0103 Histone deacetylase 4 Homo sapiens 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.025 10.7270/Q2RJ4GSK 18308563 aid1798526 Jones, P; Altamura, S; De Francesco, R; Gallinari, P; Lahm, A; Neddermann, P; Rowley, M; Serafini, S; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=24624 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=24624&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 9865515 56269575 CHEMBL272980 7008 ZINC13986811 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45644 CCC(C)[C@@H]1NC(=O)[C@H](Cc2cn(OC)c3ccccc23)NC(=O)[C@H](CCCCCC(=O)CC)NC(=O)[C@H]2CCCCN2C1=O InChI=1S/C34H49N5O6/c1-5-22(3)30-34(44)38-19-13-12-18-29(38)33(43)35-26(16-9-7-8-14-24(40)6-2)31(41)36-27(32(42)37-30)20-23-21-39(45-4)28-17-11-10-15-25(23)28/h10-11,15,17,21-22,26-27,29-30H,5-9,12-14,16,18-20H2,1-4H3,(H,35,43)(H,36,41)(H,37,42)/t22?,26-,27-,29+,30-/m0/s1 JWOGUUIOCYMBPV-LQJYRIKDSA-N 25142 (3S,6S,9S,15aR)-9-[(2R)-butan-2-yl]-6-[(1-methoxy-1H-indol-3-yl)methyl]-3-(6-oxooctyl)-tetradecahydro-1H-pyrido[1,2-a][,,,]cyclododecane-1,4,7,10-tetrone::Apicidin Histone deacetylase 4 Homo sapiens 8700 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.025 10.7270/Q2RJ4GSK 18308563 aid1798526 Jones, P; Altamura, S; De Francesco, R; Gallinari, P; Lahm, A; Neddermann, P; Rowley, M; Serafini, S; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25142 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25142&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 467801 56374284 ZINC36338664 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45645 FC(F)(F)C(=O)CCCCCCC(=O)Nc1cccc(c1)-c1ccccc1 InChI=1S/C21H22F3NO2/c22-21(23,24)19(26)13-6-1-2-7-14-20(27)25-18-12-8-11-17(15-18)16-9-4-3-5-10-16/h3-5,8-12,15H,1-2,6-7,13-14H2,(H,25,27) MURSHQSEWWUKLX-UHFFFAOYSA-N 25151 9,9,9-trifluoro-8-oxo-N-(3-phenylphenyl)nonanamide::CHEMBL115011::trifluoromethyl ketone, 11 Histone deacetylase 4 Homo sapiens 33 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.025 10.7270/Q2RJ4GSK 18308563 aid1798526 Jones, P; Altamura, S; De Francesco, R; Gallinari, P; Lahm, A; Neddermann, P; Rowley, M; Serafini, S; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25151 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25151&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023793 56374292 CHEMBL115011 ZINC13860585 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45646 CNC(=O)C(=O)CCCCCCC(=O)Nc1cccc(c1)-c1ccccc1 InChI=1S/C22H26N2O3/c1-23-22(27)20(25)14-7-2-3-8-15-21(26)24-19-13-9-12-18(16-19)17-10-5-4-6-11-17/h4-6,9-13,16H,2-3,7-8,14-15H2,1H3,(H,23,27)(H,24,26) QUTIXALGBQKSDN-UHFFFAOYSA-N 25152 CHEMBL112446::N-methyl-2-oxo-N'-(3-phenylphenyl)nonanediamide::ketoamide, 12 Histone deacetylase 4 Homo sapiens 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.025 10.7270/Q2RJ4GSK 18308563 aid1798526 Jones, P; Altamura, S; De Francesco, R; Gallinari, P; Lahm, A; Neddermann, P; Rowley, M; Serafini, S; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25152 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25152&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023794 56374293 CHEMBL112446 ZINC01553049 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45744 CCOC(=O)c1ccc(s1)C(=O)C(F)(F)F InChI=1S/C9H7F3O3S/c1-2-15-8(14)6-4-3-5(16-6)7(13)9(10,11)12/h3-4H,2H2,1H3 OCKQIBUJPOSIOM-UHFFFAOYSA-N 25153 ethyl 5-(2,2,2-trifluoroacetyl)thiophene-2-carboxylate::thiophene derivative, 1 Histone deacetylase 4 Homo sapiens 320 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25153 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25153&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 24726843 56374294 ZINC02579845 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45745 CCOC(=O)c1ccc(o1)C(=O)C(F)(F)F InChI=1S/C9H7F3O4/c1-2-15-8(14)6-4-3-5(16-6)7(13)9(10,11)12/h3-4H,2H2,1H3 NCAOGPVUVXZUCU-UHFFFAOYSA-N 25154 ethyl 5-(2,2,2-trifluoroacetyl)furan-2-carboxylate::furan derivative, 2 Histone deacetylase 4 Homo sapiens 2500 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25154 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25154&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 24726844 56374295 ZINC02579846 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45746 CCNC(=O)c1ccc(s1)C(=O)C(F)(F)F InChI=1S/C9H8F3NO2S/c1-2-13-8(15)6-4-3-5(16-6)7(14)9(10,11)12/h3-4H,2H2,1H3,(H,13,15) XYMSMXPTPHUKFO-UHFFFAOYSA-N 25155 CHEMBL462146::N-ethyl-5-(2,2,2-trifluoroacetyl)thiophene-2-carboxamide::thiophene derivative, 3a Histone deacetylase 4 Homo sapiens 1700 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25155 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25155&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023795 56374296 CHEMBL462146 ZINC29069849 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45747 FC(F)(F)C(=O)c1ccc(s1)C(=O)NCCc1ccccc1 InChI=1S/C15H12F3NO2S/c16-15(17,18)13(20)11-6-7-12(22-11)14(21)19-9-8-10-4-2-1-3-5-10/h1-7H,8-9H2,(H,19,21) PMRZVQLLYIMFFK-UHFFFAOYSA-N 25156 N-(2-phenylethyl)-5-(2,2,2-trifluoroacetyl)thiophene-2-carboxamide::thiophene derivative, 3b Histone deacetylase 4 Homo sapiens 330 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25156 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25156&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023796 56374297 ZINC29069842 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45748 CN(Cc1ccccc1)C(=O)c1ccc(s1)C(=O)C(F)(F)F InChI=1S/C15H12F3NO2S/c1-19(9-10-5-3-2-4-6-10)14(21)12-8-7-11(22-12)13(20)15(16,17)18/h2-8H,9H2,1H3 CEBFXUYKCDHZEP-UHFFFAOYSA-N 25157 CHEMBL462209::N-benzyl-N-methyl-5-(2,2,2-trifluoroacetyl)thiophene-2-carboxamide::thiophene derivative, 3c Histone deacetylase 4 Homo sapiens 510 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25157 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25157&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023797 56374298 CHEMBL462209 ZINC29069825 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45749 C[C@@H](NC(=O)c1ccc(s1)C(=O)C(F)(F)F)c1ccccc1 InChI=1S/C15H12F3NO2S/c1-9(10-5-3-2-4-6-10)19-14(21)12-8-7-11(22-12)13(20)15(16,17)18/h2-9H,1H3,(H,19,21)/t9-/m1/s1 DPKHRWMGXRDLLO-SECBINFHSA-N 25158 CHEMBL507716::N-[(1R)-1-phenylethyl]-5-(2,2,2-trifluoroacetyl)thiophene-2-carboxamide::thiophene derivative, 3d Histone deacetylase 4 Homo sapiens 76 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25158 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25158&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 15984018 56374299 CHEMBL507716 ZINC29069811 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45750 C[C@H](NC(=O)c1ccc(s1)C(=O)C(F)(F)F)c1ccccc1 InChI=1S/C15H12F3NO2S/c1-9(10-5-3-2-4-6-10)19-14(21)12-8-7-11(22-12)13(20)15(16,17)18/h2-9H,1H3,(H,19,21)/t9-/m0/s1 DPKHRWMGXRDLLO-VIFPVBQESA-N 25159 CHEMBL462208::N-[(1S)-1-phenylethyl]-5-(2,2,2-trifluoroacetyl)thiophene-2-carboxamide::thiophene derivative, 3e Histone deacetylase 4 Homo sapiens 170 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25159 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25159&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023798 56374300 CHEMBL462208 ZINC29069818 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45751 COc1ccc(CNC(=O)c2ccc(s2)C(=O)C(F)(F)F)cc1 InChI=1S/C15H12F3NO3S/c1-22-10-4-2-9(3-5-10)8-19-14(21)12-7-6-11(23-12)13(20)15(16,17)18/h2-7H,8H2,1H3,(H,19,21) KWIVOWDCZJOCGU-UHFFFAOYSA-N 25160 N-[(4-methoxyphenyl)methyl]-5-(2,2,2-trifluoroacetyl)thiophene-2-carboxamide::thiophene derivative, 3f Histone deacetylase 4 Homo sapiens 180 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25160 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25160&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023799 56374301 ZINC29069740 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45752 FC(F)(F)C(=O)c1ccc(s1)C(=O)NCC1CCCCC1 InChI=1S/C14H16F3NO2S/c15-14(16,17)12(19)10-6-7-11(21-10)13(20)18-8-9-4-2-1-3-5-9/h6-7,9H,1-5,8H2,(H,18,20) VLHNZHDVXTZZKS-UHFFFAOYSA-N 25161 N-(cyclohexylmethyl)-5-(2,2,2-trifluoroacetyl)thiophene-2-carboxamide::thiophene derivative, 3g Histone deacetylase 4 Homo sapiens 400 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25161 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25161&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023800 56374302 ZINC29069747 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45753 FC(F)(F)C(=O)c1ccc(s1)C(=O)N1CCc2ccccc12 InChI=1S/C15H10F3NO2S/c16-15(17,18)13(20)11-5-6-12(22-11)14(21)19-8-7-9-3-1-2-4-10(9)19/h1-6H,7-8H2 FPQZFCVFBLEELM-UHFFFAOYSA-N 25162 1-[5-(2,3-dihydro-1H-indol-1-ylcarbonyl)thiophen-2-yl]-2,2,2-trifluoroethan-1-one::CHEMBL525529::thiophene derivative, 3h Histone deacetylase 4 Homo sapiens 130 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25162 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25162&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023801 56374303 CHEMBL525529 ZINC29069755 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45754 CN(Cc1ccc2nccnc2c1)C(=O)c1ccc(s1)C(=O)C(F)(F)F InChI=1S/C17H12F3N3O2S/c1-23(9-10-2-3-11-12(8-10)22-7-6-21-11)16(25)14-5-4-13(26-14)15(24)17(18,19)20/h2-8H,9H2,1H3 RLNCISDDCDFAHS-UHFFFAOYSA-N 25163 CHEMBL497332::N-methyl-N-(quinoxalin-6-ylmethyl)-5-(2,2,2-trifluoroacetyl)thiophene-2-carboxamide::thiophene derivative, 3i Histone deacetylase 4 Homo sapiens 98 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25163 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25163&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 24857909 56374304 CHEMBL497332 ZINC29069764 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45755 FC(F)(F)C(=O)c1ccc(s1)C(=O)N1CCn2c(C1)ncc2-c1ccccc1 InChI=1S/C19H14F3N3O2S/c20-19(21,22)17(26)14-6-7-15(28-14)18(27)24-8-9-25-13(10-23-16(25)11-24)12-4-2-1-3-5-12/h1-7,10H,8-9,11H2 AZTSYZUNKYTXOA-UHFFFAOYSA-N 25164 2,2,2-trifluoro-1-[5-({3-phenyl-5H,6H,7H,8H-imidazo[1,2-a]pyrazin-7-yl}carbonyl)thiophen-2-yl]ethan-1-one::CHEMBL496094::thiophene derivative, 3j Histone deacetylase 4 Homo sapiens 320 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25164 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25164&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023802 56374305 CHEMBL496094 ZINC29069775 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45756 CN(Cc1ccccc1)C(=O)c1ccc(s1)C(O)C(F)(F)F InChI=1S/C15H14F3NO2S/c1-19(9-10-5-3-2-4-6-10)14(21)12-8-7-11(22-12)13(20)15(16,17)18/h2-8,13,20H,9H2,1H3 KHJHLUOUXKNRGE-UHFFFAOYSA-N 25165 N-benzyl-N-methyl-5-(2,2,2-trifluoro-1-hydroxyethyl)thiophene-2-carboxamide::thiophene derivative, 4c Histone deacetylase 4 Homo sapiens 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25165 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25165&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023803 56374306 ZINC29069792 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45757 FC(F)(F)C1(OCCO1)c1ccc(s1)C(=O)N1CCc2ccccc12 InChI=1S/C17H14F3NO3S/c18-17(19,20)16(23-9-10-24-16)14-6-5-13(25-14)15(22)21-8-7-11-3-1-2-4-12(11)21/h1-6H,7-10H2 MVRGRHBHMYHWRI-UHFFFAOYSA-N 25166 1-({5-[2-(trifluoromethyl)-1,3-dioxolan-2-yl]thiophen-2-yl}carbonyl)-2,3-dihydro-1H-indole::thiophene derivative, 5h Histone deacetylase 4 Homo sapiens 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25166 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25166&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023804 56374307 ZINC29069809 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45758 CN(Cc1ccc2nccnc2c1)C(=O)c1ccc(s1)C(O)=O InChI=1S/C16H13N3O3S/c1-19(15(20)13-4-5-14(23-13)16(21)22)9-10-2-3-11-12(8-10)18-7-6-17-11/h2-8H,9H2,1H3,(H,21,22) UTPQOIZMFVCIGX-UHFFFAOYSA-N 25167 5-[methyl(quinoxalin-6-ylmethyl)carbamoyl]thiophene-2-carboxylic acid::thiophene derivative, 7i Histone deacetylase 4 Homo sapiens 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25167 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25167&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023805 56374308 ZINC29069820 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45759 C[C@@H](NC(=O)c1ccc(s1)C(=O)NO)c1ccccc1 InChI=1S/C14H14N2O3S/c1-9(10-5-3-2-4-6-10)15-13(17)11-7-8-12(20-11)14(18)16-19/h2-9,19H,1H3,(H,15,17)(H,16,18)/t9-/m1/s1 BOZZDVHKSLWIQS-SECBINFHSA-N 25168 2-N-hydroxy-5-N-[(1R)-1-phenylethyl]thiophene-2,5-dicarboxamide::thiophene derivative, 8d Histone deacetylase 4 Homo sapiens 2700 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25168 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25168&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 10017099 56374309 ZINC29069718 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45760 C[C@@H](NC(=O)c1ccc(s1)C(C)=O)c1ccccc1 InChI=1S/C15H15NO2S/c1-10(12-6-4-3-5-7-12)16-15(18)14-9-8-13(19-14)11(2)17/h3-10H,1-2H3,(H,16,18)/t10-/m1/s1 PDTFAKXRWJUBFC-SNVBAGLBSA-N 25169 5-acetyl-N-[(1R)-1-phenylethyl]thiophene-2-carboxamide::thiophene derivative, 10d Histone deacetylase 4 Homo sapiens 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25169 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25169&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 8866284 56374310 ZINC07751153 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45761 COc1ccc(CNC(=O)c2ccc(s2)C(=O)C(F)(F)C(F)(F)F)cc1 InChI=1S/C16H12F5NO3S/c1-25-10-4-2-9(3-5-10)8-22-14(24)12-7-6-11(26-12)13(23)15(17,18)16(19,20)21/h2-7H,8H2,1H3,(H,22,24) XOEOCUIIYZMEPG-UHFFFAOYSA-N 25170 N-[(4-methoxyphenyl)methyl]-5-(2,2,3,3,3-pentafluoropropanoyl)thiophene-2-carboxamide::thiophene derivative, 11f Histone deacetylase 4 Homo sapiens 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25170 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25170&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023806 56374311 ZINC29069642 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45762 OP(O)(=O)c1ccc(s1)C(=O)N1CCc2ccccc12 InChI=1S/C13H12NO4PS/c15-13(11-5-6-12(20-11)19(16,17)18)14-8-7-9-3-1-2-4-10(9)14/h1-6H,7-8H2,(H2,16,17,18) HQFDDDYEACOCEP-UHFFFAOYSA-N 25171 5-(2,3-dihydro-1H-indol-1-ylcarbonyl)thiophene-2-phosphonic acid::thiophene derivative, 14h Histone deacetylase 4 Homo sapiens 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25171 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25171&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023807 56374312 ZINC29069573 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45763 FC(F)C(=O)c1ccc(s1)C(=O)N1CCc2ccccc12 InChI=1S/C15H11F2NO2S/c16-14(17)13(19)11-5-6-12(21-11)15(20)18-8-7-9-3-1-2-4-10(9)18/h1-6,14H,7-8H2 WZGNPOPOCGTSMZ-UHFFFAOYSA-N 25172 1-[5-(2,3-dihydro-1H-indol-1-ylcarbonyl)thiophen-2-yl]-2,2-difluoroethan-1-one::thiophene derivative, 15h Histone deacetylase 4 Homo sapiens 7600 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25172 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25172&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023808 56374313 ZINC29069581 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45764 OB(O)C(=O)c1ccc(s1)C(=O)N1CCc2ccccc12 InChI=1S/C14H12BNO4S/c17-13(15(19)20)11-5-6-12(21-11)14(18)16-8-7-9-3-1-2-4-10(9)16/h1-6,19-20H,7-8H2 AEMKXZKAFWAYEI-UHFFFAOYSA-N 25173 [5-(2,3-dihydro-1H-indol-1-ylcarbonyl)thiophen-2-yl](dihydroxyboranyl)methanone::thiophene derivative, 16h Histone deacetylase 4 Homo sapiens 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25173 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25173&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023809 56374314 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45765 CS(=O)(=O)c1ccc(s1)C(=O)N1CCc2ccccc12 InChI=1S/C14H13NO3S2/c1-20(17,18)13-7-6-12(19-13)14(16)15-9-8-10-4-2-3-5-11(10)15/h2-7H,8-9H2,1H3 TXURGPYCGHPNBT-UHFFFAOYSA-N 25174 1-[(5-methanesulfonylthiophen-2-yl)carbonyl]-2,3-dihydro-1H-indole::thiophene derivative, 17h Histone deacetylase 4 Homo sapiens 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25174 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25174&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023810 56374315 ZINC29069565 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45766 CN(Cc1ccc(s1)C(=O)C(F)(F)F)Cc1ccccc1 InChI=1S/C15H14F3NOS/c1-19(9-11-5-3-2-4-6-11)10-12-7-8-13(21-12)14(20)15(16,17)18/h2-8H,9-10H2,1H3 WIKJTMAEMSPOBF-UHFFFAOYSA-N 25175 1-(5-{[benzyl(methyl)amino]methyl}thiophen-2-yl)-2,2,2-trifluoroethan-1-one::thiophene derivative, 19c Histone deacetylase 4 Homo sapiens 970 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25175 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25175&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023811 56374316 ZINC29069603 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45767 C[C@@H](NCc1ccc(s1)C(=O)C(F)(F)F)c1ccccc1 InChI=1S/C15H14F3NOS/c1-10(11-5-3-2-4-6-11)19-9-12-7-8-13(21-12)14(20)15(16,17)18/h2-8,10,19H,9H2,1H3/t10-/m1/s1 MSNGIONWKLINQX-SNVBAGLBSA-N 25176 2,2,2-trifluoro-1-[5-({[(1R)-1-phenylethyl]amino}methyl)thiophen-2-yl]ethan-1-one::thiophene derivative, 19d Histone deacetylase 4 Homo sapiens 3700 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25176 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25176&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023812 56374317 ZINC29069612 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45768 COc1ccc(COCc2ccc(s2)C(=O)C(F)(F)F)cc1 InChI=1S/C15H13F3O3S/c1-20-11-4-2-10(3-5-11)8-21-9-12-6-7-13(22-12)14(19)15(16,17)18/h2-7H,8-9H2,1H3 MOFRXFLSGOVYKC-UHFFFAOYSA-N 25177 2,2,2-trifluoro-1-(5-{[(4-methoxyphenyl)methoxy]methyl}thiophen-2-yl)ethan-1-one::thiophene derivative, 21f Histone deacetylase 4 Homo sapiens 5500 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25177 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25177&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023813 56374318 ZINC29069589 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45769 CN(Cc1ccccc1)S(=O)(=O)c1csc(c1)C(=O)C(F)(F)F InChI=1S/C14H12F3NO3S2/c1-18(8-10-5-3-2-4-6-10)23(20,21)11-7-12(22-9-11)13(19)14(15,16)17/h2-7,9H,8H2,1H3 UMWZEUPYBZJRSL-UHFFFAOYSA-N 25178 N-benzyl-N-methyl-5-(2,2,2-trifluoroacetyl)thiophene-3-sulfonamide::thiophene derivative, 23c Histone deacetylase 4 Homo sapiens 9400 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25178 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25178&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023814 56374319 ZINC29069596 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45770 CN(Cc1ccccc1)S(=O)(=O)c1ccc(s1)C(=O)C(F)(F)F InChI=1S/C14H12F3NO3S2/c1-18(9-10-5-3-2-4-6-10)23(20,21)12-8-7-11(22-12)13(19)14(15,16)17/h2-8H,9H2,1H3 QMDPGLMZJJTIKT-UHFFFAOYSA-N 25179 N-benzyl-N-methyl-5-(2,2,2-trifluoroacetyl)thiophene-2-sulfonamide::thiophene derivative, 25c Histone deacetylase 4 Homo sapiens 340 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25179 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25179&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023815 56374320 ZINC29069556 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45771 CN(Cc1ccccc1)C(=O)c1cc(cs1)C(=O)C(F)(F)F InChI=1S/C15H12F3NO2S/c1-19(8-10-5-3-2-4-6-10)14(21)12-7-11(9-22-12)13(20)15(16,17)18/h2-7,9H,8H2,1H3 WRODGKNMXQYIQO-UHFFFAOYSA-N 25180 N-benzyl-N-methyl-4-(2,2,2-trifluoroacetyl)thiophene-2-carboxamide::thiophene derivative, 27c Histone deacetylase 4 Homo sapiens 1700 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25180 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25180&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023816 56374321 ZINC29070047 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45772 FC(F)(F)C(=O)c1csc(c1)C(=O)NCC1CCCCC1 InChI=1S/C14H16F3NO2S/c15-14(16,17)12(19)10-6-11(21-8-10)13(20)18-7-9-4-2-1-3-5-9/h6,8-9H,1-5,7H2,(H,18,20) BBSBLQQJLHVBBD-UHFFFAOYSA-N 25181 N-(cyclohexylmethyl)-4-(2,2,2-trifluoroacetyl)thiophene-2-carboxamide::thiophene derivative, 27g Histone deacetylase 4 Homo sapiens 3300 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25181 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25181&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023817 56374322 ZINC29070057 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45773 CN(Cc1ccccc1)C(=O)c1cnc(s1)C(=O)C(F)(F)F InChI=1S/C14H11F3N2O2S/c1-19(8-9-5-3-2-4-6-9)13(21)10-7-18-12(22-10)11(20)14(15,16)17/h2-7H,8H2,1H3 DBRXECPLYPTYJF-UHFFFAOYSA-N 25182 N-benzyl-N-methyl-2-(2,2,2-trifluoroacetyl)-1,3-thiazole-5-carboxamide::thiazole derivative, 29c Histone deacetylase 4 Homo sapiens 760 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25182 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25182&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023818 56374323 ZINC29070015 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45824 FC(F)(F)C(=O)c1ncc(s1)C(=O)NCC1CCCCC1 InChI=1S/C13H15F3N2O2S/c14-13(15,16)10(19)12-18-7-9(21-12)11(20)17-6-8-4-2-1-3-5-8/h7-8H,1-6H2,(H,17,20) ZOPFCMCXTRDDOT-UHFFFAOYSA-N 25183 N-(cyclohexylmethyl)-2-(2,2,2-trifluoroacetyl)-1,3-thiazole-5-carboxamide::thiazole derivative, 29g Histone deacetylase 4 Homo sapiens 850 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25183 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25183&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023819 56374324 ZINC29070024 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45825 FC(F)(F)C(=O)c1ccc([nH]1)C(=O)N1CCc2ccccc12 InChI=1S/C15H11F3N2O2/c16-15(17,18)13(21)10-5-6-11(19-10)14(22)20-8-7-9-3-1-2-4-12(9)20/h1-6,19H,7-8H2 SHCFLTDJDAJUCC-UHFFFAOYSA-N 25184 1-[5-(2,3-dihydro-1H-indol-1-ylcarbonyl)-1H-pyrrol-2-yl]-2,2,2-trifluoroethan-1-one::CHEMBL493784::pyrrole derivative, 31h Histone deacetylase 4 Homo sapiens 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25184 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25184&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023820 56374325 CHEMBL493784 ZINC29070029 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45826 FC(F)(F)C(=O)c1cccc(c1)C(=O)NCC1CCCCC1 InChI=1S/C16H18F3NO2/c17-16(18,19)14(21)12-7-4-8-13(9-12)15(22)20-10-11-5-2-1-3-6-11/h4,7-9,11H,1-3,5-6,10H2,(H,20,22) OFHDOSVGGCZRGV-UHFFFAOYSA-N 25185 N-(cyclohexylmethyl)-3-(2,2,2-trifluoroacetyl)benzamide::phenyl analogue, 34g Histone deacetylase 4 Homo sapiens 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25185 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25185&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023821 56374326 ZINC53182500 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45827 FC(F)(F)C(=O)c1ccc(cc1)C(=O)NCC1CCCCC1 InChI=1S/C16H18F3NO2/c17-16(18,19)14(21)12-6-8-13(9-7-12)15(22)20-10-11-4-2-1-3-5-11/h6-9,11H,1-5,10H2,(H,20,22) JJGHOMRZTGDXDD-UHFFFAOYSA-N 25186 CHEMBL248486::N-(cyclohexylmethyl)-4-(2,2,2-trifluoroacetyl)benzamide::phenyl analogue, 35g Histone deacetylase 4 Homo sapiens 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25186 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25186&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023822 56374327 CHEMBL248486 ZINC28880454 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 45828 NC(=O)c1ccc(cn1)C(=O)C(F)(F)F InChI=1S/C8H5F3N2O2/c9-8(10,11)6(14)4-1-2-5(7(12)15)13-3-4/h1-3H,(H2,12,15) YPVSHEOWKRJZHJ-UHFFFAOYSA-N 25187 5-(2,2,2-trifluoroacetyl)pyridine-2-carboxamide::pyridyl analogue, 37 Histone deacetylase 4 Homo sapiens 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2008.02.026 10.7270/Q2MS3R28 18440229 aid1798529 Jones, P; Bottomley, MJ; Carfí, A; Cecchetti, O; Ferrigno, F; Lo Surdo, P; Ontoria, JM; Rowley, M; Scarpelli, R; Schultz-Fademrecht, C; Steinkühler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25187 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25187&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023823 56374328 ZINC29070009 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 64362 CC(C)C[C@H](NC(C)=O)C(=O)NCC(=O)N[C@@H](CCCCNC(C)=O)C(=O)Nc1ccc2c(C)cc(=O)oc2c1 InChI=1S/C28H39N5O7/c1-16(2)12-23(31-19(5)35)27(38)30-15-25(36)33-22(8-6-7-11-29-18(4)34)28(39)32-20-9-10-21-17(3)13-26(37)40-24(21)14-20/h9-10,13-14,16,22-23H,6-8,11-12,15H2,1-5H3,(H,29,34)(H,30,38)(H,31,35)(H,32,39)(H,33,36)/t22-,23-/m0/s1 YLJRILGAXBHXDZ-GOTSBHOMSA-N 36483 (S)-6-acetamido-2-(2-((S)-2-acetamido-4-methylpentanamido)acetamido)-N-(4-methyl-2-oxo-2H-chromen-7-yl)hexanamide, 3::CID10460379 Histone deacetylase 4 Homo sapiens 1181 7.4 0.00 C Curated from the literature by BindingDB 10.1038/nchembio.313 10.7270/Q2C53J66 20139990 aid1799411 Bradner, JE; West, N; Grachan, ML; Greenberg, EF; Haggarty, SJ; Warnow, T; Mazitschek, R Dana-Farber Cancer Institute Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=36483 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=36483&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 10460379 117644069 C04149 ZINC49877706 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 64366 CC(=O)NCCCC[C@H](NC(=O)OCc1ccccc1)C(=O)Nc1ccc2c(C)cc(=O)oc2c1 InChI=1S/C26H29N3O6/c1-17-14-24(31)35-23-15-20(11-12-21(17)23)28-25(32)22(10-6-7-13-27-18(2)30)29-26(33)34-16-19-8-4-3-5-9-19/h3-5,8-9,11-12,14-15,22H,6-7,10,13,16H2,1-2H3,(H,27,30)(H,28,32)(H,29,33)/t22-/m0/s1 QPYCOBUGIVWEDU-QFIPXVFZSA-N 36484 (S)-Benzyl (6-acetamido-1-((4-methyl-2-oxo-2H-chromen-7-yl)amino)-1-oxohexan-2-yl)carbamate, 21::CID10435243 Histone deacetylase 4 Homo sapiens 642.7 7.4 0.00 C Curated from the literature by BindingDB 10.1038/nchembio.313 10.7270/Q2C53J66 20139990 aid1799411 Bradner, JE; West, N; Grachan, ML; Greenberg, EF; Haggarty, SJ; Warnow, T; Mazitschek, R Dana-Farber Cancer Institute Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=36484 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=36484&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 10435243 117644070 C04149 ZINC49771967 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 858330 Cc1cc(O)cc(C)c1-c1nc2ccc(cc2[nH]1)C(=O)NO InChI=1S/C16H15N3O3/c1-8-5-11(20)6-9(2)14(8)15-17-12-4-3-10(16(21)19-22)7-13(12)18-15/h3-7,20,22H,1-2H3,(H,17,18)(H,19,21) IHHFWSWKTPUOTJ-UHFFFAOYSA-N 425853 N-hydroxy-2-(4-hydroxy-2,6- dimethylphenyl)-1H- benzimidazole-6-carboxamide::US10512634, Example 15 Histone deacetylase 4 Homo sapiens >10000 US Patent 10.7270/Q2WD42ZQ aid1804071 US10512634 Schultz, J; Vagberg, J; Olsson, E; Farnegardh, K; Jonsson, M; Hammer, K; Kruger, L KANCERA AB http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=425853 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=425853&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137097970 434320205 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 246710 ONC(=O)c1ccc(CNC(=O)c2[nH]c(cc2-c2ccsc2)-c2ccc(O)cc2)cc1 InChI=1S/C28H27N3O3S/c1-34-23-13-11-20(12-14-23)24-17-25(21-5-3-2-4-6-21)31-26(24)28(33)30-18-19-7-9-22(10-8-19)27(32)29-15-16-35/h2-14,17,31,35H,15-16,18H2,1H3,(H,29,32)(H,30,33) BUXPYIKGVMPYJG-UHFFFAOYSA-N 119695 US8685992, 14 Histone deacetylase 4 Homo sapiens 956 30.00 C US Patent 10.7270/Q2CJ8C4X aid1800395 US8685992 Cossio Mora, FP; Zubia Olascoaga, A; Vara Salazar, Y; San Sebastian Larzabal, EI; Otaegui Ansa, D; Masdeu Margalef, M; Aldaba Arevalo, E Universidad del País Vasco http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=119695 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=119695&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 51038885 220230491 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 246711 ONC(=O)c1ccc(CNC(=O)c2[nH]c(cc2-c2ccoc2)-c2ccc(O)cc2)cc1 InChI=1S/C23H19N3O5/c27-18-7-5-15(6-8-18)20-11-19(17-9-10-31-13-17)21(25-20)23(29)24-12-14-1-3-16(4-2-14)22(28)26-30/h1-11,13,25,27,30H,12H2,(H,24,29)(H,26,28) OUFJXJJAONPLLU-UHFFFAOYSA-N 119440 BDBM119696::US8685986, 15 Histone deacetylase 4 Homo sapiens 338 30.00 C US Patent 10.7270/Q2CJ8C4X aid1800395 US8685992 Cossio Mora, FP; Zubia Olascoaga, A; Vara Salazar, Y; San Sebastian Larzabal, EI; Otaegui Ansa, D; Masdeu Margalef, M; Aldaba Arevalo, E Universidad del País Vasco http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=119440 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=119440&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 84973025 220230253 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 246712 COc1ccc(cc1)-c1cc(-c2ccoc2)c([nH]1)C(=O)NCc1ccc(cc1)C(=O)NO InChI=1S/C29H24N4O3S/c30-24-3-1-2-4-25(24)33-28(35)20-7-5-18(6-8-20)16-31-29(36)27-23(19-9-11-22(34)12-10-19)15-26(32-27)21-13-14-37-17-21/h1-15,17,32,34H,16,30H2,(H,31,36)(H,33,35) SEYQQVKFMOLZCN-UHFFFAOYSA-N 119703 US8685992, 27 Histone deacetylase 4 Homo sapiens 1083 30.00 C US Patent 10.7270/Q2CJ8C4X aid1800395 US8685992 Cossio Mora, FP; Zubia Olascoaga, A; Vara Salazar, Y; San Sebastian Larzabal, EI; Otaegui Ansa, D; Masdeu Margalef, M; Aldaba Arevalo, E Universidad del País Vasco http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=119703 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=119703&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 67082776 220230497 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 246713 COc1ccc(cc1)-c1cc(-c2ccsc2)c([nH]1)C(=O)NCc1ccc(cc1)C(=O)NO InChI=1S/C29H24N4O4/c30-24-3-1-2-4-25(24)33-28(35)20-7-5-18(6-8-20)16-31-29(36)27-23(21-13-14-37-17-21)15-26(32-27)19-9-11-22(34)12-10-19/h1-15,17,32,34H,16,30H2,(H,31,36)(H,33,35) RZUFVMUYNQBONC-UHFFFAOYSA-N 119704 US8685992, 28 Histone deacetylase 4 Homo sapiens 2431 30.00 C US Patent 10.7270/Q2CJ8C4X aid1800395 US8685992 Cossio Mora, FP; Zubia Olascoaga, A; Vara Salazar, Y; San Sebastian Larzabal, EI; Otaegui Ansa, D; Masdeu Margalef, M; Aldaba Arevalo, E Universidad del País Vasco http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=119704 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=119704&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 67082695 220230498 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 246714 Nc1ccccc1NC(=O)c1ccc(CNC(=O)c2[nH]c(cc2-c2ccoc2)-c2ccc(O)cc2)cc1 InChI=1S/C24H19FN4O3/c25-19-9-7-16(8-10-19)20-12-21(18-2-1-11-26-14-18)28-22(20)24(31)27-13-15-3-5-17(6-4-15)23(30)29-32/h1-12,14,28,32H,13H2,(H,27,31)(H,29,30) NCZPVKGOUNBDSF-UHFFFAOYSA-N 119709 US8685992, 37 Histone deacetylase 4 Homo sapiens >5000 30.00 C US Patent 10.7270/Q2CJ8C4X aid1800395 US8685992 Cossio Mora, FP; Zubia Olascoaga, A; Vara Salazar, Y; San Sebastian Larzabal, EI; Otaegui Ansa, D; Masdeu Margalef, M; Aldaba Arevalo, E Universidad del País Vasco http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=119709 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=119709&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 88850562 220230503 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 253335 CN1CCc2c(C1)c1ccccc1n2Cc1ccc(cc1)C(=O)NO InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::Tubastatin A::US10227295, Compound Tubastatin A::US10456394, Tubastatin A::US11207431, Example D::US8748451, 6::US9249087, Tubacin::US9751832, Tubastatin A::US9956192, Compound Tubastatin-A Histone deacetylase 4 Homo sapiens >30000 8 25.00 C US Patent 10.7270/Q26D5RPK aid1800512 US8748451 Kozikowski, A; Butler, KV; Kalin, JH University of Illinois http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 ZINC51951670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 253359 ONC(=O)CCCCCCN(c1ccccn1)c1ccccn1 InChI=1S/C17H22N4O2/c22-17(20-23)11-3-1-2-8-14-21(15-9-4-6-12-18-15)16-10-5-7-13-19-16/h4-7,9-10,12-13,23H,1-3,8,11,14H2,(H,20,22) QKTORDWLHYWRJF-UHFFFAOYSA-N 124199 US8748458, 3 Histone deacetylase 4 Homo sapiens 307 37.00 C US Patent 10.7270/Q22N50Z7 aid1800513 US8748458 Shuttleworth, SJ; Tomassi, CD Karus Therapeutics Limited http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=124199 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=124199&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 46852450 225150591 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 253365 ONC(=O)CCCCCCN(c1ccccn1)c1ccc2ccccc2n1 InChI=1S/C21H24N4O2/c26-21(24-27)12-3-1-2-8-16-25(19-11-6-7-15-22-19)20-14-13-17-9-4-5-10-18(17)23-20/h4-7,9-11,13-15,27H,1-3,8,12,16H2,(H,24,26) JMWOJCWEYBYEOY-UHFFFAOYSA-N 124200 US8748458, 4 Histone deacetylase 4 Homo sapiens 545 37.00 C US Patent 10.7270/Q22N50Z7 aid1800513 US8748458 Shuttleworth, SJ; Tomassi, CD Karus Therapeutics Limited http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=124200 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=124200&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 46843052 225150592 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 293070 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 340 Curated from the literature by BindingDB 10.1016/j.bioorg.2015.02.009 10.7270/Q2T152C2 25797804 aid1801045 Shahidul Islam, M; Nurul Islam, M; Ashraful Hoque, M; Nishino, N; Kato, T; Kim, HJ; Ito, A; Yoshida, M Kyushu Institute of Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 293071 ONC(=O)CCCCC[C@H](NC(=O)OCc1ccccc1)C(=O)Nc1cccc2cccnc12 InChI=1S/C25H28N4O5/c30-22(29-33)15-6-2-5-13-21(28-25(32)34-17-18-9-3-1-4-10-18)24(31)27-20-14-7-11-19-12-8-16-26-23(19)20/h1,3-4,7-12,14,16,21,33H,2,5-6,13,15,17H2,(H,27,31)(H,28,32)(H,29,30)/t21-/m0/s1 UEGKDJGASMFKBQ-NRFANRHFSA-N 50200895 (S)-benzyl 8-(hydroxyamino)-1,8-dioxo-1-(quinolin-8-ylamino)octan-2-ylcarbamate::CHEMBL221955 Histone deacetylase 4 Homo sapiens 11 Curated from the literature by BindingDB 10.1016/j.bioorg.2015.02.009 10.7270/Q2T152C2 25797804 aid1801045 Shahidul Islam, M; Nurul Islam, M; Ashraful Hoque, M; Nishino, N; Kato, T; Kim, HJ; Ito, A; Yoshida, M Kyushu Institute of Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50200895 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50200895&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 9956086 104080932 CHEMBL221955 ZINC27087290 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 293072 CC(=O)SCCCCC[C@H](NC(=O)OCc1ccccc1)C(=O)Nc1cccc2cccnc12 InChI=1S/C26H29N3O4S/c1-19(30)34-17-7-3-6-14-23(29-26(32)33-18-20-10-4-2-5-11-20)25(31)28-22-15-8-12-21-13-9-16-27-24(21)22/h2,4-5,8-13,15-16,23H,3,6-7,14,17-18H2,1H3,(H,28,31)(H,29,32)/t23-/m0/s1 UJKGYYPNUCRQFO-QHCPKHFHSA-N 152479 Z-L-Am7(Ac)-QA (1) Histone deacetylase 4 Homo sapiens 18 Curated from the literature by BindingDB 10.1016/j.bioorg.2015.02.009 10.7270/Q2T152C2 25797804 aid1801045 Shahidul Islam, M; Nurul Islam, M; Ashraful Hoque, M; Nishino, N; Kato, T; Kim, HJ; Ito, A; Yoshida, M Kyushu Institute of Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=152479 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=152479&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91937716 252826730 C04334 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 293073 COCCOCC(=O)SCCCCC[C@H](NC(=O)OCc1ccccc1)C(=O)Nc1cccc2cccnc12 InChI=1S/C29H35N3O6S/c1-36-17-18-37-21-26(33)39-19-7-3-6-14-25(32-29(35)38-20-22-10-4-2-5-11-22)28(34)31-24-15-8-12-23-13-9-16-30-27(23)24/h2,4-5,8-13,15-16,25H,3,6-7,14,17-21H2,1H3,(H,31,34)(H,32,35)/t25-/m0/s1 ADSFNXXUDGBABJ-VWLOTQADSA-N 152480 Z-L-Am7(AcEtMe)-QA (2) Histone deacetylase 4 Homo sapiens 18 Curated from the literature by BindingDB 10.1016/j.bioorg.2015.02.009 10.7270/Q2T152C2 25797804 aid1801045 Shahidul Islam, M; Nurul Islam, M; Ashraful Hoque, M; Nishino, N; Kato, T; Kim, HJ; Ito, A; Yoshida, M Kyushu Institute of Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=152480 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=152480&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91937717 252826731 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 293074 OCCSSCCCCC[C@H](NC(=O)OCc1ccccc1)C(=O)Nc1cccc2cccnc12 InChI=1S/C26H31N3O4S2/c30-16-18-35-34-17-6-2-5-13-23(29-26(32)33-19-20-9-3-1-4-10-20)25(31)28-22-14-7-11-21-12-8-15-27-24(21)22/h1,3-4,7-12,14-15,23,30H,2,5-6,13,16-19H2,(H,28,31)(H,29,32)/t23-/m0/s1 OMEMORTXMDILLA-QHCPKHFHSA-N 152481 Z-L-Am7(betaMe)-QA (3) Histone deacetylase 4 Homo sapiens 2.0 Curated from the literature by BindingDB 10.1016/j.bioorg.2015.02.009 10.7270/Q2T152C2 25797804 aid1801045 Shahidul Islam, M; Nurul Islam, M; Ashraful Hoque, M; Nishino, N; Kato, T; Kim, HJ; Ito, A; Yoshida, M Kyushu Institute of Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=152481 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=152481&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91937718 252826732 C15496 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 293075 O=C(NC(CCCCCSSCCCCC[C@H](NC(=O)OCc1ccccc1)C(=O)Nc1cccc2cccnc12)C(=O)Nc1cccc2cccnc12)OCc1ccccc1 InChI=1S/C48H52N6O6S2/c55-45(51-39-27-13-21-37-23-15-29-49-43(37)39)41(53-47(57)59-33-35-17-5-1-6-18-35)25-9-3-11-31-61-62-32-12-4-10-26-42(54-48(58)60-34-36-19-7-2-8-20-36)46(56)52-40-28-14-22-38-24-16-30-50-44(38)40/h1-2,5-8,13-24,27-30,41-42H,3-4,9-12,25-26,31-34H2,(H,51,55)(H,52,56)(H,53,57)(H,54,58)/t41-,42?/m0/s1 XQPDEMOFEZWKBH-DYJLHVNUSA-N 152482 (Z-L-Am7(S-)-QA)2 (4) Histone deacetylase 4 Homo sapiens 3.4 Curated from the literature by BindingDB 10.1016/j.bioorg.2015.02.009 10.7270/Q2T152C2 25797804 aid1801045 Shahidul Islam, M; Nurul Islam, M; Ashraful Hoque, M; Nishino, N; Kato, T; Kim, HJ; Ito, A; Yoshida, M Kyushu Institute of Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=152482 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=152482&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91937719 252826733 C15496 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305675 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1CC1 InChI=1S/C13H10F3N3O2/c14-13(15,16)12-18-10(19-21-12)7-1-3-8(4-2-7)11(20)17-9-5-6-9/h1-4,9H,5-6H2,(H,17,20) YCVWWNLTUACWPI-UHFFFAOYSA-N 162728 US9056843, 19 Histone deacetylase 4 Homo sapiens 120 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801324 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162728 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162728&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230960 310304667 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305676 CN(C)c1ccc(NC(=O)c2ccc(cc2)-c2noc(n2)C(F)(F)F)cc1 InChI=1S/C18H15F3N4O2/c1-25(2)14-9-7-13(8-10-14)22-16(26)12-5-3-11(4-6-12)15-23-17(27-24-15)18(19,20)21/h3-10H,1-2H3,(H,22,26) XIBGMXLIDIRVAM-UHFFFAOYSA-N 162750 US9056843, 41 Histone deacetylase 4 Homo sapiens 1500 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801324 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162750 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162750&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230697 310304689 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305677 Cc1cc(NC(=O)c2ccc(cc2)-c2noc(n2)C(F)(F)F)ccn1 InChI=1S/C16H11F3N4O2/c1-9-8-12(6-7-20-9)21-14(24)11-4-2-10(3-5-11)13-22-15(25-23-13)16(17,18)19/h2-8H,1H3,(H,20,21,24) KNTZPJOJMGCEPU-UHFFFAOYSA-N 162779 US9056843, 70 Histone deacetylase 4 Homo sapiens 90 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801324 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162779 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162779&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230903 310304718 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305678 FC(F)(F)c1nc(no1)-c1ccc(cc1)S(=O)(=O)Nc1cccnc1 InChI=1S/C14H9F3N4O3S/c15-14(16,17)13-19-12(20-24-13)9-3-5-11(6-4-9)25(22,23)21-10-2-1-7-18-8-10/h1-8,21H PYHKYGFZDLEQKV-UHFFFAOYSA-N 162809 US9056843, 100 Histone deacetylase 4 Homo sapiens 70 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801324 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162809 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162809&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230839 310304746 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305679 Fc1cccc(NS(=O)(=O)c2ccc(cc2)-c2noc(n2)C(F)(F)F)c1 InChI=1S/C15H9F4N3O3S/c16-10-2-1-3-11(8-10)22-26(23,24)12-6-4-9(5-7-12)13-20-14(25-21-13)15(17,18)19/h1-8,22H VJECNJFLZGGHEX-UHFFFAOYSA-N 162815 US9056843, 106 Histone deacetylase 4 Homo sapiens 200 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801324 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162815 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162815&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230784 310304752 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305680 CCN(CC)C[C@H](C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C17H21F3N4O2/c1-4-24(5-2)10-11(3)21-15(25)13-8-6-12(7-9-13)14-22-16(26-23-14)17(18,19)20/h6-9,11H,4-5,10H2,1-3H3,(H,21,25)/t11-/m0/s1 BWCIUZLJTVXSMW-NSHDSACASA-N 162842 US9056843, 133 Histone deacetylase 4 Homo sapiens 48 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801324 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162842 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162842&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230717 310304779 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305681 CCN(C)C[C@@H](C)NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C16H18F4N4O2/c1-4-24(3)8-9(2)21-14(25)11-6-5-10(7-12(11)17)13-22-15(26-23-13)16(18,19)20/h5-7,9H,4,8H2,1-3H3,(H,21,25)/t9-/m1/s1 NSBYDCURMKSEIJ-SECBINFHSA-N 162849 US9056843, 140 Histone deacetylase 4 Homo sapiens 72 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801324 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162849 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162849&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230843 310304786 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305682 CN(C)C(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C12H10F3N3O2/c1-18(2)10(19)8-5-3-7(4-6-8)9-16-11(20-17-9)12(13,14)15/h3-6H,1-2H3 HPOCHXQWZPPNBY-UHFFFAOYSA-N 162710 US9056843, 1 Histone deacetylase 4 Homo sapiens 360 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162710 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162710&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230787 310304650 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305683 CNC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C11H8F3N3O2/c1-15-9(18)7-4-2-6(3-5-7)8-16-10(19-17-8)11(12,13)14/h2-5H,1H3,(H,15,18) OUMSNRPZKWUWES-UHFFFAOYSA-N 162711 US9056843, 2 Histone deacetylase 4 Homo sapiens 530 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230945 310304651 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305684 CNC(=O)Cc1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C12H10F3N3O2/c1-16-9(19)6-7-2-4-8(5-3-7)10-17-11(20-18-10)12(13,14)15/h2-5H,6H2,1H3,(H,16,19) HDIGXHQTAVNCES-UHFFFAOYSA-N 162712 US9056843, 3 Histone deacetylase 4 Homo sapiens 1900 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162712 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162712&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230676 310304652 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305685 CN(C)C(=O)Cc1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C13H12F3N3O2/c1-19(2)10(20)7-8-3-5-9(6-4-8)11-17-12(21-18-11)13(14,15)16/h3-6H,7H2,1-2H3 DOZQOPCRFHELFA-UHFFFAOYSA-N 162713 US9056843, 4 Histone deacetylase 4 Homo sapiens 620 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162713 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162713&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230695 310304653 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305686 CC(C)NC(=O)Cc1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C14H14F3N3O2/c1-8(2)18-11(21)7-9-3-5-10(6-4-9)12-19-13(22-20-12)14(15,16)17/h3-6,8H,7H2,1-2H3,(H,18,21) MLBIBJOCXAUCPH-UHFFFAOYSA-N 162714 US9056843, 5 Histone deacetylase 4 Homo sapiens 970 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162714 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162714&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71231064 310304654 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305687 CCCCNC(=O)Cc1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C15H16F3N3O2/c1-2-3-8-19-12(22)9-10-4-6-11(7-5-10)13-20-14(23-21-13)15(16,17)18/h4-7H,2-3,8-9H2,1H3,(H,19,22) FGWWMUDKFJLEEP-UHFFFAOYSA-N 162715 US9056843, 6 Histone deacetylase 4 Homo sapiens 630 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162715 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162715&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230871 310304655 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305688 COCCNC(=O)Cc1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C14H14F3N3O3/c1-22-7-6-18-11(21)8-9-2-4-10(5-3-9)12-19-13(23-20-12)14(15,16)17/h2-5H,6-8H2,1H3,(H,18,21) OLHZABUSLVLNQH-UHFFFAOYSA-N 162716 US9056843, 7 Histone deacetylase 4 Homo sapiens 960 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162716 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162716&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230800 310304656 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305689 CCOC(=O)CNC(=O)Cc1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C15H14F3N3O4/c1-2-24-12(23)8-19-11(22)7-9-3-5-10(6-4-9)13-20-14(25-21-13)15(16,17)18/h3-6H,2,7-8H2,1H3,(H,19,22) ONDBNZKXBIECQO-UHFFFAOYSA-N 162717 US9056843, 8 Histone deacetylase 4 Homo sapiens 580 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162717 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162717&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230780 310304657 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305690 FC(F)(F)c1nc(no1)-c1ccc(CC(=O)N2CCOCC2)cc1 InChI=1S/C15H14F3N3O3/c16-15(17,18)14-19-13(20-24-14)11-3-1-10(2-4-11)9-12(22)21-5-7-23-8-6-21/h1-4H,5-9H2 CFKSFKXROKZYDV-UHFFFAOYSA-N 162718 US9056843, 9 Histone deacetylase 4 Homo sapiens 850 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162718 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162718&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230700 310304658 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305691 CN1CCN(CC1)C(=O)Cc1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C16H17F3N4O2/c1-22-6-8-23(9-7-22)13(24)10-11-2-4-12(5-3-11)14-20-15(25-21-14)16(17,18)19/h2-5H,6-10H2,1H3 FHPYVAJINGPABL-UHFFFAOYSA-N 162719 US9056843, 10 Histone deacetylase 4 Homo sapiens 1300 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162719 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162719&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230803 310304659 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305692 CON(C)C(=O)Cc1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C13H12F3N3O3/c1-19(21-2)10(20)7-8-3-5-9(6-4-8)11-17-12(22-18-11)13(14,15)16/h3-6H,7H2,1-2H3 RHOWMWOUFAJXKQ-UHFFFAOYSA-N 162720 US9056843, 11 Histone deacetylase 4 Homo sapiens 1100 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162720 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162720&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71486775 310304660 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305693 CCNC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C12H10F3N3O2/c1-2-16-10(19)8-5-3-7(4-6-8)9-17-11(20-18-9)12(13,14)15/h3-6H,2H2,1H3,(H,16,19) WWCPMLUISCRKPF-UHFFFAOYSA-N 162721 US9056843, 12 Histone deacetylase 4 Homo sapiens 430 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162721 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162721&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230950 310304661 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305694 OCCNC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C12H10F3N3O3/c13-12(14,15)11-17-9(18-21-11)7-1-3-8(4-2-7)10(20)16-5-6-19/h1-4,19H,5-6H2,(H,16,20) NCMUYLGLYZSHBA-UHFFFAOYSA-N 162722 US9056843, 13::US9056843, 17 Histone deacetylase 4 Homo sapiens 660 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162722 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162722&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230690 310304662 C04080 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305695 CCN(C)C(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C13H12F3N3O2/c1-3-19(2)11(20)9-6-4-8(5-7-9)10-17-12(21-18-10)13(14,15)16/h4-7H,3H2,1-2H3 OWYUDNFHZRLOQM-UHFFFAOYSA-N 162723 US9056843, 14 Histone deacetylase 4 Homo sapiens 900 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162723 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162723&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230884 310304663 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305696 CN(CCO)C(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C13H12F3N3O3/c1-19(6-7-20)11(21)9-4-2-8(3-5-9)10-17-12(22-18-10)13(14,15)16/h2-5,20H,6-7H2,1H3 DUONAKZCSCVNFH-UHFFFAOYSA-N 162724 US9056843, 15 Histone deacetylase 4 Homo sapiens 990 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162724 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162724&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230955 310304664 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305697 COCCNC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C13H12F3N3O3/c1-21-7-6-17-11(20)9-4-2-8(3-5-9)10-18-12(22-19-10)13(14,15)16/h2-5H,6-7H2,1H3,(H,17,20) GUJZIRUOIWKNCQ-UHFFFAOYSA-N 162725 US9056843, 16 Histone deacetylase 4 Homo sapiens 1400 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162725 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162725&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230699 310304665 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305698 OCCNC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C12H10F3N3O3/c13-12(14,15)11-17-9(18-21-11)7-1-3-8(4-2-7)10(20)16-5-6-19/h1-4,19H,5-6H2,(H,16,20) NCMUYLGLYZSHBA-UHFFFAOYSA-N 162722 US9056843, 13::US9056843, 17 Histone deacetylase 4 Homo sapiens 1400 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162722 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162722&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230690 310304662 C04080 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305699 COCCN(C)C(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C14H14F3N3O3/c1-20(7-8-22-2)12(21)10-5-3-9(4-6-10)11-18-13(23-19-11)14(15,16)17/h3-6H,7-8H2,1-2H3 FZARNFAFIAPTIY-UHFFFAOYSA-N 162727 US9056843, 18 Histone deacetylase 4 Homo sapiens 390 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162727 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162727&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230848 310304666 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305700 CC(C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C13H12F3N3O2/c1-7(2)17-11(20)9-5-3-8(4-6-9)10-18-12(21-19-10)13(14,15)16/h3-7H,1-2H3,(H,17,20) YGJGXPWYQMDHLZ-UHFFFAOYSA-N 162729 US9056843, 20 Histone deacetylase 4 Homo sapiens 1000 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162729 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162729&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230959 310304668 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305701 COCCCNC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C14H14F3N3O3/c1-22-8-2-7-18-12(21)10-5-3-9(4-6-10)11-19-13(23-20-11)14(15,16)17/h3-6H,2,7-8H2,1H3,(H,18,21) HDUDAIBDRVYJPA-UHFFFAOYSA-N 162730 US9056843, 21 Histone deacetylase 4 Homo sapiens 730 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162730 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162730&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230962 310304669 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305702 FCCNC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C12H9F4N3O2/c13-5-6-17-10(20)8-3-1-7(2-4-8)9-18-11(21-19-9)12(14,15)16/h1-4H,5-6H2,(H,17,20) QODBUGGODSSXSA-UHFFFAOYSA-N 162731 US9056843, 22 Histone deacetylase 4 Homo sapiens 870 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162731 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162731&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71486844 310304670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305703 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)N1CCCC1 InChI=1S/C14H12F3N3O2/c15-14(16,17)13-18-11(19-22-13)9-3-5-10(6-4-9)12(21)20-7-1-2-8-20/h3-6H,1-2,7-8H2 LDCGWTBLKGMXOU-UHFFFAOYSA-N 162732 US9056843, 23 Histone deacetylase 4 Homo sapiens 1500 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162732 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162732&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230722 310304671 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305704 CC(C)N(C)C(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C14H14F3N3O2/c1-8(2)20(3)12(21)10-6-4-9(5-7-10)11-18-13(22-19-11)14(15,16)17/h4-8H,1-3H3 OBPARYKTAQRTGU-UHFFFAOYSA-N 162733 US9056843, 24 Histone deacetylase 4 Homo sapiens 770 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162733 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162733&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230808 310304672 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305705 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1CCC1 InChI=1S/C14H12F3N3O2/c15-14(16,17)13-19-11(20-22-13)8-4-6-9(7-5-8)12(21)18-10-2-1-3-10/h4-7,10H,1-3H2,(H,18,21) RCIALLJWGLHRGI-UHFFFAOYSA-N 162734 US9056843, 25 Histone deacetylase 4 Homo sapiens 470 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162734 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162734&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230838 310304673 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305706 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NCC1CC1 InChI=1S/C14H12F3N3O2/c15-14(16,17)13-19-11(20-22-13)9-3-5-10(6-4-9)12(21)18-7-8-1-2-8/h3-6,8H,1-2,7H2,(H,18,21) UZDLGBNHYREMCH-UHFFFAOYSA-N 162735 US9056843, 26 Histone deacetylase 4 Homo sapiens 610 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162735 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162735&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230878 310304674 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305707 CC(C)CNC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C14H14F3N3O2/c1-8(2)7-18-12(21)10-5-3-9(4-6-10)11-19-13(22-20-11)14(15,16)17/h3-6,8H,7H2,1-2H3,(H,18,21) BAEVURPLUCNNJZ-UHFFFAOYSA-N 162736 US9056843, 27 Histone deacetylase 4 Homo sapiens 1200 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162736 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162736&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230875 310304675 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305708 C[C@H](CO)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C13H12F3N3O3/c1-7(6-20)17-11(21)9-4-2-8(3-5-9)10-18-12(22-19-10)13(14,15)16/h2-5,7,20H,6H2,1H3,(H,17,21)/t7-/m1/s1 OVJXKZYFRSLKOB-SSDOTTSWSA-N 162737 US9056843, 28 Histone deacetylase 4 Homo sapiens 350 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162737 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162737&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230997 310304676 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305709 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1CCCC1 InChI=1S/C15H14F3N3O2/c16-15(17,18)14-20-12(21-23-14)9-5-7-10(8-6-9)13(22)19-11-3-1-2-4-11/h5-8,11H,1-4H2,(H,19,22) QNOFNGIYSBDWCK-UHFFFAOYSA-N 162738 US9056843, 29 Histone deacetylase 4 Homo sapiens 1200 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162738 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162738&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 53604893 310304677 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305710 CCC(CC)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C15H16F3N3O2/c1-3-11(4-2)19-13(22)10-7-5-9(6-8-10)12-20-14(23-21-12)15(16,17)18/h5-8,11H,3-4H2,1-2H3,(H,19,22) CHSAEGDXJBTHLE-UHFFFAOYSA-N 162739 US9056843, 30 Histone deacetylase 4 Homo sapiens 6400 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162739 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162739&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230869 310304678 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305711 CN(C)CCNC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C14H15F3N4O2/c1-21(2)8-7-18-12(22)10-5-3-9(4-6-10)11-19-13(23-20-11)14(15,16)17/h3-6H,7-8H2,1-2H3,(H,18,22) WQQRFNUUMOENDZ-UHFFFAOYSA-N 162740 US9056843, 31 Histone deacetylase 4 Homo sapiens 80 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162740 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162740&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230972 310304679 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305712 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)N1CCOCC1 InChI=1S/C14H12F3N3O3/c15-14(16,17)13-18-11(19-23-13)9-1-3-10(4-2-9)12(21)20-5-7-22-8-6-20/h1-4H,5-8H2 ZCUCOLTXMNWPAO-UHFFFAOYSA-N 162741 US9056843, 32 Histone deacetylase 4 Homo sapiens 4400 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162741 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162741&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230723 310304680 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305713 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)N1CCCCC1 InChI=1S/C15H14F3N3O2/c16-15(17,18)14-19-12(20-23-14)10-4-6-11(7-5-10)13(22)21-8-2-1-3-9-21/h4-7H,1-3,8-9H2 RLVQKWNRZLOFFG-UHFFFAOYSA-N 162742 US9056843, 33 Histone deacetylase 4 Homo sapiens 400 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162742 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162742&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230718 310304681 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305714 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1CCCCC1 InChI=1S/C16H16F3N3O2/c17-16(18,19)15-21-13(22-24-15)10-6-8-11(9-7-10)14(23)20-12-4-2-1-3-5-12/h6-9,12H,1-5H2,(H,20,23) UVRXMEVVBPJLKM-UHFFFAOYSA-N 162743 US9056843, 34 Histone deacetylase 4 Homo sapiens 750 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162743 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162743&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230750 310304682 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305715 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)Nc1ccccc1 InChI=1S/C16H10F3N3O2/c17-16(18,19)15-21-13(22-24-15)10-6-8-11(9-7-10)14(23)20-12-4-2-1-3-5-12/h1-9H,(H,20,23) HPXKHBOPEQOIGG-UHFFFAOYSA-N 162744 US9056843, 35 Histone deacetylase 4 Homo sapiens 6700 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162744 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162744&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230961 310304683 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305716 CN1CCN(CC1)C(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C15H15F3N4O2/c1-21-6-8-22(9-7-21)13(23)11-4-2-10(3-5-11)12-19-14(24-20-12)15(16,17)18/h2-5H,6-9H2,1H3 MNYTWBQGSPDBNG-UHFFFAOYSA-N 162745 US9056843, 36 Histone deacetylase 4 Homo sapiens 2700 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162745 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162745&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230704 310304684 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305717 CN(C)CCN(C)C(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C15H17F3N4O2/c1-21(2)8-9-22(3)13(23)11-6-4-10(5-7-11)12-19-14(24-20-12)15(16,17)18/h4-7H,8-9H2,1-3H3 LJLKZLDXCUPHCY-UHFFFAOYSA-N 162746 US9056843, 37 Histone deacetylase 4 Homo sapiens 340 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162746 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162746&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71231062 310304685 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305718 CN1CCC(CC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C16H17F3N4O2/c1-23-8-6-12(7-9-23)20-14(24)11-4-2-10(3-5-11)13-21-15(25-22-13)16(17,18)19/h2-5,12H,6-9H2,1H3,(H,20,24) ZKXVGQIJTDTQSU-UHFFFAOYSA-N 162747 US9056843, 38 Histone deacetylase 4 Homo sapiens 300 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162747 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162747&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230714 310304686 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305719 CN(C)C1CCN(CC1)C(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C17H19F3N4O2/c1-23(2)13-7-9-24(10-8-13)15(25)12-5-3-11(4-6-12)14-21-16(26-22-14)17(18,19)20/h3-6,13H,7-10H2,1-2H3 YGICMNXAHMVDFR-UHFFFAOYSA-N 162748 US9056843, 39 Histone deacetylase 4 Homo sapiens 1200 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162748 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162748&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90149742 310304687 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305720 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NCCCn1ccnc1 InChI=1S/C16H14F3N5O2/c17-16(18,19)15-22-13(23-26-15)11-2-4-12(5-3-11)14(25)21-6-1-8-24-9-7-20-10-24/h2-5,7,9-10H,1,6,8H2,(H,21,25) LKODDWQUWKQCNK-UHFFFAOYSA-N 162749 US9056843, 40 Histone deacetylase 4 Homo sapiens 460 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162749 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162749&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230988 310304688 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305721 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)N1CCN(CC1)c1ccccc1 InChI=1S/C20H17F3N4O2/c21-20(22,23)19-24-17(25-29-19)14-6-8-15(9-7-14)18(28)27-12-10-26(11-13-27)16-4-2-1-3-5-16/h1-9H,10-13H2 YROWRZJBWQXKEN-UHFFFAOYSA-N 162751 US9056843, 42 Histone deacetylase 4 Homo sapiens 4200 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162751 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162751&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230736 310304690 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305722 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)N1CCC(Cc2ccccc2)CC1 InChI=1S/C22H20F3N3O2/c23-22(24,25)21-26-19(27-30-21)17-6-8-18(9-7-17)20(29)28-12-10-16(11-13-28)14-15-4-2-1-3-5-15/h1-9,16H,10-14H2 YLBCXOIFKCBADR-UHFFFAOYSA-N 162752 US9056843, 43 Histone deacetylase 4 Homo sapiens 290 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162752 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162752&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230910 310304691 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305723 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NCc1ccc(CN2CCOCC2)cc1 InChI=1S/C22H21F3N4O3/c23-22(24,25)21-27-19(28-32-21)17-5-7-18(8-6-17)20(30)26-13-15-1-3-16(4-2-15)14-29-9-11-31-12-10-29/h1-8H,9-14H2,(H,26,30) RYYVPBGCWHBQSE-UHFFFAOYSA-N 162753 US9056843, 44 Histone deacetylase 4 Homo sapiens 380 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162753 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162753&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230765 310304692 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305724 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NCCc1ccccc1 InChI=1S/C18H14F3N3O2/c19-18(20,21)17-23-15(24-26-17)13-6-8-14(9-7-13)16(25)22-11-10-12-4-2-1-3-5-12/h1-9H,10-11H2,(H,22,25) ZHWAHTLIBHKQHD-UHFFFAOYSA-N 162754 US9056843, 45 Histone deacetylase 4 Homo sapiens 4200 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162754 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162754&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230922 310304693 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305725 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NCc1ccccc1 InChI=1S/C17H12F3N3O2/c18-17(19,20)16-22-14(23-25-16)12-6-8-13(9-7-12)15(24)21-10-11-4-2-1-3-5-11/h1-9H,10H2,(H,21,24) QSZJMHJUHPETAJ-UHFFFAOYSA-N 162755 US9056843, 46 Histone deacetylase 4 Homo sapiens 780 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162755 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162755&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230694 310304694 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305726 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)Nc1ccncc1 InChI=1S/C15H9F3N4O2/c16-15(17,18)14-21-12(22-24-14)9-1-3-10(4-2-9)13(23)20-11-5-7-19-8-6-11/h1-8H,(H,19,20,23) HYUNVYPZXAPTLK-UHFFFAOYSA-N 162756 US9056843, 47 Histone deacetylase 4 Homo sapiens 54 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162756 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162756&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230889 310304695 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305727 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)Nc1cccnc1 InChI=1S/C15H9F3N4O2/c16-15(17,18)14-21-12(22-24-14)9-3-5-10(6-4-9)13(23)20-11-2-1-7-19-8-11/h1-8H,(H,20,23) WKYPMIUTBVBTBC-UHFFFAOYSA-N 162757 US9056843, 48 Histone deacetylase 4 Homo sapiens 140 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162757 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162757&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230854 310304696 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305728 CN1CCC(CNC(=O)c2ccc(cc2)-c2noc(n2)C(F)(F)F)CC1 InChI=1S/C17H19F3N4O2/c1-24-8-6-11(7-9-24)10-21-15(25)13-4-2-12(3-5-13)14-22-16(26-23-14)17(18,19)20/h2-5,11H,6-10H2,1H3,(H,21,25) PEYXGCUWDPMOQQ-UHFFFAOYSA-N 162758 US9056843, 49 Histone deacetylase 4 Homo sapiens 990 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162758 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162758&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71231002 310304697 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305729 C[C@@H](CO)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C13H12F3N3O3/c1-7(6-20)17-11(21)9-4-2-8(3-5-9)10-18-12(22-19-10)13(14,15)16/h2-5,7,20H,6H2,1H3,(H,17,21)/t7-/m0/s1 OVJXKZYFRSLKOB-ZETCQYMHSA-N 162759 US9056843, 50 Histone deacetylase 4 Homo sapiens 620 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162759 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162759&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230908 310304698 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305730 CC(CNC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F)N(C)C InChI=1S/C15H17F3N4O2/c1-9(22(2)3)8-19-13(23)11-6-4-10(5-7-11)12-20-14(24-21-12)15(16,17)18/h4-7,9H,8H2,1-3H3,(H,19,23) DAZQBYXNTIVFIN-UHFFFAOYSA-N 162760 US9056843, 51 Histone deacetylase 4 Homo sapiens 90 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162760 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162760&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230953 310304699 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305731 CN(C)C(=O)CNC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C14H13F3N4O3/c1-21(2)10(22)7-18-12(23)9-5-3-8(4-6-9)11-19-13(24-20-11)14(15,16)17/h3-6H,7H2,1-2H3,(H,18,23) DVNWGPYBIKWMID-UHFFFAOYSA-N 162761 US9056843, 52 Histone deacetylase 4 Homo sapiens 3200 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162761 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162761&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230917 310304700 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305732 CC(CN(C)C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C15H17F3N4O2/c1-9(8-22(2)3)19-13(23)11-6-4-10(5-7-11)12-20-14(24-21-12)15(16,17)18/h4-7,9H,8H2,1-3H3,(H,19,23) RUDQZAZYCMBBDU-UHFFFAOYSA-N 162762 US9056843, 53 Histone deacetylase 4 Homo sapiens 26 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162762 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162762&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230883 310304701 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305733 OC1CCN(C1)C(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C14H12F3N3O3/c15-14(16,17)13-18-11(19-23-13)8-1-3-9(4-2-8)12(22)20-6-5-10(21)7-20/h1-4,10,21H,5-7H2 JVBZAWBETPLJQP-UHFFFAOYSA-N 162763 US9056843, 54 Histone deacetylase 4 Homo sapiens 2000 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162763 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162763&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230836 310304702 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305734 CC(C)(C)OC(=O)N1CCN(CC1)C(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C19H21F3N4O4/c1-18(2,3)29-17(28)26-10-8-25(9-11-26)15(27)13-6-4-12(5-7-13)14-23-16(30-24-14)19(20,21)22/h4-7H,8-11H2,1-3H3 HHIGFWAPRFPOAE-UHFFFAOYSA-N 162764 US9056843, 55 Histone deacetylase 4 Homo sapiens 2800 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162764 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162764&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230794 310304703 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305735 CCC(CO)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C14H14F3N3O3/c1-2-10(7-21)18-12(22)9-5-3-8(4-6-9)11-19-13(23-20-11)14(15,16)17/h3-6,10,21H,2,7H2,1H3,(H,18,22) KLMHYDZGQAUVJU-UHFFFAOYSA-N 162765 US9056843, 56 Histone deacetylase 4 Homo sapiens 550 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162765 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162765&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230669 310304704 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305736 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1CCOCC1 InChI=1S/C15H14F3N3O3/c16-15(17,18)14-20-12(21-24-14)9-1-3-10(4-2-9)13(22)19-11-5-7-23-8-6-11/h1-4,11H,5-8H2,(H,19,22) WFAMAZWNHSUPHS-UHFFFAOYSA-N 162766 US9056843, 57 Histone deacetylase 4 Homo sapiens 520 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162766 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162766&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230918 310304705 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305737 CC(C)CC(CO)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C16H18F3N3O3/c1-9(2)7-12(8-23)20-14(24)11-5-3-10(4-6-11)13-21-15(25-22-13)16(17,18)19/h3-6,9,12,23H,7-8H2,1-2H3,(H,20,24) RTGVPFOGXQMUDV-UHFFFAOYSA-N 162767 US9056843, 58 Histone deacetylase 4 Homo sapiens 650 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162767 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162767&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230678 310304706 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305738 CC(C)(C)OC(=O)N1CCC(CC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C20H23F3N4O4/c1-19(2,3)30-18(29)27-10-8-14(9-11-27)24-16(28)13-6-4-12(5-7-13)15-25-17(31-26-15)20(21,22)23/h4-7,14H,8-11H2,1-3H3,(H,24,28) BNYIMPFCWKQUKO-UHFFFAOYSA-N 162768 US9056843, 59 Histone deacetylase 4 Homo sapiens 1400 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162768 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162768&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230886 310304707 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305739 CC(C)(C)OC(=O)NC1CCCCC1NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C21H25F3N4O4/c1-20(2,3)31-19(30)26-15-7-5-4-6-14(15)25-17(29)13-10-8-12(9-11-13)16-27-18(32-28-16)21(22,23)24/h8-11,14-15H,4-7H2,1-3H3,(H,25,29)(H,26,30) SJXPNFQVEDVGNN-UHFFFAOYSA-N 162769 US9056843, 60 Histone deacetylase 4 Homo sapiens 2500 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162769 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162769&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71231821 310304708 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305740 OC1CCCCC1NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C16H16F3N3O3/c17-16(18,19)15-21-13(22-25-15)9-5-7-10(8-6-9)14(24)20-11-3-1-2-4-12(11)23/h5-8,11-12,23H,1-4H2,(H,20,24) PEVBMHBRFKTGBF-UHFFFAOYSA-N 162770 US9056843, 61 Histone deacetylase 4 Homo sapiens 790 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162770 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162770&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230672 310304709 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305741 CC(C)(C)OC(=O)N1CCCC(C1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C20H23F3N4O4/c1-19(2,3)30-18(29)27-10-4-5-14(11-27)24-16(28)13-8-6-12(7-9-13)15-25-17(31-26-15)20(21,22)23/h6-9,14H,4-5,10-11H2,1-3H3,(H,24,28) AMSIRPKTHALNTG-UHFFFAOYSA-N 162771 US9056843, 62 Histone deacetylase 4 Homo sapiens 600 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162771 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162771&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230687 310304710 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305742 CNC(=O)CNC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C13H11F3N4O3/c1-17-9(21)6-18-11(22)8-4-2-7(3-5-8)10-19-12(23-20-10)13(14,15)16/h2-5H,6H2,1H3,(H,17,21)(H,18,22) ANBHBOSPBLPVGY-UHFFFAOYSA-N 162772 US9056843, 63 Histone deacetylase 4 Homo sapiens 780 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162772 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162772&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71231075 310304711 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305743 CC(=O)N1CCC(CC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C17H17F3N4O3/c1-10(25)24-8-6-13(7-9-24)21-15(26)12-4-2-11(3-5-12)14-22-16(27-23-14)17(18,19)20/h2-5,13H,6-9H2,1H3,(H,21,26) PDVOQWPQBJPSGT-UHFFFAOYSA-N 162773 US9056843, 64 Histone deacetylase 4 Homo sapiens 510 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162773 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162773&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230983 310304712 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305744 CN1C(C)(C)CC(CC1(C)C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C20H25F3N4O2/c1-18(2)10-14(11-19(3,4)27(18)5)24-16(28)13-8-6-12(7-9-13)15-25-17(29-26-15)20(21,22)23/h6-9,14H,10-11H2,1-5H3,(H,24,28) GGMOBWZNPWJEJS-UHFFFAOYSA-N 162774 US9056843, 65 Histone deacetylase 4 Homo sapiens 240 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162774 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162774&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71231824 310304713 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305745 CC(C)(C)OC(=O)N1CCC(C1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C19H21F3N4O4/c1-18(2,3)29-17(28)26-9-8-13(10-26)23-15(27)12-6-4-11(5-7-12)14-24-16(30-25-14)19(20,21)22/h4-7,13H,8-10H2,1-3H3,(H,23,27) GANJXJXQJXMNGM-UHFFFAOYSA-N 162775 US9056843, 66 Histone deacetylase 4 Homo sapiens 330 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162775 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162775&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230958 310304714 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305746 COc1cc(NC(=O)c2ccc(cc2)-c2noc(n2)C(F)(F)F)ccn1 InChI=1S/C16H11F3N4O3/c1-25-12-8-11(6-7-20-12)21-14(24)10-4-2-9(3-5-10)13-22-15(26-23-13)16(17,18)19/h2-8H,1H3,(H,20,21,24) SNHBOCUHRATDMD-UHFFFAOYSA-N 162776 US9056843, 67 Histone deacetylase 4 Homo sapiens 160 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162776 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162776&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230874 310304715 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305747 Cc1cc(NC(=O)c2ccc(cc2)-c2noc(n2)C(F)(F)F)cc(C)n1 InChI=1S/C17H13F3N4O2/c1-9-7-13(8-10(2)21-9)22-15(25)12-5-3-11(4-6-12)14-23-16(26-24-14)17(18,19)20/h3-8H,1-2H3,(H,21,22,25) LRPMALDGVSZZCZ-UHFFFAOYSA-N 162777 US9056843, 68 Histone deacetylase 4 Homo sapiens 170 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162777 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162777&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71231834 310304716 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305748 CC(C)(C)c1cc(NC(=O)c2ccc(cc2)-c2noc(n2)C(F)(F)F)ccn1 InChI=1S/C19H17F3N4O2/c1-18(2,3)14-10-13(8-9-23-14)24-16(27)12-6-4-11(5-7-12)15-25-17(28-26-15)19(20,21)22/h4-10H,1-3H3,(H,23,24,27) CEMDGSJFCGBITC-UHFFFAOYSA-N 162778 US9056843, 69 Histone deacetylase 4 Homo sapiens 290 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162778 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162778&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230995 310304717 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305749 Fc1cc(NC(=O)c2ccc(cc2)-c2noc(n2)C(F)(F)F)ccn1 InChI=1S/C15H8F4N4O2/c16-11-7-10(5-6-20-11)21-13(24)9-3-1-8(2-4-9)12-22-14(25-23-12)15(17,18)19/h1-7H,(H,20,21,24) BXFUKLNQVVWJAF-UHFFFAOYSA-N 162780 US9056843, 71 Histone deacetylase 4 Homo sapiens 920 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162780 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162780&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230746 310304719 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305750 Oc1cc(NC(=O)c2ccc(cc2)-c2noc(n2)C(F)(F)F)ccn1 InChI=1S/C15H9F3N4O3/c16-15(17,18)14-21-12(22-25-14)8-1-3-9(4-2-8)13(24)20-10-5-6-19-11(23)7-10/h1-7H,(H2,19,20,23,24) NLRDGERSGBVMEI-UHFFFAOYSA-N 162781 US9056843, 72 Histone deacetylase 4 Homo sapiens 140 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162781 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162781&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230811 310304720 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305751 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)Nc1ccnc(c1)C#N InChI=1S/C16H8F3N5O2/c17-16(18,19)15-23-13(24-26-15)9-1-3-10(4-2-9)14(25)22-11-5-6-21-12(7-11)8-20/h1-7H,(H,21,22,25) JDABOMNBVNHXEX-UHFFFAOYSA-N 162782 US9056843, 73 Histone deacetylase 4 Homo sapiens 53 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162782 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162782&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230781 310304721 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305752 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)Nc1ccnc(c1)C(F)(F)F InChI=1S/C16H8F6N4O2/c17-15(18,19)11-7-10(5-6-23-11)24-13(27)9-3-1-8(2-4-9)12-25-14(28-26-12)16(20,21)22/h1-7H,(H,23,24,27) XTKIFUMMJGGKQY-UHFFFAOYSA-N 162783 US9056843, 74 Histone deacetylase 4 Homo sapiens 190 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162783 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162783&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 89392516 310304722 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305753 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)Nc1ccnc(Cl)c1 InChI=1S/C15H8ClF3N4O2/c16-11-7-10(5-6-20-11)21-13(24)9-3-1-8(2-4-9)12-22-14(25-23-12)15(17,18)19/h1-7H,(H,20,21,24) KQNUAZJWXAWJGE-UHFFFAOYSA-N 162784 US9056843, 75 Histone deacetylase 4 Homo sapiens 160 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162784 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162784&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71487211 310304723 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305754 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1CCNCC1 InChI=1S/C15H15F3N4O2/c16-15(17,18)14-21-12(22-24-14)9-1-3-10(4-2-9)13(23)20-11-5-7-19-8-6-11/h1-4,11,19H,5-8H2,(H,20,23) XIFXZWCFBKXMDS-UHFFFAOYSA-N 162785 US9056843, 76 Histone deacetylase 4 Homo sapiens 150 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162785 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162785&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230939 310304724 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305755 NC1CCCCC1NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C16H17F3N4O2/c17-16(18,19)15-22-13(23-25-15)9-5-7-10(8-6-9)14(24)21-12-4-2-1-3-11(12)20/h5-8,11-12H,1-4,20H2,(H,21,24) VMVSNRMSJYGJSA-UHFFFAOYSA-N 162786 US9056843, 77 Histone deacetylase 4 Homo sapiens 350 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162786 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162786&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230755 310304725 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305756 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NCC1CCCCN1 InChI=1S/C16H17F3N4O2/c17-16(18,19)15-22-13(23-25-15)10-4-6-11(7-5-10)14(24)21-9-12-3-1-2-8-20-12/h4-7,12,20H,1-3,8-9H2,(H,21,24) KTWOCFCHDBZNAU-UHFFFAOYSA-N 162787 US9056843, 78 Histone deacetylase 4 Homo sapiens 30 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162787 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162787&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230712 310304726 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305757 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1CCCNC1 InChI=1S/C15H15F3N4O2/c16-15(17,18)14-21-12(22-24-14)9-3-5-10(6-4-9)13(23)20-11-2-1-7-19-8-11/h3-6,11,19H,1-2,7-8H2,(H,20,23) UTOKIBJBESYARY-UHFFFAOYSA-N 162788 US9056843, 79 Histone deacetylase 4 Homo sapiens 800 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162788 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162788&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230991 310304727 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305758 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1CCNC1 InChI=1S/C14H13F3N4O2/c15-14(16,17)13-20-11(21-23-13)8-1-3-9(4-2-8)12(22)19-10-5-6-18-7-10/h1-4,10,18H,5-7H2,(H,19,22) UHMRHXFYCAGYDK-UHFFFAOYSA-N 162789 US9056843, 80::US9056843, 86::US9056843, 87 Histone deacetylase 4 Homo sapiens 470 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162789 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162789&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230795 310304728 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305759 C[C@H](CN(C)C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C15H17F3N4O2/c1-9(8-22(2)3)19-13(23)11-6-4-10(5-7-11)12-20-14(24-21-12)15(16,17)18/h4-7,9H,8H2,1-3H3,(H,19,23)/t9-/m1/s1 RUDQZAZYCMBBDU-SECBINFHSA-N 162790 US9056843, 81 Histone deacetylase 4 Homo sapiens 34 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162790 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162790&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230987 310304729 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305760 C[C@@H](CN(C)C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C15H17F3N4O2/c1-9(8-22(2)3)19-13(23)11-6-4-10(5-7-11)12-20-14(24-21-12)15(16,17)18/h4-7,9H,8H2,1-3H3,(H,19,23)/t9-/m0/s1 RUDQZAZYCMBBDU-VIFPVBQESA-N 162791 US9056843, 82 Histone deacetylase 4 Homo sapiens 120 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162791 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162791&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71231076 310304730 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305761 CC(C)[C@@H](CN(C)C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C17H21F3N4O2/c1-10(2)13(9-24(3)4)21-15(25)12-7-5-11(6-8-12)14-22-16(26-23-14)17(18,19)20/h5-8,10,13H,9H2,1-4H3,(H,21,25)/t13-/m1/s1 AEYCDQOGCGZAQF-CYBMUJFWSA-N 162792 US9056843, 83 Histone deacetylase 4 Homo sapiens 15 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162792 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162792&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230861 310304731 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305762 CC(C)[C@H](CN(C)C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C17H21F3N4O2/c1-10(2)13(9-24(3)4)21-15(25)12-7-5-11(6-8-12)14-22-16(26-23-14)17(18,19)20/h5-8,10,13H,9H2,1-4H3,(H,21,25)/t13-/m0/s1 AEYCDQOGCGZAQF-ZDUSSCGKSA-N 162793 US9056843, 84 Histone deacetylase 4 Homo sapiens 490 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162793 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162793&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230965 310304732 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305763 CC(C)C[C@H](CN(C)C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C18H23F3N4O2/c1-11(2)9-14(10-25(3)4)22-16(26)13-7-5-12(6-8-13)15-23-17(27-24-15)18(19,20)21/h5-8,11,14H,9-10H2,1-4H3,(H,22,26)/t14-/m1/s1 FUZUCHDVPZXYLX-CQSZACIVSA-N 162794 US9056843, 85 Histone deacetylase 4 Homo sapiens 48 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162794 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162794&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71231828 310304733 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305764 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1CCNC1 InChI=1S/C14H13F3N4O2/c15-14(16,17)13-20-11(21-23-13)8-1-3-9(4-2-8)12(22)19-10-5-6-18-7-10/h1-4,10,18H,5-7H2,(H,19,22) UHMRHXFYCAGYDK-UHFFFAOYSA-N 162789 US9056843, 80::US9056843, 86::US9056843, 87 Histone deacetylase 4 Homo sapiens 26 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162789 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162789&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230795 310304728 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305765 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1CCNC1 InChI=1S/C14H13F3N4O2/c15-14(16,17)13-20-11(21-23-13)8-1-3-9(4-2-8)12(22)19-10-5-6-18-7-10/h1-4,10,18H,5-7H2,(H,19,22) UHMRHXFYCAGYDK-UHFFFAOYSA-N 162789 US9056843, 80::US9056843, 86::US9056843, 87 Histone deacetylase 4 Homo sapiens 300 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162789 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162789&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230795 310304728 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305766 C[C@H](CN(C)C)NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C15H16F4N4O2/c1-8(7-23(2)3)20-13(24)10-5-4-9(6-11(10)16)12-21-14(25-22-12)15(17,18)19/h4-6,8H,7H2,1-3H3,(H,20,24)/t8-/m1/s1 VOMITJFOPUYFCG-MRVPVSSYSA-N 162797 US9056843, 88 Histone deacetylase 4 Homo sapiens 12 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162797 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162797&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230817 310304734 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305767 CC(C)[C@H](CN(C)C)NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C17H20F4N4O2/c1-9(2)13(8-25(3)4)22-15(26)11-6-5-10(7-12(11)18)14-23-16(27-24-14)17(19,20)21/h5-7,9,13H,8H2,1-4H3,(H,22,26)/t13-/m0/s1 SEFLMEHQUXUCGV-ZDUSSCGKSA-N 162798 US9056843, 89 Histone deacetylase 4 Homo sapiens 45 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162798 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162798&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71231823 310304735 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305768 Cc1cc(NC(=O)c2ccc(cc2F)-c2noc(n2)C(F)(F)F)cc(C)n1 InChI=1S/C17H12F4N4O2/c1-8-5-11(6-9(2)22-8)23-15(26)12-4-3-10(7-13(12)18)14-24-16(27-25-14)17(19,20)21/h3-7H,1-2H3,(H,22,23,26) XRJFYSYVAPTXDH-UHFFFAOYSA-N 162799 US9056843, 90 Histone deacetylase 4 Homo sapiens 440 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162799 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162799&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230990 310304736 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305769 CC(CO)NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C13H11F4N3O3/c1-6(5-21)18-11(22)8-3-2-7(4-9(8)14)10-19-12(23-20-10)13(15,16)17/h2-4,6,21H,5H2,1H3,(H,18,22) CGAIENVNQZIGEE-UHFFFAOYSA-N 162800 US9056843, 91 Histone deacetylase 4 Homo sapiens 500 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162800 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162800&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230872 310304737 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305770 CN(C)C[C@@H](Cc1ccccc1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C21H21F3N4O2/c1-28(2)13-17(12-14-6-4-3-5-7-14)25-19(29)16-10-8-15(9-11-16)18-26-20(30-27-18)21(22,23)24/h3-11,17H,12-13H2,1-2H3,(H,25,29)/t17-/m1/s1 OKQODVVBOYRGOX-QGZVFWFLSA-N 162801 US9056843, 92 Histone deacetylase 4 Homo sapiens 85 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162801 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162801&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230877 310304738 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305771 CN(C)C[C@H](Cc1ccccc1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C21H21F3N4O2/c1-28(2)13-17(12-14-6-4-3-5-7-14)25-19(29)16-10-8-15(9-11-16)18-26-20(30-27-18)21(22,23)24/h3-11,17H,12-13H2,1-2H3,(H,25,29)/t17-/m0/s1 OKQODVVBOYRGOX-KRWDZBQOSA-N 162802 US9056843, 93 Histone deacetylase 4 Homo sapiens 190 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162802 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162802&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230904 310304739 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305772 CC(CN(C)C)N(C)C(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C16H19F3N4O2/c1-10(9-22(2)3)23(4)14(24)12-7-5-11(6-8-12)13-20-15(25-21-13)16(17,18)19/h5-8,10H,9H2,1-4H3 DHTRSJIKOUWOPE-UHFFFAOYSA-N 162803 US9056843, 94 Histone deacetylase 4 Homo sapiens 520 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162803 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162803&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230994 310304740 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305773 Fc1cc(ccc1C(=O)NC1CCNC1)-c1noc(n1)C(F)(F)F InChI=1S/C14H12F4N4O2/c15-10-5-7(11-21-13(24-22-11)14(16,17)18)1-2-9(10)12(23)20-8-3-4-19-6-8/h1-2,5,8,19H,3-4,6H2,(H,20,23) HBDFDUASWNHARO-UHFFFAOYSA-N 162804 US9056843, 95 Histone deacetylase 4 Homo sapiens 160 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162804 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162804&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230870 310304741 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305774 FC(F)(F)c1nc(no1)-c1ccc(cc1)S(=O)(=O)Nc1ccccc1 InChI=1S/C15H10F3N3O3S/c16-15(17,18)14-19-13(20-24-14)10-6-8-12(9-7-10)25(22,23)21-11-4-2-1-3-5-11/h1-9,21H SIAORXMCCJMMQI-UHFFFAOYSA-N 162805 US9056843, 96 Histone deacetylase 4 Homo sapiens 96 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162805 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162805&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230771 310304742 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305775 FC(F)(F)c1nc(no1)-c1ccc(cc1)S(=O)(=O)NCc1ccccc1 InChI=1S/C16H12F3N3O3S/c17-16(18,19)15-21-14(22-25-15)12-6-8-13(9-7-12)26(23,24)20-10-11-4-2-1-3-5-11/h1-9,20H,10H2 PXYCEUHIRAXEMS-UHFFFAOYSA-N 162806 US9056843, 97 Histone deacetylase 4 Homo sapiens 430 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162806 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162806&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230969 310304743 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305776 CN(C)CCNS(=O)(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C13H15F3N4O3S/c1-20(2)8-7-17-24(21,22)10-5-3-9(4-6-10)11-18-12(23-19-11)13(14,15)16/h3-6,17H,7-8H2,1-2H3 JBJFEZGKJXAMHI-UHFFFAOYSA-N 162807 US9056843, 98 Histone deacetylase 4 Homo sapiens 360 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162807 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162807&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230913 310304744 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305777 CN(C)CCN(C)S(=O)(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C14H17F3N4O3S/c1-20(2)8-9-21(3)25(22,23)11-6-4-10(5-7-11)12-18-13(24-19-12)14(15,16)17/h4-7H,8-9H2,1-3H3 UBVWFRWJFZEEQG-UHFFFAOYSA-N 162808 US9056843, 99 Histone deacetylase 4 Homo sapiens 1350 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162808 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162808&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230758 310304745 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305778 FC(F)(F)c1nc(no1)-c1ccc(cc1)S(=O)(=O)NCC1CCCCC1 InChI=1S/C16H18F3N3O3S/c17-16(18,19)15-21-14(22-25-15)12-6-8-13(9-7-12)26(23,24)20-10-11-4-2-1-3-5-11/h6-9,11,20H,1-5,10H2 AQSONWJIIFUAFZ-UHFFFAOYSA-N 162810 US9056843, 101 Histone deacetylase 4 Homo sapiens 2950 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162810 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162810&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230888 310304747 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305779 FC(F)(F)c1nc(no1)-c1ccc(cc1)S(=O)(=O)N[C@@H]1CCNC1 InChI=1S/C13H13F3N4O3S/c14-13(15,16)12-18-11(19-23-12)8-1-3-10(4-2-8)24(21,22)20-9-5-6-17-7-9/h1-4,9,17,20H,5-7H2/t9-/m1/s1 AAWHMGOBZKUZOG-SECBINFHSA-N 162811 US9056843, 102 Histone deacetylase 4 Homo sapiens 3200 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162811 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162811&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230899 310304748 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305780 Cc1ccccc1NS(=O)(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C16H12F3N3O3S/c1-10-4-2-3-5-13(10)22-26(23,24)12-8-6-11(7-9-12)14-20-15(25-21-14)16(17,18)19/h2-9,22H,1H3 ODALFKHUQBMPOY-UHFFFAOYSA-N 162812 US9056843, 103 Histone deacetylase 4 Homo sapiens 80 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162812 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162812&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230868 310304749 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305781 FC(F)(F)c1nc(no1)-c1ccc(cc1)S(=O)(=O)Nc1ccccc1Cl InChI=1S/C15H9ClF3N3O3S/c16-11-3-1-2-4-12(11)22-26(23,24)10-7-5-9(6-8-10)13-20-14(25-21-13)15(17,18)19/h1-8,22H YADZNZJJYXXYPH-UHFFFAOYSA-N 162813 US9056843, 104 Histone deacetylase 4 Homo sapiens 840 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162813 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162813&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230692 310304750 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305782 Cc1cccc(NS(=O)(=O)c2ccc(cc2)-c2noc(n2)C(F)(F)F)c1 InChI=1S/C16H12F3N3O3S/c1-10-3-2-4-12(9-10)22-26(23,24)13-7-5-11(6-8-13)14-20-15(25-21-14)16(17,18)19/h2-9,22H,1H3 XVQXAPJYHCFGLN-UHFFFAOYSA-N 162814 US9056843, 105 Histone deacetylase 4 Homo sapiens 270 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162814 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162814&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230880 310304751 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305783 FC(F)(F)c1nc(no1)-c1ccc(cc1)S(=O)(=O)Nc1cccc(Cl)c1 InChI=1S/C15H9ClF3N3O3S/c16-10-2-1-3-11(8-10)22-26(23,24)12-6-4-9(5-7-12)13-20-14(25-21-13)15(17,18)19/h1-8,22H CCTJSYDYNOIIBA-UHFFFAOYSA-N 162816 US9056843, 107 Histone deacetylase 4 Homo sapiens 790 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162816 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162816&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230743 310304753 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305784 Cc1ccc(NS(=O)(=O)c2ccc(cc2)-c2noc(n2)C(F)(F)F)cc1 InChI=1S/C16H12F3N3O3S/c1-10-2-6-12(7-3-10)22-26(23,24)13-8-4-11(5-9-13)14-20-15(25-21-14)16(17,18)19/h2-9,22H,1H3 FFRHGVVKHFNCCX-UHFFFAOYSA-N 162817 US9056843, 108 Histone deacetylase 4 Homo sapiens 93 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162817 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162817&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230856 310304754 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305785 Fc1ccc(NS(=O)(=O)c2ccc(cc2)-c2noc(n2)C(F)(F)F)cc1 InChI=1S/C15H9F4N3O3S/c16-10-3-5-11(6-4-10)22-26(23,24)12-7-1-9(2-8-12)13-20-14(25-21-13)15(17,18)19/h1-8,22H XBXBLIPKIMLSST-UHFFFAOYSA-N 162818 US9056843, 109 Histone deacetylase 4 Homo sapiens 97 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162818 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162818&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230951 310304755 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305786 FC(F)(F)c1nc(no1)-c1ccc(cc1)S(=O)(=O)Nc1ccc(Cl)cc1 InChI=1S/C15H9ClF3N3O3S/c16-10-3-5-11(6-4-10)22-26(23,24)12-7-1-9(2-8-12)13-20-14(25-21-13)15(17,18)19/h1-8,22H GJIFKHWOYWTPKS-UHFFFAOYSA-N 162819 US9056843, 110 Histone deacetylase 4 Homo sapiens 200 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162819 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162819&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230895 310304756 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305787 Fc1ccccc1NS(=O)(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C15H9F4N3O3S/c16-11-3-1-2-4-12(11)22-26(23,24)10-7-5-9(6-8-10)13-20-14(25-21-13)15(17,18)19/h1-8,22H BAQFLYLUGGEAAK-UHFFFAOYSA-N 162820 US9056843, 111 Histone deacetylase 4 Homo sapiens 290 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162820 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162820&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230688 310304757 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305788 CN(C)CCCN(C)S(=O)(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C15H19F3N4O3S/c1-21(2)9-4-10-22(3)26(23,24)12-7-5-11(6-8-12)13-19-14(25-20-13)15(16,17)18/h5-8H,4,9-10H2,1-3H3 HETPZWLRRXRTRS-UHFFFAOYSA-N 162821 US9056843, 112 Histone deacetylase 4 Homo sapiens 820 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162821 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162821&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230711 310304758 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305789 CN(C)CCCNS(=O)(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C14H17F3N4O3S/c1-21(2)9-3-8-18-25(22,23)11-6-4-10(5-7-11)12-19-13(24-20-12)14(15,16)17/h4-7,18H,3,8-9H2,1-2H3 IENSWCOQUWBZLF-UHFFFAOYSA-N 162822 US9056843, 113 Histone deacetylase 4 Homo sapiens 300 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162822 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162822&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230873 310304759 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305790 CN(C)S(=O)(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C11H10F3N3O3S/c1-17(2)21(18,19)8-5-3-7(4-6-8)9-15-10(20-16-9)11(12,13)14/h3-6H,1-2H3 BBWXDEFVCIBKHE-UHFFFAOYSA-N 162823 US9056843, 114 Histone deacetylase 4 Homo sapiens 630 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162823 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162823&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230885 310304760 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305791 CN1CCC(CNS(=O)(=O)c2ccc(cc2)-c2noc(n2)C(F)(F)F)C1 InChI=1S/C15H17F3N4O3S/c1-22-7-6-10(9-22)8-19-26(23,24)12-4-2-11(3-5-12)13-20-14(25-21-13)15(16,17)18/h2-5,10,19H,6-9H2,1H3 FCZGXHOQIVWVFD-UHFFFAOYSA-N 162824 US9056843, 115 Histone deacetylase 4 Homo sapiens 2700 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162824 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162824&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230828 310304761 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305792 OCCCNS(=O)(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C12H12F3N3O4S/c13-12(14,15)11-17-10(18-22-11)8-2-4-9(5-3-8)23(20,21)16-6-1-7-19/h2-5,16,19H,1,6-7H2 NJWYZTKOYPVYBP-UHFFFAOYSA-N 162825 US9056843, 116 Histone deacetylase 4 Homo sapiens 160 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162825 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162825&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230984 310304762 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305793 CN(C)C[C@H](Cc1ccccc1)NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C21H20F4N4O2/c1-29(2)12-15(10-13-6-4-3-5-7-13)26-19(30)16-9-8-14(11-17(16)22)18-27-20(31-28-18)21(23,24)25/h3-9,11,15H,10,12H2,1-2H3,(H,26,30)/t15-/m0/s1 IIXGHCJWHUQEEN-HNNXBMFYSA-N 162826 US9056843, 117 Histone deacetylase 4 Homo sapiens 110 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162826 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162826&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230915 310304763 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305794 CN(C)C[C@@H](Cc1ccccc1)NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C21H20F4N4O2/c1-29(2)12-15(10-13-6-4-3-5-7-13)26-19(30)16-9-8-14(11-17(16)22)18-27-20(31-28-18)21(23,24)25/h3-9,11,15H,10,12H2,1-2H3,(H,26,30)/t15-/m1/s1 IIXGHCJWHUQEEN-OAHLLOKOSA-N 162827 US9056843, 118 Histone deacetylase 4 Homo sapiens 220 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162827 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162827&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71231074 310304764 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305795 CN(C)CC(C)(C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C16H19F3N4O2/c1-15(2,9-23(3)4)21-13(24)11-7-5-10(6-8-11)12-20-14(25-22-12)16(17,18)19/h5-8H,9H2,1-4H3,(H,21,24) YBYICGLHJYBMRX-UHFFFAOYSA-N 162828 US9056843, 119 Histone deacetylase 4 Homo sapiens 36 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162828 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162828&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230907 310304765 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305796 CN(C)CC(C)(C)NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C16H18F4N4O2/c1-15(2,8-24(3)4)22-13(25)10-6-5-9(7-11(10)17)12-21-14(26-23-12)16(18,19)20/h5-7H,8H2,1-4H3,(H,22,25) RDZHZIOZCVVQSC-UHFFFAOYSA-N 162829 US9056843, 120 Histone deacetylase 4 Homo sapiens 210 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162829 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162829&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230898 310304766 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305797 CCN(CC)CC(C)NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C17H20F4N4O2/c1-4-25(5-2)9-10(3)22-15(26)12-7-6-11(8-13(12)18)14-23-16(27-24-14)17(19,20)21/h6-8,10H,4-5,9H2,1-3H3,(H,22,26) VAWWFWWPRMCDFX-UHFFFAOYSA-N 162830 US9056843, 121 Histone deacetylase 4 Homo sapiens 15 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162830 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162830&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230702 310304767 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305798 CC(CNC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F)N(C)C InChI=1S/C15H16F4N4O2/c1-8(23(2)3)7-20-13(24)10-5-4-9(6-11(10)16)12-21-14(25-22-12)15(17,18)19/h4-6,8H,7H2,1-3H3,(H,20,24) LVSPUWRCTGAYQT-UHFFFAOYSA-N 162831 US9056843, 122 Histone deacetylase 4 Homo sapiens 85 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162831 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162831&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230946 310304768 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305799 CCN(CC)CC(C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C17H21F3N4O2/c1-4-24(5-2)10-11(3)21-15(25)13-8-6-12(7-9-13)14-22-16(26-23-14)17(18,19)20/h6-9,11H,4-5,10H2,1-3H3,(H,21,25) BWCIUZLJTVXSMW-UHFFFAOYSA-N 162832 US9056843, 123 Histone deacetylase 4 Homo sapiens 7.6 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162832 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162832&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230719 310304769 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305800 C[C@H](CN(C)C)NC(=O)c1c(F)cc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C15H15F5N4O2/c1-7(6-24(2)3)21-13(25)11-9(16)4-8(5-10(11)17)12-22-14(26-23-12)15(18,19)20/h4-5,7H,6H2,1-3H3,(H,21,25)/t7-/m1/s1 MSPYLYCWIAXLPK-SSDOTTSWSA-N 162833 US9056843, 124 Histone deacetylase 4 Homo sapiens 310 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162833 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162833&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230777 310304770 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305801 C[C@H](CN(C)C)NC(=O)c1ccc(cc1Cl)-c1noc(n1)C(F)(F)F InChI=1S/C15H16ClF3N4O2/c1-8(7-23(2)3)20-13(24)10-5-4-9(6-11(10)16)12-21-14(25-22-12)15(17,18)19/h4-6,8H,7H2,1-3H3,(H,20,24)/t8-/m1/s1 OQLDBOVPKFOUAF-MRVPVSSYSA-N 162834 US9056843, 125 Histone deacetylase 4 Homo sapiens 53 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162834 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162834&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230928 310304771 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305802 CCN(CC)C[C@@H](C)NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C17H20F4N4O2/c1-4-25(5-2)9-10(3)22-15(26)12-7-6-11(8-13(12)18)14-23-16(27-24-14)17(19,20)21/h6-8,10H,4-5,9H2,1-3H3,(H,22,26)/t10-/m1/s1 VAWWFWWPRMCDFX-SNVBAGLBSA-N 162835 US9056843, 126 Histone deacetylase 4 Homo sapiens 8.9 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162835 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162835&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230887 310304772 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305803 CCN(CC)C[C@H](C)NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C17H20F4N4O2/c1-4-25(5-2)9-10(3)22-15(26)12-7-6-11(8-13(12)18)14-23-16(27-24-14)17(19,20)21/h6-8,10H,4-5,9H2,1-3H3,(H,22,26)/t10-/m0/s1 VAWWFWWPRMCDFX-JTQLQIEISA-N 162836 US9056843, 127 Histone deacetylase 4 Homo sapiens 44 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162836 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162836&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230701 310304773 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305804 C[C@H](CN1CCCC1)NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C17H18F4N4O2/c1-10(9-25-6-2-3-7-25)22-15(26)12-5-4-11(8-13(12)18)14-23-16(27-24-14)17(19,20)21/h4-5,8,10H,2-3,6-7,9H2,1H3,(H,22,26)/t10-/m1/s1 PXMISIRKDSDEBN-SNVBAGLBSA-N 162837 US9056843, 128 Histone deacetylase 4 Homo sapiens 26 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162837 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162837&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230979 310304774 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305805 C[C@H](CN1CCCCC1)NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C18H20F4N4O2/c1-11(10-26-7-3-2-4-8-26)23-16(27)13-6-5-12(9-14(13)19)15-24-17(28-25-15)18(20,21)22/h5-6,9,11H,2-4,7-8,10H2,1H3,(H,23,27)/t11-/m1/s1 OHIUPIMOMLQZKN-LLVKDONJSA-N 162838 US9056843, 129 Histone deacetylase 4 Homo sapiens 13 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162838 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162838&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230809 310304775 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305806 C[C@H](CN1CCCC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C17H19F3N4O2/c1-11(10-24-8-2-3-9-24)21-15(25)13-6-4-12(5-7-13)14-22-16(26-23-14)17(18,19)20/h4-7,11H,2-3,8-10H2,1H3,(H,21,25)/t11-/m1/s1 GPAXDYNOSUVDDO-LLVKDONJSA-N 162839 US9056843, 130 Histone deacetylase 4 Homo sapiens 11 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162839 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162839&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230767 310304776 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305807 C[C@H](CN1CCCCC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C18H21F3N4O2/c1-12(11-25-9-3-2-4-10-25)22-16(26)14-7-5-13(6-8-14)15-23-17(27-24-15)18(19,20)21/h5-8,12H,2-4,9-11H2,1H3,(H,22,26)/t12-/m1/s1 WTZFUFARAWDPGC-GFCCVEGCSA-N 162840 US9056843, 131 Histone deacetylase 4 Homo sapiens 10 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162840 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162840&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230957 310304777 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305808 CCN(CC)C[C@@H](C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C17H21F3N4O2/c1-4-24(5-2)10-11(3)21-15(25)13-8-6-12(7-9-13)14-22-16(26-23-14)17(18,19)20/h6-9,11H,4-5,10H2,1-3H3,(H,21,25)/t11-/m1/s1 BWCIUZLJTVXSMW-LLVKDONJSA-N 162841 US9056843, 132 Histone deacetylase 4 Homo sapiens 5 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162841 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162841&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230900 310304778 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305809 CCN(CC)C[C@H](NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F)C(C)C InChI=1S/C19H25F3N4O2/c1-5-26(6-2)11-15(12(3)4)23-17(27)14-9-7-13(8-10-14)16-24-18(28-25-16)19(20,21)22/h7-10,12,15H,5-6,11H2,1-4H3,(H,23,27)/t15-/m0/s1 XWILVJLRPDEIMI-HNNXBMFYSA-N 162843 US9056843, 134 Histone deacetylase 4 Homo sapiens 9.8 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162843 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162843&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230857 310304780 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305810 CCN(CC)C[C@H](NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F)C(C)C InChI=1S/C19H24F4N4O2/c1-5-27(6-2)10-15(11(3)4)24-17(28)13-8-7-12(9-14(13)20)16-25-18(29-26-16)19(21,22)23/h7-9,11,15H,5-6,10H2,1-4H3,(H,24,28)/t15-/m0/s1 IQTWKGODRCNBRQ-HNNXBMFYSA-N 162844 US9056843, 135 Histone deacetylase 4 Homo sapiens 10 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162844 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162844&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71231063 310304781 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305811 CCN(C)C[C@@H](C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C16H19F3N4O2/c1-4-23(3)9-10(2)20-14(24)12-7-5-11(6-8-12)13-21-15(25-22-13)16(17,18)19/h5-8,10H,4,9H2,1-3H3,(H,20,24)/t10-/m1/s1 CJEZHYMNVHWABM-SNVBAGLBSA-N 162845 US9056843, 136 Histone deacetylase 4 Homo sapiens 8.9 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162845 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162845&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71231832 310304782 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305812 CCCN(CCC)C[C@@H](C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C19H25F3N4O2/c1-4-10-26(11-5-2)12-13(3)23-17(27)15-8-6-14(7-9-15)16-24-18(28-25-16)19(20,21)22/h6-9,13H,4-5,10-12H2,1-3H3,(H,23,27)/t13-/m1/s1 HMXFCVJIASWKMB-CYBMUJFWSA-N 162846 US9056843, 137 Histone deacetylase 4 Homo sapiens 0.97 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162846 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162846&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230790 310304783 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305813 C[C@H](CN(C)C(C)C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C17H21F3N4O2/c1-10(2)24(4)9-11(3)21-15(25)13-7-5-12(6-8-13)14-22-16(26-23-14)17(18,19)20/h5-8,10-11H,9H2,1-4H3,(H,21,25)/t11-/m1/s1 MRBOCCFMPAZCHO-LLVKDONJSA-N 162847 US9056843, 138 Histone deacetylase 4 Homo sapiens 4.5 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162847 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162847&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230799 310304784 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305814 CCCN(C)C[C@@H](C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C17H21F3N4O2/c1-4-9-24(3)10-11(2)21-15(25)13-7-5-12(6-8-13)14-22-16(26-23-14)17(18,19)20/h5-8,11H,4,9-10H2,1-3H3,(H,21,25)/t11-/m1/s1 CBKPEONLDRDXEZ-LLVKDONJSA-N 162848 US9056843, 139 Histone deacetylase 4 Homo sapiens 1 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162848 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162848&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230864 310304785 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305815 CCCN(CCC)C[C@@H](C)NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C19H24F4N4O2/c1-4-8-27(9-5-2)11-12(3)24-17(28)14-7-6-13(10-15(14)20)16-25-18(29-26-16)19(21,22)23/h6-7,10,12H,4-5,8-9,11H2,1-3H3,(H,24,28)/t12-/m1/s1 GSSWPNVQSNAXRF-GFCCVEGCSA-N 162850 US9056843, 141 Histone deacetylase 4 Homo sapiens 1.4 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162850 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162850&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230938 310304787 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305816 C[C@H](CN(C)C(C)C)NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C17H20F4N4O2/c1-9(2)25(4)8-10(3)22-15(26)12-6-5-11(7-13(12)18)14-23-16(27-24-14)17(19,20)21/h5-7,9-10H,8H2,1-4H3,(H,22,26)/t10-/m1/s1 XIDHNMBDXJJOCG-SNVBAGLBSA-N 162851 US9056843, 142 Histone deacetylase 4 Homo sapiens 7.2 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162851 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162851&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90149763 310304788 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305817 CCCN(C)C[C@@H](C)NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C17H20F4N4O2/c1-4-7-25(3)9-10(2)22-15(26)12-6-5-11(8-13(12)18)14-23-16(27-24-14)17(19,20)21/h5-6,8,10H,4,7,9H2,1-3H3,(H,22,26)/t10-/m1/s1 OBJZEJYAHAWEPJ-SNVBAGLBSA-N 162852 US9056843, 143 Histone deacetylase 4 Homo sapiens 1.2 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162852 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162852&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230937 310304789 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305818 CC(CN(C)C)N(C)C(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C16H18F4N4O2/c1-9(8-23(2)3)24(4)14(25)11-6-5-10(7-12(11)17)13-21-15(26-22-13)16(18,19)20/h5-7,9H,8H2,1-4H3 CFSZGVBQVHHAJP-UHFFFAOYSA-N 162853 US9056843, 144 Histone deacetylase 4 Homo sapiens 180 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162853 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162853&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230862 310304790 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305819 CCCN(CC)C[C@@H](C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C18H23F3N4O2/c1-4-10-25(5-2)11-12(3)22-16(26)14-8-6-13(7-9-14)15-23-17(27-24-15)18(19,20)21/h6-9,12H,4-5,10-11H2,1-3H3,(H,22,26)/t12-/m1/s1 MZANSCGRZGFLKJ-GFCCVEGCSA-N 162854 US9056843, 145 Histone deacetylase 4 Homo sapiens 0.75 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162854 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162854&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230806 310304791 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305820 CCCN(CC)C[C@@H](C)NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C18H22F4N4O2/c1-4-8-26(5-2)10-11(3)23-16(27)13-7-6-12(9-14(13)19)15-24-17(28-25-15)18(20,21)22/h6-7,9,11H,4-5,8,10H2,1-3H3,(H,23,27)/t11-/m1/s1 HPKMFYOAMOHAPX-LLVKDONJSA-N 162855 US9056843, 146 Histone deacetylase 4 Homo sapiens 1.6 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162855 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162855&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230819 310304792 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305821 C[C@H](CN1CCOCC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C17H19F3N4O3/c1-11(10-24-6-8-26-9-7-24)21-15(25)13-4-2-12(3-5-13)14-22-16(27-23-14)17(18,19)20/h2-5,11H,6-10H2,1H3,(H,21,25)/t11-/m1/s1 VQZSNKRVEFQCIK-LLVKDONJSA-N 162856 US9056843, 147 Histone deacetylase 4 Homo sapiens 300 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162856 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162856&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230852 310304793 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305822 C[C@H](CN1CCOCC1)NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C17H18F4N4O3/c1-10(9-25-4-6-27-7-5-25)22-15(26)12-3-2-11(8-13(12)18)14-23-16(28-24-14)17(19,20)21/h2-3,8,10H,4-7,9H2,1H3,(H,22,26)/t10-/m1/s1 ZSFASTLMALEKOU-SNVBAGLBSA-N 162857 US9056843, 148 Histone deacetylase 4 Homo sapiens 380 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162857 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162857&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230841 310304794 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305823 CN1CCCC(C1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C16H17F3N4O2/c1-23-8-2-3-12(9-23)20-14(24)11-6-4-10(5-7-11)13-21-15(25-22-13)16(17,18)19/h4-7,12H,2-3,8-9H2,1H3,(H,20,24) LCPPNVATQMMHLI-UHFFFAOYSA-N 162858 US9056843, 149 Histone deacetylase 4 Homo sapiens 140 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162858 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162858&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230892 310304795 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305824 CCCCN(C)C[C@@H](C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C18H23F3N4O2/c1-4-5-10-25(3)11-12(2)22-16(26)14-8-6-13(7-9-14)15-23-17(27-24-15)18(19,20)21/h6-9,12H,4-5,10-11H2,1-3H3,(H,22,26)/t12-/m1/s1 WXLBRYDDTZHKQD-GFCCVEGCSA-N 162859 US9056843, 150 Histone deacetylase 4 Homo sapiens 1.1 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162859 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162859&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71231827 310304796 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305825 CCCCN(C)C[C@@H](C)NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F InChI=1S/C18H22F4N4O2/c1-4-5-8-26(3)10-11(2)23-16(27)13-7-6-12(9-14(13)19)15-24-17(28-25-15)18(20,21)22/h6-7,9,11H,4-5,8,10H2,1-3H3,(H,23,27)/t11-/m1/s1 JGZQUKKFHYQNLD-LLVKDONJSA-N 162860 US9056843, 151 Histone deacetylase 4 Homo sapiens 1.8 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162860 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162860&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230924 310304797 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305826 CCN(C[C@@H](C)NC(=O)c1ccc(cc1F)-c1noc(n1)C(F)(F)F)C(C)C InChI=1S/C18H22F4N4O2/c1-5-26(10(2)3)9-11(4)23-16(27)13-7-6-12(8-14(13)19)15-24-17(28-25-15)18(20,21)22/h6-8,10-11H,5,9H2,1-4H3,(H,23,27)/t11-/m1/s1 NITIVAZXKWXNAT-LLVKDONJSA-N 162861 US9056843, 152 Histone deacetylase 4 Homo sapiens 8.4 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162861 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162861&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90149775 310304798 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305827 CN1CC[C@H](C1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C15H15F3N4O2/c1-22-7-6-11(8-22)19-13(23)10-4-2-9(3-5-10)12-20-14(24-21-12)15(16,17)18/h2-5,11H,6-8H2,1H3,(H,19,23)/t11-/m1/s1 GCYGDWWBMNPQIH-LLVKDONJSA-N 162862 US9056843, 153 Histone deacetylase 4 Homo sapiens 3.6 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162862 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162862&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230996 310304799 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305828 CN1CCC[C@H](C1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C16H17F3N4O2/c1-23-8-2-3-12(9-23)20-14(24)11-6-4-10(5-7-11)13-21-15(25-22-13)16(17,18)19/h4-7,12H,2-3,8-9H2,1H3,(H,20,24)/t12-/m1/s1 LCPPNVATQMMHLI-GFCCVEGCSA-N 162863 US9056843, 154 Histone deacetylase 4 Homo sapiens 110 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162863 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162863&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230999 310304800 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305829 CCN(CC)CCNC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C16H19F3N4O2/c1-3-23(4-2)10-9-20-14(24)12-7-5-11(6-8-12)13-21-15(25-22-13)16(17,18)19/h5-8H,3-4,9-10H2,1-2H3,(H,20,24) PZAVITOFPPUOOH-UHFFFAOYSA-N 162864 US9056843, 155 Histone deacetylase 4 Homo sapiens 12 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162864 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162864&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230837 310304801 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305830 C[C@H](CN(C)Cc1ccccc1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C21H21F3N4O2/c1-14(12-28(2)13-15-6-4-3-5-7-15)25-19(29)17-10-8-16(9-11-17)18-26-20(30-27-18)21(22,23)24/h3-11,14H,12-13H2,1-2H3,(H,25,29)/t14-/m1/s1 RESDVUQVZOJNSO-CQSZACIVSA-N 162865 US9056843, 156 Histone deacetylase 4 Homo sapiens 0.85 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162865 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162865&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230992 310304802 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305831 CNCCNC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C13H13F3N4O2/c1-17-6-7-18-11(21)9-4-2-8(3-5-9)10-19-12(22-20-10)13(14,15)16/h2-5,17H,6-7H2,1H3,(H,18,21) CNYMWZQRODJNQU-UHFFFAOYSA-N 162866 US9056843, 157 Histone deacetylase 4 Homo sapiens 40 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162866 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162866&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230826 310304803 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 305832 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NCCNc1ccccc1 InChI=1S/C18H15F3N4O2/c19-18(20,21)17-24-15(25-27-17)12-6-8-13(9-7-12)16(26)23-11-10-22-14-4-2-1-3-5-14/h1-9,22H,10-11H2,(H,23,26) DSUWXSUDZATUMM-UHFFFAOYSA-N 162867 US9056843, 158 Histone deacetylase 4 Homo sapiens 360 8 25.00 C US Patent 10.7270/Q24F1PG8 aid1801322 US9056843 Hebach, C; Joly, E; Kallen, J; Ternois, JG; Tintelnot-Blomley, M Novartis AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162867 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162867&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230968 310304804 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 306621 CCCCNNC(=O)c1ccc(Br)cc1 InChI=1S/C11H15BrN2O/c1-2-3-8-13-14-11(15)9-4-6-10(12)7-5-9/h4-7,13H,2-3,8H2,1H3,(H,14,15) BVQCFCYPFJOOAV-UHFFFAOYSA-N 163619 UF010::US10807944, Compound UF010 Histone deacetylase 4 Homo sapiens >1.00e+5 8 Curated from the literature by BindingDB 10.1016/j.chembiol.2014.12.015 10.7270/Q2TX3D48 25699604 aid1801335 Wang, Y; Stowe, RL; Pinello, CE; Tian, G; Madoux, F; Li, D; Zhao, LY; Li, JL; Wang, Y; Wang, Y; Ma, H; Hodder, P; Roush, WR; Liao, D University of Florida College of Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=163619 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=163619&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4596836 310305336 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 324007 Cc1[nH]c2ccccc2c1CCNCc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C21H23N3O2/c1-15-18(19-4-2-3-5-20(19)23-15)12-13-22-14-17-8-6-16(7-9-17)10-11-21(25)24-26/h2-11,22-23,26H,12-14H2,1H3,(H,24,25)/b11-10+ FPOHNWQLNRZRFC-ZHACJKMWSA-N 29589 Faridak::LBH-589::LBH-589B::Panobinostat::US10722597, Compound Panobinostat Histone deacetylase 4 Homo sapiens 373 7.4 25.00 C Curated from the literature by BindingDB 10.1021/acschembio.5b00640 10.7270/Q2BZ64T2 26640968 aid1801572 Wagner, FF; Lundh, M; Kaya, T; McCarren, P; Zhang, YL; Chattopadhyay, S; Gale, JP; Galbo, T; Fisher, SL; Meier, BC; Vetere, A; Richardson, S; Morgan, NG; Christensen, DP; Gilbert, TJ; Hooker, JM; Leroy, M; Walpita, D; Mandrup-Poulsen, T; Wagner, BK; Holson, EB Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=29589 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=29589&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search LBH 5EF8 6918837 81055018 ZINC22010649 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 324016 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >3.33e+4 7.4 25.00 C Curated from the literature by BindingDB 10.1021/acschembio.5b00640 10.7270/Q2BZ64T2 26640968 aid1801572 Wagner, FF; Lundh, M; Kaya, T; McCarren, P; Zhang, YL; Chattopadhyay, S; Gale, JP; Galbo, T; Fisher, SL; Meier, BC; Vetere, A; Richardson, S; Morgan, NG; Christensen, DP; Gilbert, TJ; Hooker, JM; Leroy, M; Walpita, D; Mandrup-Poulsen, T; Wagner, BK; Holson, EB Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 324022 CC(=O)Nc1ccc(cc1)C(=O)Nc1ccccc1N InChI=1S/C15H15N3O2/c1-10(19)17-12-8-6-11(7-9-12)15(20)18-14-5-3-2-4-13(14)16/h2-9H,16H2,1H3,(H,17,19)(H,18,20) VAZAPHZUAVEOMC-UHFFFAOYSA-N 19422 4-(acetylamino)-N-(2-amino-phenyl) benzamide::CI-994::N-(2-aminophenyl)-4-acetamidobenzamide::N-acetyldinaline::US11207431, Example F::US11377423, CI-994 Histone deacetylase 4 Homo sapiens >3.33e+4 7.4 25.00 C Curated from the literature by BindingDB 10.1021/acschembio.5b00640 10.7270/Q2BZ64T2 26640968 aid1801572 Wagner, FF; Lundh, M; Kaya, T; McCarren, P; Zhang, YL; Chattopadhyay, S; Gale, JP; Galbo, T; Fisher, SL; Meier, BC; Vetere, A; Richardson, S; Morgan, NG; Christensen, DP; Gilbert, TJ; Hooker, JM; Leroy, M; Walpita, D; Mandrup-Poulsen, T; Wagner, BK; Holson, EB Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19422 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19422&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 2746 46519444 ZINC00003803 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 324028 CC(=O)Nc1ccc(cc1)C(=O)Nc1cc(ccc1N)-c1ccncc1 InChI=1S/C20H18N4O2/c1-13(25)23-17-5-2-15(3-6-17)20(26)24-19-12-16(4-7-18(19)21)14-8-10-22-11-9-14/h2-12H,21H2,1H3,(H,23,25)(H,24,26) BBHURYMVPMFILR-UHFFFAOYSA-N 178095 BRD2492 Histone deacetylase 4 Homo sapiens >3.33e+4 7.4 25.00 C Curated from the literature by BindingDB 10.1021/acschembio.5b00640 10.7270/Q2BZ64T2 26640968 aid1801572 Wagner, FF; Lundh, M; Kaya, T; McCarren, P; Zhang, YL; Chattopadhyay, S; Gale, JP; Galbo, T; Fisher, SL; Meier, BC; Vetere, A; Richardson, S; Morgan, NG; Christensen, DP; Gilbert, TJ; Hooker, JM; Leroy, M; Walpita, D; Mandrup-Poulsen, T; Wagner, BK; Holson, EB Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=178095 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=178095&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118987449 313063486 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 324034 CC(=O)Nc1ccc(cc1)C(=O)Nc1ccc(F)cc1N InChI=1S/C15H14FN3O2/c1-9(20)18-12-5-2-10(3-6-12)15(21)19-14-7-4-11(16)8-13(14)17/h2-8H,17H2,1H3,(H,18,20)(H,19,21) RRJDFENBXIEAPD-UHFFFAOYSA-N 178100 BRD3308::US11377423, Cmpd 1 Histone deacetylase 4 Homo sapiens >3.33e+4 7.4 25.00 C Curated from the literature by BindingDB 10.1021/acschembio.5b00640 10.7270/Q2BZ64T2 26640968 aid1801572 Wagner, FF; Lundh, M; Kaya, T; McCarren, P; Zhang, YL; Chattopadhyay, S; Gale, JP; Galbo, T; Fisher, SL; Meier, BC; Vetere, A; Richardson, S; Morgan, NG; Christensen, DP; Gilbert, TJ; Hooker, JM; Leroy, M; Walpita, D; Mandrup-Poulsen, T; Wagner, BK; Holson, EB Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=178100 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=178100&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72734382 313063491 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 338342 CCN1CCN(CC1)C(c1cccnc1)c1cc(Cl)c2cccnc2c1O InChI=1S/C21H23ClN4O/c1-2-25-9-11-26(12-10-25)20(15-5-3-7-23-14-15)17-13-18(22)16-6-4-8-24-19(16)21(17)27/h3-8,13-14,20,27H,2,9-12H2,1H3 XAFSFXYJOJWLJD-UHFFFAOYSA-N 49152 5-chloranyl-7-[(4-ethylpiperazin-1-yl)-pyridin-3-yl-methyl]quinolin-8-ol::5-chloro-7-[(4-ethyl-1-piperazinyl)-(3-pyridinyl)methyl]-8-quinolinol::5-chloro-7-[(4-ethylpiperazin-1-yl)-pyridin-3-ylmethyl]quinolin-8-ol::5-chloro-7-[(4-ethylpiperazino)-(3-pyridyl)methyl]quinolin-8-ol::BRD4354::MLS000564806::SMR000151966::cid_3516032 Histone deacetylase 4 Homo sapiens 1.38e+4 7.4 Curated from the literature by BindingDB 10.1021/acschembio.6b00012 10.7270/Q2QF8RPQ 27064299 aid1801789 Boskovic, ZV; Kemp, MM; Freedy, AM; Viswanathan, VS; Pop, MS; Fuller, JH; Martinez, NM; Figueroa Lazú, SO; Hong, JA; Lewis, TA; Calarese, D; Love, JD; Vetere, A; Almo, SC; Schreiber, SL; Koehler, AN Broad Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=49152 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=49152&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 3516032 252629433 ZINC21486915 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 342809 COc1cc2c(Oc3ccc(NC(=O)C4(CC4)C(=O)Nc4ccc(F)cc4)cc3F)ccnc2cc1OCCCC(=O)NO InChI=1S/C31H28F2N4O7/c1-42-26-16-21-23(17-27(26)43-14-2-3-28(38)37-41)34-13-10-24(21)44-25-9-8-20(15-22(25)33)36-30(40)31(11-12-31)29(39)35-19-6-4-18(32)5-7-19/h4-10,13,15-17,41H,2-3,11-12,14H2,1H3,(H,35,39)(H,36,40)(H,37,38) LYXOBSREVZDKST-UHFFFAOYSA-N 191640 US9186318, 9 Histone deacetylase 4 Homo sapiens >10000 US Patent 10.7270/Q2ZP44XG aid1801877 US9186318 Yun, Z; Wang, H Beijing Konruns Pharmaceutical Co., Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=191640 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=191640&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71466525 317222916 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 342820 COc1cc2c(Oc3ccc(NC(=O)C4(CC4)C(=O)Nc4ccc(F)cc4)cc3F)ccnc2cc1OCCCCCC(=O)NO InChI=1S/C33H32F2N4O7/c1-44-28-18-23-25(19-29(28)45-16-4-2-3-5-30(40)39-43)36-15-12-26(23)46-27-11-10-22(17-24(27)35)38-32(42)33(13-14-33)31(41)37-21-8-6-20(34)7-9-21/h6-12,15,17-19,43H,2-5,13-14,16H2,1H3,(H,37,41)(H,38,42)(H,39,40) CDTJUAMUMLOLCG-UHFFFAOYSA-N 191641 US9186318, 13 Histone deacetylase 4 Homo sapiens >10000 US Patent 10.7270/Q2ZP44XG aid1801877 US9186318 Yun, Z; Wang, H Beijing Konruns Pharmaceutical Co., Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=191641 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=191641&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71466592 317222917 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 351789 ONC(=O)\C=C\c1cccc(c1)S(=O)(=O)N[C@H](C(=O)Nc1cccc2ccccc12)c1ccccc1 InChI=1S/C27H23N3O5S/c31-25(29-33)17-16-19-8-6-13-22(18-19)36(34,35)30-26(21-10-2-1-3-11-21)27(32)28-24-15-7-12-20-9-4-5-14-23(20)24/h1-18,26,30,33H,(H,28,32)(H,29,31)/b17-16+/t26-/m0/s1 JCEFNCFZXQDHRY-ZOGILVBSSA-N 198192 (S,E)-N-hydroxy-3-(3-(N-(2-(naphthalen-1-ylamino)-2-oxo-1-phenylethyl)sulfamoyl)phenyl)acrylamide (10s) Histone deacetylase 4 Homo sapiens 23000 Curated from the literature by BindingDB 10.1111/cbdd.12787 10.7270/Q2D50KSD 27235003 aid1802061 Li, J; Li, X; Wang, X; Hou, J; Zang, J; Gao, S; Xu, W; Zhang, Y Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=198192 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=198192&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122198640 318489264 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 351790 ONC(=O)\C=C\c1cccc(c1)S(=O)(=O)Nc1ccccc1 InChI=1S/C15H14N2O4S/c18-15(16-19)10-9-12-5-4-8-14(11-12)22(20,21)17-13-6-2-1-3-7-13/h1-11,17,19H,(H,16,18)/b10-9+ NCNRHFGMJRPRSK-MDZDMXLPSA-N 25150 (2E)-N-hydroxy-3-[3-(phenylsulfamoyl)phenyl]prop-2-enamide::Belinosta::Belinostat::PXD-101::PXD101 Histone deacetylase 4 Homo sapiens 9850 Curated from the literature by BindingDB 10.1111/cbdd.12787 10.7270/Q2D50KSD 27235003 aid1802061 Li, J; Li, X; Wang, X; Hou, J; Zang, J; Gao, S; Xu, W; Zhang, Y Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25150 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25150&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5OG 5EEN 6918638 56374291 61076 ZINC03818726 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 350481 C[C@H](\C=C\C(=O)NO)\C=C(/C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20)/b10-5+,13-11+/t12-/m1/s1 ALCVRKZFLFWUAZ-LSSUCPAZSA-N 197336 R-TSA Histone deacetylase 4 Homo sapiens 9613 Curated from the literature by BindingDB 10.1038/nchembio.2140 10.7270/Q2V986V6 27454931 aid1802036 Miyake, Y; Keusch, JJ; Wang, L; Saito, M; Hess, D; Wang, X; Melancon, BJ; Helquist, P; Gut, H; Matthias, P Friedrich Miescher Institute for Biomedical Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=197336 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=197336&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122198565 318488484 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 350482 C[C@@H](\C=C\C(=O)NO)\C=C(/C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20)/b10-5+,13-11+/t12-/m0/s1 ALCVRKZFLFWUAZ-CSFUQHBASA-N 197337 S-TSA Histone deacetylase 4 Homo sapiens 6341 Curated from the literature by BindingDB 10.1038/nchembio.2140 10.7270/Q2V986V6 27454931 aid1802036 Miyake, Y; Keusch, JJ; Wang, L; Saito, M; Hess, D; Wang, X; Melancon, BJ; Helquist, P; Gut, H; Matthias, P Friedrich Miescher Institute for Biomedical Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=197337 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=197337&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122198566 318488485 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 365015 Cc1ccc(NC(=O)[C@@H](NC(=O)c2ccc(cc2)C(=O)NO)c2c[nH]c3ccccc23)cc1 206287 (S)-N1-(3-(1H-indol-3-yl)-1-oxo-1-(p-tolylamino)propan-2-yl)-N4-hydroxyterephthalamide (12m) Histone deacetylase 4 Homo sapiens >1.00e+5 Curated from the literature by BindingDB 10.1111/cbdd.12819 10.7270/Q2SQ8Z69 27416889 aid1802240 Wang, X; Li, X; Li, J; Hou, J; Qu, Y; Yu, C; He, F; Xu, W; Wu, J Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=206287 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=206287&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 123131719 321901845 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 365020 ONC(=O)\C=C\c1cccc(c1)S(=O)(=O)Nc1ccccc1 InChI=1S/C15H14N2O4S/c18-15(16-19)10-9-12-5-4-8-14(11-12)22(20,21)17-13-6-2-1-3-7-13/h1-11,17,19H,(H,16,18)/b10-9+ NCNRHFGMJRPRSK-MDZDMXLPSA-N 25150 (2E)-N-hydroxy-3-[3-(phenylsulfamoyl)phenyl]prop-2-enamide::Belinosta::Belinostat::PXD-101::PXD101 Histone deacetylase 4 Homo sapiens 9.9e+3 Curated from the literature by BindingDB 10.1111/cbdd.12819 10.7270/Q2SQ8Z69 27416889 aid1802240 Wang, X; Li, X; Li, J; Hou, J; Qu, Y; Yu, C; He, F; Xu, W; Wu, J Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25150 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25150&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5OG 5EEN 6918638 56374291 61076 ZINC03818726 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 372462 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >5.0e+4 8 4.00 C Curated from the literature by BindingDB 10.1021/acschembio.6b00776 10.7270/Q23R0RQN 27977115 aid1802356 Nalawansha, DA; Pflum, MK Wayne State University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 372463 CC(=O)Nc1ccc(cc1)C(=O)Nc1cc(ccc1N)-c1cccs1 InChI=1S/C19H17N3O2S/c1-12(23)21-15-7-4-13(5-8-15)19(24)22-17-11-14(6-9-16(17)20)18-3-2-10-25-18/h2-11H,20H2,1H3,(H,21,23)(H,22,24) ABZSPJVXTTUFAA-UHFFFAOYSA-N 19423 HDAC inhibitor, Compound 1::N-[2-amino-5-(thiophen-2-yl)phenyl]-4-acetamidobenzamide::N-[2-amino-5-(thiophen-2-yl)phenyl]-4-acetamidobenzamide (60)::SHI-1:2::benzamide-type inhibitor, 19 Histone deacetylase 4 Homo sapiens >1.0e+4 8 4.00 C Curated from the literature by BindingDB 10.1021/acschembio.6b00776 10.7270/Q23R0RQN 27977115 aid1802356 Nalawansha, DA; Pflum, MK Wayne State University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19423 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19423&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 20Y 4LY1 6918878 46519445 ZINC14970815 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 372464 CN1CCc2c(C1)c1ccccc1n2Cc1ccc(cc1)C(=O)NO InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::Tubastatin A::US10227295, Compound Tubastatin A::US10456394, Tubastatin A::US11207431, Example D::US8748451, 6::US9249087, Tubacin::US9751832, Tubastatin A::US9956192, Compound Tubastatin-A Histone deacetylase 4 Homo sapiens >3.0e+4 8 4.00 C Curated from the literature by BindingDB 10.1021/acschembio.6b00776 10.7270/Q23R0RQN 27977115 aid1802356 Nalawansha, DA; Pflum, MK Wayne State University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 ZINC51951670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 366808 Cc1ccc(NC(=O)CCCCCC(=O)Nc2ccccc2N)cc1 InChI=1S/C20H25N3O2/c1-15-11-13-16(14-12-15)22-19(24)9-3-2-4-10-20(25)23-18-8-6-5-7-17(18)21/h5-8,11-14H,2-4,9-10,21H2,1H3,(H,22,24)(H,23,25) WTKBRPXPNAKVEQ-UHFFFAOYSA-N 207628 US9265734, RGFA8::US9796664, Compound RGFA8 Histone deacetylase 4 Homo sapiens >100000 US Patent 10.7270/Q2BK1B5B aid1802268 US9265734 Rusche, JR; Peet, NP; Hopper, AT BioMarin Pharmaceutical Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=207628 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=207628&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 16070100 322058197 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 366818 C[C@H](\C=C(/C)\C=C\C(=O)NO)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1 RTKIYFITIVXBLE-QEQCGCAPSA-N 50005711 CHEBI:46024::GNF-Pf-1011::TRICHOSTATIN::Trichostatin A::Trichostatin A (TSA)::US10011611, Trichostatin A::US10722597, Compound Trichostatin::US11535598, Compound Trichostatin A::US9265734, TSA Histone deacetylase 4 Homo sapiens 34.8 US Patent 10.7270/Q2BK1B5B aid1802268 US9265734 Rusche, JR; Peet, NP; Hopper, AT BioMarin Pharmaceutical Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 444732 242056952 DB04297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 377200 Oc1c(I)cc(Cl)c2cccnc12 InChI=1S/C9H5ClINO/c10-6-4-7(11)9(13)8-5(6)2-1-3-12-8/h1-4,13H QCDFBFJGMNKBDO-UHFFFAOYSA-N 32188 CLIOQUINOL::Clioquinol (CQ)::TG2-36-2::cid_2788 Histone deacetylase 4 Homo sapiens 3.11e+4 8 Curated from the literature by BindingDB 10.1074/jbc.M113.472563 10.7270/Q2668C1K 24114842 aid1802451 Cao, B; Li, J; Zhu, J; Shen, M; Han, K; Zhang, Z; Yu, Y; Wang, Y; Wu, D; Chen, S; Sun, A; Tang, X; Zhao, Y; Qiao, C; Hou, T; Mao, X Soochow University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=32188 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=32188&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search CQL 3KCX 2788 252615638 74460 DB04815 ZINC06409735 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 377207 Oc1c(I)cc(Cl)c2cccnc12 InChI=1S/C9H5ClINO/c10-6-4-7(11)9(13)8-5(6)2-1-3-12-8/h1-4,13H QCDFBFJGMNKBDO-UHFFFAOYSA-N 32188 CLIOQUINOL::Clioquinol (CQ)::TG2-36-2::cid_2788 Histone deacetylase 4 Homo sapiens 5.24e+4 8 Curated from the literature by BindingDB 10.1074/jbc.M113.472563 10.7270/Q2668C1K 24114842 aid1802451 Cao, B; Li, J; Zhu, J; Shen, M; Han, K; Zhang, Z; Yu, Y; Wang, Y; Wu, D; Chen, S; Sun, A; Tang, X; Zhao, Y; Qiao, C; Hou, T; Mao, X Soochow University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=32188 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=32188&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search CQL 3KCX 2788 252615638 74460 DB04815 ZINC06409735 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 377215 C[C@H](\C=C(/C)\C=C\C(=O)NO)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1 RTKIYFITIVXBLE-QEQCGCAPSA-N 50005711 CHEBI:46024::GNF-Pf-1011::TRICHOSTATIN::Trichostatin A::Trichostatin A (TSA)::US10011611, Trichostatin A::US10722597, Compound Trichostatin::US11535598, Compound Trichostatin A::US9265734, TSA Histone deacetylase 4 Homo sapiens 3.23e+3 8 Curated from the literature by BindingDB 10.1074/jbc.M113.472563 10.7270/Q2668C1K 24114842 aid1802451 Cao, B; Li, J; Zhu, J; Shen, M; Han, K; Zhang, Z; Yu, Y; Wang, Y; Wu, D; Chen, S; Sun, A; Tang, X; Zhao, Y; Qiao, C; Hou, T; Mao, X Soochow University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 444732 242056952 DB04297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 374952 Nc1ccccc1NC(=O)c1ccc(CNC(=O)OCc2cccnc2)cc1 InChI=1S/C21H20N4O3/c22-18-5-1-2-6-19(18)25-20(26)17-9-7-15(8-10-17)13-24-21(27)28-14-16-4-3-11-23-12-16/h1-12H,13-14,22H2,(H,24,27)(H,25,26) INVTYAOGFAGBOE-UHFFFAOYSA-N 19410 CHEMBL27759::MS-275::US11377423, MS-275::US11672788, Compound Entinostat::US9265734, MS-275::US9796664, Compound MS-275::benzamide-type inhibitor, 3::pyridin-3-ylmethyl N-({4-[(2-aminophenyl)carbamoyl]phenyl}methyl)carbamate Histone deacetylase 4 Homo sapiens >1.0e+4 7.5 Curated from the literature by BindingDB 10.1074/jbc.M113.490706 10.7270/Q2KK99MZ 23897821 aid1802398 Lauffer, BE; Mintzer, R; Fong, R; Mukund, S; Tam, C; Zilberleyb, I; Flicke, B; Ritscher, A; Fedorowicz, G; Vallero, R; Ortwine, DF; Gunzner, J; Modrusan, Z; Neumann, L; Koth, CM; Lupardus, PJ; Kaminker, JS; Heise, CE; Steiner, P Genentech Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19410 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19410&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4261 46519433 CHEMBL27759 7007 ZINC01488870 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 374953 CC(=O)Nc1ccc(cc1)C(=O)Nc1cc(ccc1N)-c1cccs1 InChI=1S/C19H17N3O2S/c1-12(23)21-15-7-4-13(5-8-15)19(24)22-17-11-14(6-9-16(17)20)18-3-2-10-25-18/h2-11H,20H2,1H3,(H,21,23)(H,22,24) ABZSPJVXTTUFAA-UHFFFAOYSA-N 19423 HDAC inhibitor, Compound 1::N-[2-amino-5-(thiophen-2-yl)phenyl]-4-acetamidobenzamide::N-[2-amino-5-(thiophen-2-yl)phenyl]-4-acetamidobenzamide (60)::SHI-1:2::benzamide-type inhibitor, 19 Histone deacetylase 4 Homo sapiens >1.0e+4 7.5 Curated from the literature by BindingDB 10.1074/jbc.M113.490706 10.7270/Q2KK99MZ 23897821 aid1802398 Lauffer, BE; Mintzer, R; Fong, R; Mukund, S; Tam, C; Zilberleyb, I; Flicke, B; Ritscher, A; Fedorowicz, G; Vallero, R; Ortwine, DF; Gunzner, J; Modrusan, Z; Neumann, L; Koth, CM; Lupardus, PJ; Kaminker, JS; Heise, CE; Steiner, P Genentech Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19423 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19423&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 20Y 4LY1 6918878 46519445 ZINC14970815 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 374954 Nc1ccc(cc1NC(=O)c1ccc(nc1)N1CCC2(CNC2=O)CC1)-c1cccs1 InChI=1S/C23H23N5O2S/c24-17-5-3-15(19-2-1-11-31-19)12-18(17)27-21(29)16-4-6-20(25-13-16)28-9-7-23(8-10-28)14-26-22(23)30/h1-6,11-13H,7-10,14,24H2,(H,26,30)(H,27,29) BHUJWKLXOJFZOZ-UHFFFAOYSA-N 50276074 CHEMBL470791::HDAC inhibitor, Compound 2::N-(2-amino-5-(thiophen-2-yl)phenyl)-6-(1-oxo-2,7-diazaspiro[3.5]nonan-7-yl)nicotinamide Histone deacetylase 4 Homo sapiens >1.0e+4 7.5 Curated from the literature by BindingDB 10.1074/jbc.M113.490706 10.7270/Q2KK99MZ 23897821 aid1802398 Lauffer, BE; Mintzer, R; Fong, R; Mukund, S; Tam, C; Zilberleyb, I; Flicke, B; Ritscher, A; Fedorowicz, G; Vallero, R; Ortwine, DF; Gunzner, J; Modrusan, Z; Neumann, L; Koth, CM; Lupardus, PJ; Kaminker, JS; Heise, CE; Steiner, P Genentech Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50276074 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50276074&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44590208 104119391 CHEMBL470791 ZINC40395080 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 374955 C[C@H](\C=C(/C)\C=C\C(=O)NO)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1 RTKIYFITIVXBLE-QEQCGCAPSA-N 50005711 CHEBI:46024::GNF-Pf-1011::TRICHOSTATIN::Trichostatin A::Trichostatin A (TSA)::US10011611, Trichostatin A::US10722597, Compound Trichostatin::US11535598, Compound Trichostatin A::US9265734, TSA Histone deacetylase 4 Homo sapiens 2.4e+3 7.5 Curated from the literature by BindingDB 10.1074/jbc.M113.490706 10.7270/Q2KK99MZ 23897821 aid1802398 Lauffer, BE; Mintzer, R; Fong, R; Mukund, S; Tam, C; Zilberleyb, I; Flicke, B; Ritscher, A; Fedorowicz, G; Vallero, R; Ortwine, DF; Gunzner, J; Modrusan, Z; Neumann, L; Koth, CM; Lupardus, PJ; Kaminker, JS; Heise, CE; Steiner, P Genentech Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 444732 242056952 DB04297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 374956 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >1.0e+4 7.5 Curated from the literature by BindingDB 10.1074/jbc.M113.490706 10.7270/Q2KK99MZ 23897821 aid1802398 Lauffer, BE; Mintzer, R; Fong, R; Mukund, S; Tam, C; Zilberleyb, I; Flicke, B; Ritscher, A; Fedorowicz, G; Vallero, R; Ortwine, DF; Gunzner, J; Modrusan, Z; Neumann, L; Koth, CM; Lupardus, PJ; Kaminker, JS; Heise, CE; Steiner, P Genentech Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 381825 OCc1ccc(cc1)[C@@H]1C[C@H](CSc2nc(c(o2)-c2ccccc2)-c2ccccc2)O[C@@H](O1)c1ccc(NC(=O)CCCCCCC(=O)NO)cc1 InChI=1S/C41H43N3O7S/c45-26-28-17-19-29(20-18-28)35-25-34(27-52-41-43-38(30-11-5-3-6-12-30)39(51-41)31-13-7-4-8-14-31)49-40(50-35)32-21-23-33(24-22-32)42-36(46)15-9-1-2-10-16-37(47)44-48/h3-8,11-14,17-24,34-35,40,45,48H,1-2,9-10,15-16,25-27H2,(H,42,46)(H,44,47)/t34-,35+,40+/m1/s1 BHUZLJOUHMBZQY-YXQOSMAKSA-N 22449 CHEMBL356769::N-(4-{(2R,4R,6S)-4-{[(4,5-diphenyl-1,3-oxazol-2-yl)sulfanyl]methyl}-6-[4-(hydroxymethyl)phenyl]-1,3-dioxan-2-yl}phenyl)-N -hydroxyoctanediamide::Tubacin::US9249087, Tubastatin A Histone deacetylase 4 Homo sapiens >30000 8 US Patent 10.7270/Q2Q23Z3W aid1802491 US9249087 Kozikowski, A; Kalin, JH; Butler, KV; Bergman, J; Hancock, WW University of Illinois http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=22449 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=22449&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6675804 49846263 CHEMBL356769 7374 ZINC27551136 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 381826 CN1CCc2c(C1)c1ccccc1n2Cc1ccc(cc1)C(=O)NO InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::Tubastatin A::US10227295, Compound Tubastatin A::US10456394, Tubastatin A::US11207431, Example D::US8748451, 6::US9249087, Tubacin::US9751832, Tubastatin A::US9956192, Compound Tubastatin-A Histone deacetylase 4 Homo sapiens 17300 8 US Patent 10.7270/Q2Q23Z3W aid1802491 US9249087 Kozikowski, A; Kalin, JH; Butler, KV; Bergman, J; Hancock, WW University of Illinois http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 ZINC51951670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50068901 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 177 ChEMBL 10.1016/j.bmcl.2006.12.028 10.7270/Q29W0H0K 17196388 Mai, A; Rotili, D; Massa, S; Brosch, G; Simonetti, G; Passariello, C; Palamara, AT Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50076396 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 76000 ChEMBL 10.1021/ml400175d 10.7270/Q2CZ38KR 24015327 Ko, KS; Steffey, ME; Brandvold, KR; Soellner, MB University of Michigan http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50076405 Nc1ncnc2n(nc(-c3ccc(Cl)cc3)c12)-c1cccc(c1)-c1cnnn1CCCCCC(=O)NO InChI=1S/C25H24ClN9O2/c26-18-10-8-16(9-11-18)23-22-24(27)28-15-29-25(22)35(31-23)19-6-4-5-17(13-19)20-14-30-33-34(20)12-3-1-2-7-21(36)32-37/h4-6,8-11,13-15,37H,1-3,7,12H2,(H,32,36)(H2,27,28,29) SJKCAVNLLOXGJL-UHFFFAOYSA-N 50437405 CHEMBL2408778 Histone deacetylase 4 Homo sapiens 3982 ChEMBL 10.1021/ml400175d 10.7270/Q2CZ38KR 24015327 Ko, KS; Steffey, ME; Brandvold, KR; Soellner, MB University of Michigan http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50437405 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50437405&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72164895 175449722 CHEMBL2408778 ZINC96273265 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50076553 ONC(=O)CCCCSc1nc(cc(=O)[nH]1)-c1ccc(Cl)cc1 InChI=1S/C15H16ClN3O3S/c16-11-6-4-10(5-7-11)12-9-14(21)18-15(17-12)23-8-2-1-3-13(20)19-22/h4-7,9,22H,1-3,8H2,(H,19,20)(H,17,18,21) LHYXCEVXWUZPDV-UHFFFAOYSA-N 50002747 CHEMBL217546 Histone deacetylase 4 Homo sapiens 2.83 ChEMBL 10.1016/j.bmcl.2006.12.028 10.7270/Q29W0H0K 17196388 Mai, A; Rotili, D; Massa, S; Brosch, G; Simonetti, G; Passariello, C; Palamara, AT Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50002747 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50002747&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 16729195 242056226 CHEMBL217546 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50076554 ONC(=O)CCCCSc1nc(cc(=O)[nH]1)-c1cccc(Cl)c1 InChI=1S/C15H16ClN3O3S/c16-11-5-3-4-10(8-11)12-9-14(21)18-15(17-12)23-7-2-1-6-13(20)19-22/h3-5,8-9,22H,1-2,6-7H2,(H,19,20)(H,17,18,21) UBKSBANVHOVYGV-UHFFFAOYSA-N 50002746 CHEMBL217545 Histone deacetylase 4 Homo sapiens 5.65 ChEMBL 10.1016/j.bmcl.2006.12.028 10.7270/Q29W0H0K 17196388 Mai, A; Rotili, D; Massa, S; Brosch, G; Simonetti, G; Passariello, C; Palamara, AT Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50002746 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50002746&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 16664734 242056225 CHEMBL217545 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50082457 ONC(=O)\C=C\c1ccc(OC[C@H](Cc2c[nH]c3ccccc23)NC(=O)c2ccc(Cl)cc2)cc1 InChI=1S/C27H24ClN3O4/c28-21-10-8-19(9-11-21)27(33)30-22(15-20-16-29-25-4-2-1-3-24(20)25)17-35-23-12-5-18(6-13-23)7-14-26(32)31-34/h1-14,16,22,29,34H,15,17H2,(H,30,33)(H,31,32)/b14-7+/t22-/m0/s1 WPUMMIJDKOEGAE-MNTLFOFUSA-N 50004757 CHEMBL3233698 Histone deacetylase 4 Homo sapiens 5701 ChEMBL 10.1021/jm401877m 10.7270/Q2D79CZ8 24694055 Li, X; Inks, ES; Li, X; Hou, J; Chou, CJ; Zhang, J; Jiang, Y; Zhang, Y; Xu, W Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50004757 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50004757&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 73776472 242056846 CHEMBL3233698 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50082904 C[C@H](\C=C(/C)\C=C\C(=O)NO)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1 RTKIYFITIVXBLE-QEQCGCAPSA-N 50005711 CHEBI:46024::GNF-Pf-1011::TRICHOSTATIN::Trichostatin A::Trichostatin A (TSA)::US10011611, Trichostatin A::US10722597, Compound Trichostatin::US11535598, Compound Trichostatin A::US9265734, TSA Histone deacetylase 4 Homo sapiens 12 ChEMBL 10.1016/j.ejmech.2014.04.021 10.7270/Q2V989KV 24742384 Cincinelli, R; Musso, L; Giannini, G; Zuco, V; De Cesare, M; Zunino, F; Dallavalle, S Universit£ di Milano http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 444732 242056952 DB04297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50082913 ONC(=O)\C=C\c1ccc(c(Cl)c1)-c1ccc(CC#N)c(c1)C12CC3CC(CC(C3)C1)C2 InChI=1S/C27H27ClN2O2/c28-25-12-17(2-6-26(31)30-32)1-5-23(25)22-4-3-21(7-8-29)24(13-22)27-14-18-9-19(15-27)11-20(10-18)16-27/h1-6,12-13,18-20,32H,7,9-11,14-16H2,(H,30,31)/b6-2+ ZDEMAYQXILUXCI-QHHAFSJGSA-N 50005730 CHEMBL3235790 Histone deacetylase 4 Homo sapiens 40000 ChEMBL 10.1016/j.ejmech.2014.04.021 10.7270/Q2V989KV 24742384 Cincinelli, R; Musso, L; Giannini, G; Zuco, V; De Cesare, M; Zunino, F; Dallavalle, S Universit£ di Milano http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005730 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005730&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90654946 103919178 CHEMBL3235790 ZINC29212399 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50082923 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 490 ChEMBL 10.1016/j.ejmech.2014.04.021 10.7270/Q2V989KV 24742384 Cincinelli, R; Musso, L; Giannini, G; Zuco, V; De Cesare, M; Zunino, F; Dallavalle, S Universit£ di Milano http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50082929 ONC(=O)\C=C\c1ccc(cc1)-c1ccc(O)c(c1)C12CC3CC(CC(C3)C1)C2 InChI=1S/C25H27NO3/c27-23-7-6-21(20-4-1-16(2-5-20)3-8-24(28)26-29)12-22(23)25-13-17-9-18(14-25)11-19(10-17)15-25/h1-8,12,17-19,27,29H,9-11,13-15H2,(H,26,28)/b8-3+ UGGXMNLTFKYUMB-FPYGCLRLSA-N 50005744 CHEMBL3235463 Histone deacetylase 4 Homo sapiens 61000 ChEMBL 10.1016/j.ejmech.2014.04.021 10.7270/Q2V989KV 24742384 Cincinelli, R; Musso, L; Giannini, G; Zuco, V; De Cesare, M; Zunino, F; Dallavalle, S Universit£ di Milano http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005744 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005744&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 15986417 242056953 CHEMBL3235463 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50082945 COc1ccc(cc1)-c1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C16H15NO3/c1-20-15-9-7-14(8-10-15)13-5-2-12(3-6-13)4-11-16(18)17-19/h2-11,19H,1H3,(H,17,18)/b11-4+ WKQPXLKFQLGQSM-NYYWCZLTSA-N 50293361 CHEMBL561209::N-Hydroxy-E-3-(4'-methoxybiphenyl-4-yl)-acrylamide Histone deacetylase 4 Homo sapiens 99000 ChEMBL 10.1016/j.ejmech.2014.04.021 10.7270/Q2V989KV 24742384 Cincinelli, R; Musso, L; Giannini, G; Zuco, V; De Cesare, M; Zunino, F; Dallavalle, S Universit£ di Milano http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50293361 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50293361&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 15986509 104134912 CHEMBL561209 ZINC34852254 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50082950 COc1ccc(cc1)-c1ccc(\C=C\C=C\C(=O)NO)cc1 InChI=1S/C18H17NO3/c1-22-17-12-10-16(11-13-17)15-8-6-14(7-9-15)4-2-3-5-18(20)19-21/h2-13,21H,1H3,(H,19,20)/b4-2+,5-3+ FXNPBRHKCIZIAB-ZUVMSYQZSA-N 50293369 CHEMBL538364::E,E-5-(4'-Methoxybiphenyl-4-yl)-penta-2,4-dienoic acid Nhydroxyamide Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.ejmech.2014.04.021 10.7270/Q2V989KV 24742384 Cincinelli, R; Musso, L; Giannini, G; Zuco, V; De Cesare, M; Zunino, F; Dallavalle, S Universit£ di Milano http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50293369 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50293369&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 42631047 104134920 CHEMBL538364 ZINC42966074 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50082951 COc1ccc(cc1C12CC3CC(CC(C3)C1)C2)-c1ccc(\C=C\C=C\C(=O)NO)cc1 InChI=1S/C28H31NO3/c1-32-26-11-10-24(23-8-6-19(7-9-23)4-2-3-5-27(30)29-31)15-25(26)28-16-20-12-21(17-28)14-22(13-20)18-28/h2-11,15,20-22,31H,12-14,16-18H2,1H3,(H,29,30)/b4-2+,5-3+ UDXLWODFRMOKRH-ZUVMSYQZSA-N 50005732 CHEMBL3235787 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.ejmech.2014.04.021 10.7270/Q2V989KV 24742384 Cincinelli, R; Musso, L; Giannini, G; Zuco, V; De Cesare, M; Zunino, F; Dallavalle, S Universit£ di Milano http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005732 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005732&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90654947 103919180 CHEMBL3235787 ZINC29212769 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50082970 ONC(=O)\C=C\c1ccc(cc1)-c1ccc(O)cc1 InChI=1S/C15H13NO3/c17-14-8-6-13(7-9-14)12-4-1-11(2-5-12)3-10-15(18)16-19/h1-10,17,19H,(H,16,18)/b10-3+ MGGQEULGVBEMAL-XCVCLJGOSA-N 50293358 CHEMBL556332::N-Hydroxy-E-3-(4'-hydroxybiphenyl-4-yl)-acrylamide Histone deacetylase 4 Homo sapiens 17000 ChEMBL 10.1016/j.ejmech.2014.04.021 10.7270/Q2V989KV 24742384 Cincinelli, R; Musso, L; Giannini, G; Zuco, V; De Cesare, M; Zunino, F; Dallavalle, S Universit£ di Milano http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50293358 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50293358&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 15986418 104134909 CHEMBL556332 ZINC34852064 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50085674 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 493 ChEMBL 10.1016/j.ejmech.2014.01.056 10.7270/Q2V40WQX 24565573 Baruchello, R; Simoni, D; Marchetti, P; Rondanin, R; Mangiola, S; Costantini, C; Meli, M; Giannini, G; Vesci, L; Carollo, V; Brunetti, T; Battistuzzi, G; Tolomeo, M; Cabri, W Universit£ degli Studi di Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50085685 CC(C)c1cc(C(=O)N2CCc3onc(C(=O)NCCCCCCC(=O)NO)c3C2)c(O)cc1O InChI=1S/C24H32N4O7/c1-14(2)15-11-16(19(30)12-18(15)29)24(33)28-10-8-20-17(13-28)22(27-35-20)23(32)25-9-6-4-3-5-7-21(31)26-34/h11-12,14,29-30,34H,3-10,13H2,1-2H3,(H,25,32)(H,26,31) MSHYQCFSRGHYAU-UHFFFAOYSA-N 50007730 CHEMBL3233755 Histone deacetylase 4 Homo sapiens 75900 ChEMBL 10.1016/j.ejmech.2014.01.056 10.7270/Q2V40WQX 24565573 Baruchello, R; Simoni, D; Marchetti, P; Rondanin, R; Mangiola, S; Costantini, C; Meli, M; Giannini, G; Vesci, L; Carollo, V; Brunetti, T; Battistuzzi, G; Tolomeo, M; Cabri, W Universit£ degli Studi di Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50007730 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50007730&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302594 103921000 CHEMBL3233755 ZINC27884809 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50086139 CC(C)c1cc(c(O)cc1O)-n1nnc(C(=O)NCCCCCCC(=O)NO)c1-c1ccc(CN2CCOCC2)cc1 InChI=1S/C30H40N6O6/c1-20(2)23-17-24(26(38)18-25(23)37)36-29(22-10-8-21(9-11-22)19-35-13-15-42-16-14-35)28(32-34-36)30(40)31-12-6-4-3-5-7-27(39)33-41/h8-11,17-18,20,37-38,41H,3-7,12-16,19H2,1-2H3,(H,31,40)(H,33,39) IBHAGSBJXPUIFA-UHFFFAOYSA-N 50008222 CHEMBL3235118 Histone deacetylase 4 Homo sapiens 71500 ChEMBL 10.1021/jm401536b 10.7270/Q2JQ12HR 24588105 Taddei, M; Ferrini, S; Giannotti, L; Corsi, M; Manetti, F; Giannini, G; Vesci, L; Milazzo, FM; Alloatti, D; Guglielmi, MB; Castorina, M; Cervoni, ML; Barbarino, M; Foderà, R; Carollo, V; Pisano, C; Armaroli, S; Cabri, W Universit£ degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50008222 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50008222&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90655296 103921435 CHEMBL3235118 ZINC27729548 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50086140 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 493 ChEMBL 10.1021/jm401536b 10.7270/Q2JQ12HR 24588105 Taddei, M; Ferrini, S; Giannotti, L; Corsi, M; Manetti, F; Giannini, G; Vesci, L; Milazzo, FM; Alloatti, D; Guglielmi, MB; Castorina, M; Cervoni, ML; Barbarino, M; Foderà, R; Carollo, V; Pisano, C; Armaroli, S; Cabri, W Universit£ degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50099653 Nc1ccc(cc1NC(=O)c1ccc(nc1)N1CCC2(CNC(=O)O2)CC1)-c1cccs1 InChI=1S/C23H23N5O3S/c24-17-5-3-15(19-2-1-11-32-19)12-18(17)27-21(29)16-4-6-20(25-13-16)28-9-7-23(8-10-28)14-26-22(30)31-23/h1-6,11-13H,7-10,14,24H2,(H,26,30)(H,27,29) MUTPWJCHZIMJSP-UHFFFAOYSA-N 50016941 CHEMBL3286732 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1021/ml4004233 10.7270/Q2HH6MM7 24900838 Methot, JL; Hoffman, DM; Witter, DJ; Stanton, MG; Harrington, P; Hamblett, C; Siliphaivanh, P; Wilson, K; Hubbs, J; Heidebrecht, R; Kral, AM; Ozerova, N; Fleming, JC; Wang, H; Szewczak, AA; Middleton, RE; Hughes, B; Cruz, JC; Haines, BB; Chenard, M; Kenific, CM; Harsch, A; Secrist, JP; Miller, TA Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50016941 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50016941&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 24744325 103928275 CHEMBL3286732 ZINC25973772 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 858331 ONC(=O)c1ccc2nc([nH]c2c1)-c1ccccc1C(F)(F)F InChI=1S/C15H10F3N3O2/c16-15(17,18)10-4-2-1-3-9(10)13-19-11-6-5-8(14(22)21-23)7-12(11)20-13/h1-7,23H,(H,19,20)(H,21,22) GBJUULAYFXKVRP-UHFFFAOYSA-N 425854 N-hydroxy-2-[2- (trifluoromethyl)phenyl]-1H- benzimidazole-6-carboxamide::US10512634, Example 18 Histone deacetylase 4 Homo sapiens >10000 US Patent 10.7270/Q2WD42ZQ aid1804071 US10512634 Schultz, J; Vagberg, J; Olsson, E; Farnegardh, K; Jonsson, M; Hammer, K; Kruger, L KANCERA AB http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=425854 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=425854&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122690152 434320206 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50235882 ONC(=O)CCCCc1ccn(Cc2ccc(cc2)-c2ccccc2)n1 InChI=1S/C21H23N3O2/c25-21(23-26)9-5-4-8-20-14-15-24(22-20)16-17-10-12-19(13-11-17)18-6-2-1-3-7-18/h1-3,6-7,10-15,26H,4-5,8-9,16H2,(H,23,25) GIMAODGURWKHJY-UHFFFAOYSA-N 50026431 CHEMBL3335300 Histone deacetylase 4 Homo sapiens 83100 ChEMBL 10.1016/j.ejmech.2014.09.024 10.7270/Q2NV9KTB 25218912 Yao, Y; Liao, C; Li, Z; Wang, Z; Sun, Q; Liu, C; Yang, Y; Tu, Z; Jiang, S Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026431 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026431&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118714377 313065268 CHEMBL3335300 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50235989 ONC(=O)CCCCc1ccn(Cc2ccc(Nc3ccccc3)cc2)n1 InChI=1S/C21H24N4O2/c26-21(24-27)9-5-4-8-20-14-15-25(23-20)16-17-10-12-19(13-11-17)22-18-6-2-1-3-7-18/h1-3,6-7,10-15,22,27H,4-5,8-9,16H2,(H,24,26) XXOUJCCBKBTDDB-UHFFFAOYSA-N 50026429 CHEMBL3335299 Histone deacetylase 4 Homo sapiens 56300 ChEMBL 10.1016/j.ejmech.2014.09.024 10.7270/Q2NV9KTB 25218912 Yao, Y; Liao, C; Li, Z; Wang, Z; Sun, Q; Liu, C; Yang, Y; Tu, Z; Jiang, S Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026429 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026429&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118714376 312528513 CHEMBL3335299 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50235990 ONC(=O)CCCCc1ccn(Cc2ccc(cc2)-n2ccc3ccccc23)n1 InChI=1S/C23H24N4O2/c28-23(25-29)8-4-2-6-20-14-15-26(24-20)17-18-9-11-21(12-10-18)27-16-13-19-5-1-3-7-22(19)27/h1,3,5,7,9-16,29H,2,4,6,8,17H2,(H,25,28) VUALYNHSKFMOKH-UHFFFAOYSA-N 50026433 CHEMBL3335298 Histone deacetylase 4 Homo sapiens 86400 ChEMBL 10.1016/j.ejmech.2014.09.024 10.7270/Q2NV9KTB 25218912 Yao, Y; Liao, C; Li, Z; Wang, Z; Sun, Q; Liu, C; Yang, Y; Tu, Z; Jiang, S Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026433 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026433&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118714375 313065270 CHEMBL3335298 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50235991 ONC(=O)CCCCc1ccn(Cc2cccc(c2)-c2ccccc2)n1 InChI=1S/C21H23N3O2/c25-21(23-26)12-5-4-11-20-13-14-24(22-20)16-17-7-6-10-19(15-17)18-8-2-1-3-9-18/h1-3,6-10,13-15,26H,4-5,11-12,16H2,(H,23,25) UDRKLVCIAKBNQW-UHFFFAOYSA-N 50026450 CHEMBL3335283 Histone deacetylase 4 Homo sapiens 81500 ChEMBL 10.1016/j.ejmech.2014.09.024 10.7270/Q2NV9KTB 25218912 Yao, Y; Liao, C; Li, Z; Wang, Z; Sun, Q; Liu, C; Yang, Y; Tu, Z; Jiang, S Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026450 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026450&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72195322 103936090 52884 CHEMBL3335283 ZINC00895354 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50236391 COc1cc(OC)cc(\C=C\c2ccc(OC)c(NC(=O)CCCCCCC(=O)NO)c2)c1 InChI=1S/C25H32N2O6/c1-31-20-14-19(15-21(17-20)32-2)11-10-18-12-13-23(33-3)22(16-18)26-24(28)8-6-4-5-7-9-25(29)27-30/h10-17,30H,4-9H2,1-3H3,(H,26,28)(H,27,29)/b11-10+ NZMWPDHOFLWFSH-ZHACJKMWSA-N 50026643 CHEMBL3335369 Histone deacetylase 4 Homo sapiens 9800 ChEMBL 10.1021/ml5000959 10.7270/Q2125V70 25221651 Giacomini, E; Nebbioso, A; Ciotta, A; Ianni, C; Falchi, F; Roberti, M; Tolomeo, M; Grimaudo, S; Cristina, AD; Pipitone, RM; Altucci, L; Recanatini, M University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026643 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026643&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118714414 313065315 CHEMBL3335369 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50236392 COc1cc(OC)cc(\C=C/c2ccc(OC)c(NC(=O)CCCCCCC(=O)NO)c2)c1 InChI=1S/C25H32N2O6/c1-31-20-14-19(15-21(17-20)32-2)11-10-18-12-13-23(33-3)22(16-18)26-24(28)8-6-4-5-7-9-25(29)27-30/h10-17,30H,4-9H2,1-3H3,(H,26,28)(H,27,29)/b11-10- NZMWPDHOFLWFSH-KHPPLWFESA-N 50026644 CHEMBL3335370 Histone deacetylase 4 Homo sapiens 7600 ChEMBL 10.1021/ml5000959 10.7270/Q2125V70 25221651 Giacomini, E; Nebbioso, A; Ciotta, A; Ianni, C; Falchi, F; Roberti, M; Tolomeo, M; Grimaudo, S; Cristina, AD; Pipitone, RM; Altucci, L; Recanatini, M University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026644 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026644&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118714415 103936233 CHEMBL3335370 ZINC28755765 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50236396 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 7800 ChEMBL 10.1021/ml5000959 10.7270/Q2125V70 25221651 Giacomini, E; Nebbioso, A; Ciotta, A; Ianni, C; Falchi, F; Roberti, M; Tolomeo, M; Grimaudo, S; Cristina, AD; Pipitone, RM; Altucci, L; Recanatini, M University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50237824 ONC(=O)c1ccc2CCN(Cc3ccc(o3)-c3cccc(c3)[N+]([O-])=O)Cc2c1 InChI=1S/C21H19N3O5/c25-21(22-26)16-5-4-14-8-9-23(12-17(14)10-16)13-19-6-7-20(29-19)15-2-1-3-18(11-15)24(27)28/h1-7,10-11,26H,8-9,12-13H2,(H,22,25) PMFDRULHDRRWFP-UHFFFAOYSA-N 50027664 CHEMBL3338404 Histone deacetylase 4 Homo sapiens 67800 ChEMBL 10.1021/jm5008962 10.7270/Q29C700V 25238284 Tang, G; Wong, JC; Zhang, W; Wang, Z; Zhang, N; Peng, Z; Zhang, Z; Rong, Y; Li, S; Zhang, M; Yu, L; Feng, T; Zhang, X; Wu, X; Wu, JZ; Chen, L Roche Pharmaceutical Research and Early Development http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50027664 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50027664&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 101882265 103937133 CHEMBL3338404 ZINC27977384 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50237825 ONC(=O)c1ccc2CC[C@H](Cc2c1)Nc1nccc(n1)-c1cccnc1 InChI=1S/C20H19N5O2/c26-19(25-27)14-4-3-13-5-6-17(11-16(13)10-14)23-20-22-9-7-18(24-20)15-2-1-8-21-12-15/h1-4,7-10,12,17,27H,5-6,11H2,(H,25,26)(H,22,23,24)/t17-/m1/s1 MWLFQRZKKHIDTM-QGZVFWFLSA-N 50027662 CHEMBL3338418 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/jm5008962 10.7270/Q29C700V 25238284 Tang, G; Wong, JC; Zhang, W; Wang, Z; Zhang, N; Peng, Z; Zhang, Z; Rong, Y; Li, S; Zhang, M; Yu, L; Feng, T; Zhang, X; Wu, X; Wu, JZ; Chen, L Roche Pharmaceutical Research and Early Development http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50027662 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50027662&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 92045024 313065329 CHEMBL3338418 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50237826 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 76000 ChEMBL 10.1021/jm5008962 10.7270/Q29C700V 25238284 Tang, G; Wong, JC; Zhang, W; Wang, Z; Zhang, N; Peng, Z; Zhang, Z; Rong, Y; Li, S; Zhang, M; Yu, L; Feng, T; Zhang, X; Wu, X; Wu, JZ; Chen, L Roche Pharmaceutical Research and Early Development http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50253017 Cn1cccc1C(=O)N1CCn2cc(cc2C1)C(=O)NO InChI=1S/C14H16N4O3/c1-16-4-2-3-12(16)14(20)18-6-5-17-8-10(13(19)15-21)7-11(17)9-18/h2-4,7-8,21H,5-6,9H2,1H3,(H,15,19) HXYDFXUSMZJLIU-UHFFFAOYSA-N 50036285 CHEMBL3353053 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2014.10.022 10.7270/Q2B859QH 25454270 Blackburn, C; Barrett, C; Brunson, M; Chin, J; England, D; Garcia, K; Gigstad, K; Gould, A; Gutierrez, J; Hoar, K; Rowland, RS; Tsu, C; Ringeling, J; Wager, K; Xu, H TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50036285 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50036285&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 58465708 312528635 CHEMBL3353053 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50253018 Cn1cccc1C(=O)NCc1ccc(cc1)C(=O)NO InChI=1S/C14H15N3O3/c1-17-8-2-3-12(17)14(19)15-9-10-4-6-11(7-5-10)13(18)16-20/h2-8,20H,9H2,1H3,(H,15,19)(H,16,18) FOBBYTXDJVRRLB-UHFFFAOYSA-N 50440912 CHEMBL2431862 Histone deacetylase 4 Homo sapiens 15000 ChEMBL 10.1016/j.bmcl.2014.10.022 10.7270/Q2B859QH 25454270 Blackburn, C; Barrett, C; Brunson, M; Chin, J; England, D; Garcia, K; Gigstad, K; Gould, A; Gutierrez, J; Hoar, K; Rowland, RS; Tsu, C; Ringeling, J; Wager, K; Xu, H TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50440912 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50440912&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 73333311 175453229 CHEMBL2431862 ZINC96284628 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50253019 Cn1cccc1C(=O)N1CCc2cc(ccc2C1)C(=O)NO InChI=1S/C16H17N3O3/c1-18-7-2-3-14(18)16(21)19-8-6-11-9-12(15(20)17-22)4-5-13(11)10-19/h2-5,7,9,22H,6,8,10H2,1H3,(H,17,20) NNQAQGDSGCGFER-UHFFFAOYSA-N 50440907 CHEMBL2431901 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2014.10.022 10.7270/Q2B859QH 25454270 Blackburn, C; Barrett, C; Brunson, M; Chin, J; England, D; Garcia, K; Gigstad, K; Gould, A; Gutierrez, J; Hoar, K; Rowland, RS; Tsu, C; Ringeling, J; Wager, K; Xu, H TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50440907 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50440907&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 49831258 175453224 CHEMBL2431901 ZINC68248700 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50253020 OCc1ccc(cc1)[C@@H]1C[C@H](CSc2nc(c(o2)-c2ccccc2)-c2ccccc2)O[C@@H](O1)c1ccc(NC(=O)CCCCCCC(=O)NO)cc1 InChI=1S/C41H43N3O7S/c45-26-28-17-19-29(20-18-28)35-25-34(27-52-41-43-38(30-11-5-3-6-12-30)39(51-41)31-13-7-4-8-14-31)49-40(50-35)32-21-23-33(24-22-32)42-36(46)15-9-1-2-10-16-37(47)44-48/h3-8,11-14,17-24,34-35,40,45,48H,1-2,9-10,15-16,25-27H2,(H,42,46)(H,44,47)/t34-,35+,40+/m1/s1 BHUZLJOUHMBZQY-YXQOSMAKSA-N 22449 CHEMBL356769::N-(4-{(2R,4R,6S)-4-{[(4,5-diphenyl-1,3-oxazol-2-yl)sulfanyl]methyl}-6-[4-(hydroxymethyl)phenyl]-1,3-dioxan-2-yl}phenyl)-N -hydroxyoctanediamide::Tubacin::US9249087, Tubastatin A Histone deacetylase 4 Homo sapiens 17300 ChEMBL 10.1016/j.bmcl.2014.10.022 10.7270/Q2B859QH 25454270 Blackburn, C; Barrett, C; Brunson, M; Chin, J; England, D; Garcia, K; Gigstad, K; Gould, A; Gutierrez, J; Hoar, K; Rowland, RS; Tsu, C; Ringeling, J; Wager, K; Xu, H TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=22449 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=22449&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6675804 49846263 CHEMBL356769 7374 ZINC27551136 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50253021 CN1CCc2c(C1)c1ccccc1n2Cc1ccc(cc1)C(=O)NO InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::Tubastatin A::US10227295, Compound Tubastatin A::US10456394, Tubastatin A::US11207431, Example D::US8748451, 6::US9249087, Tubacin::US9751832, Tubastatin A::US9956192, Compound Tubastatin-A Histone deacetylase 4 Homo sapiens >30000 ChEMBL 10.1016/j.bmcl.2014.10.022 10.7270/Q2B859QH 25454270 Blackburn, C; Barrett, C; Brunson, M; Chin, J; England, D; Garcia, K; Gigstad, K; Gould, A; Gutierrez, J; Hoar, K; Rowland, RS; Tsu, C; Ringeling, J; Wager, K; Xu, H TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 ZINC51951670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50258266 COc1ccccc1C(=O)N[C@H](COc1cccc(\C=C\C(=O)NO)c1)Cc1c[nH]c2ccccc12 50038729 CHEMBL3354920 Histone deacetylase 4 Homo sapiens 440 ChEMBL 10.1016/j.ejmech.2014.10.077 10.7270/Q2NG4S8Z 25462271 Li, X; Hou, J; Li, X; Jiang, Y; Liu, X; Mu, W; Jin, Y; Zhang, Y; Xu, W Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50038729 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50038729&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118720529 313067350 CHEMBL3354920 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50276373 C[C@H](\C=C(/C)\C=C\C(=O)NO)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1 RTKIYFITIVXBLE-QEQCGCAPSA-N 50005711 CHEBI:46024::GNF-Pf-1011::TRICHOSTATIN::Trichostatin A::Trichostatin A (TSA)::US10011611, Trichostatin A::US10722597, Compound Trichostatin::US11535598, Compound Trichostatin A::US9265734, TSA Histone deacetylase 4 Homo sapiens 34 ChEMBL 10.1016/j.bmc.2014.06.029 10.7270/Q23F4R9P 24997578 Hoque, MA; Islam, MN; Islam, MS; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 444732 242056952 DB04297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50276374 C[C@@H]1NC(=O)[C@H]2CCCCCSSCCCCC[C@H](NC(=O)[C@H]3CCCN3C1=O)C(=O)N2 InChI=1S/C22H36N4O4S2/c1-15-22(30)26-12-8-11-18(26)21(29)25-17-10-5-3-7-14-32-31-13-6-2-4-9-16(19(27)23-15)24-20(17)28/h15-18H,2-14H2,1H3,(H,23,27)(H,24,28)(H,25,29)/t15-,16+,17-,18+/m0/s1 UFOGKVCQIBKIPF-XWTMOSNGSA-N 50048858 CHEMBL3310506 Histone deacetylase 4 Homo sapiens >100 ChEMBL 10.1016/j.bmc.2014.06.029 10.7270/Q23F4R9P 24997578 Hoque, MA; Islam, MN; Islam, MS; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50048858 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50048858&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118706554 103979239 CHEMBL3310506 ZINC13745297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50276375 CC(C)[C@@H]1NC(=O)[C@H]2CCCCCSSCCCCC[C@H](NC(=O)[C@H]3CCCN3C1=O)C(=O)N2 InChI=1S/C24H40N4O4S2/c1-16(2)20-24(32)28-13-9-12-19(28)23(31)26-17-10-5-3-7-14-33-34-15-8-4-6-11-18(22(30)27-20)25-21(17)29/h16-20H,3-15H2,1-2H3,(H,25,29)(H,26,31)(H,27,30)/t17-,18+,19+,20-/m0/s1 GHEMSUBEZDZMNW-NMLBUPMWSA-N 50048859 CHEMBL3310507 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmc.2014.06.029 10.7270/Q23F4R9P 24997578 Hoque, MA; Islam, MN; Islam, MS; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50048859 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50048859&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118706555 103979240 CHEMBL3310507 ZINC13745293 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50276376 O=C1N[C@H]2CCCCCSSCCCCC[C@@H](NC2=O)C(=O)N[C@@H](Cc2ccccc2)C(=O)N2CCC[C@H]12 InChI=1S/C28H40N4O4S2/c33-25-22-14-7-3-9-18-38-37-17-8-2-6-13-21(29-25)26(34)31-23(19-20-11-4-1-5-12-20)28(36)32-16-10-15-24(32)27(35)30-22/h1,4-5,11-12,21-24H,2-3,6-10,13-19H2,(H,29,33)(H,30,35)(H,31,34)/t21-,22+,23+,24-/m1/s1 ZQICYEMFUJEREY-NAVOZUGXSA-N 50048860 CHEMBL3310508 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmc.2014.06.029 10.7270/Q23F4R9P 24997578 Hoque, MA; Islam, MN; Islam, MS; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50048860 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50048860&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118706556 103979241 CHEMBL3310508 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50276377 C[C@@H]1NC(=O)[C@H]2CCOCCSSCCCCC[C@H](NC(=O)[C@H]3CCCN3C1=O)C(=O)N2 InChI=1S/C21H34N4O5S2/c1-14-21(29)25-9-5-7-17(25)20(28)24-15-6-3-2-4-12-31-32-13-11-30-10-8-16(18(26)22-14)23-19(15)27/h14-17H,2-13H2,1H3,(H,22,26)(H,23,27)(H,24,28)/t14-,15-,16+,17+/m0/s1 KEWVXCHCIIDYGU-MWDXBVQZSA-N 50048861 CHEMBL3310509 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmc.2014.06.029 10.7270/Q23F4R9P 24997578 Hoque, MA; Islam, MN; Islam, MS; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50048861 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50048861&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118706557 103979242 CHEMBL3310509 ZINC13745299 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50276378 CC(C)[C@@H]1NC(=O)[C@@H]2CCCCCSSCCCCC[C@H](NC(=O)[C@H]3CCCN3C1=O)C(=O)N2 InChI=1S/C24H40N4O4S2/c1-16(2)20-24(32)28-13-9-12-19(28)23(31)26-17-10-5-3-7-14-33-34-15-8-4-6-11-18(22(30)27-20)25-21(17)29/h16-20H,3-15H2,1-2H3,(H,25,29)(H,26,31)(H,27,30)/t17-,18-,19+,20-/m0/s1 GHEMSUBEZDZMNW-HAGHYFMRSA-N 50048862 CHEMBL3310510 Histone deacetylase 4 Homo sapiens 63000 ChEMBL 10.1016/j.bmc.2014.06.029 10.7270/Q23F4R9P 24997578 Hoque, MA; Islam, MN; Islam, MS; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50048862 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50048862&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 102140473 103979243 CHEMBL3310510 ZINC13745270 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50276379 CC(C)[C@@H]1NC(=O)[C@H]2Cc3ccccc3CN2C(=O)[C@@H]2CCCCCSSCCCCC[C@@H](NC1=O)C(=O)N2 InChI=1S/C29H42N4O4S2/c1-19(2)25-28(36)30-22-13-5-3-9-15-38-39-16-10-4-6-14-23(31-26(22)34)29(37)33-18-21-12-8-7-11-20(21)17-24(33)27(35)32-25/h7-8,11-12,19,22-25H,3-6,9-10,13-18H2,1-2H3,(H,30,36)(H,31,34)(H,32,35)/t22-,23+,24-,25+/m1/s1 QUONJWHHYGIQCS-RCTAOEEJSA-N 50048863 CHEMBL3310511 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmc.2014.06.029 10.7270/Q23F4R9P 24997578 Hoque, MA; Islam, MN; Islam, MS; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50048863 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50048863&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 102140474 103979244 CHEMBL3310511 ZINC13745309 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50266515 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 150 ChEMBL 10.1016/j.bmc.2014.05.001 10.7270/Q24T6M0V 24864038 Tashima, T; Murata, H; Kodama, H Nippon Pharmaceutical Chemicals Co., Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50266516 ONC(=O)CCCCCCC(=O)Nc1ccc2[nH]c(=O)ccc2c1 InChI=1S/C17H21N3O4/c21-15(5-3-1-2-4-6-17(23)20-24)18-13-8-9-14-12(11-13)7-10-16(22)19-14/h7-11,24H,1-6H2,(H,18,21)(H,19,22)(H,20,23) LMKXBBIZQUFLCC-UHFFFAOYSA-N 50044640 CHEMBL3311464 Histone deacetylase 4 Homo sapiens 63 ChEMBL 10.1016/j.bmc.2014.05.001 10.7270/Q24T6M0V 24864038 Tashima, T; Murata, H; Kodama, H Nippon Pharmaceutical Chemicals Co., Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50044640 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50044640&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118987707 313068259 CHEMBL3311464 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50266517 ONC(=O)CCCCCCC(=O)Nc1ccc2NC(=O)CCc2c1 InChI=1S/C17H23N3O4/c21-15(5-3-1-2-4-6-17(23)20-24)18-13-8-9-14-12(11-13)7-10-16(22)19-14/h8-9,11,24H,1-7,10H2,(H,18,21)(H,19,22)(H,20,23) HXDYRFDOQYZPBS-UHFFFAOYSA-N 50044641 CHEMBL3311465 Histone deacetylase 4 Homo sapiens 120 ChEMBL 10.1016/j.bmc.2014.05.001 10.7270/Q24T6M0V 24864038 Tashima, T; Murata, H; Kodama, H Nippon Pharmaceutical Chemicals Co., Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50044641 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50044641&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86581152 313068260 CHEMBL3311465 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50266518 CC1(C)CC(=O)Nc2ccc(NC(=O)CCCCCCC(=O)NO)cc12 InChI=1S/C19H27N3O4/c1-19(2)12-18(25)21-15-10-9-13(11-14(15)19)20-16(23)7-5-3-4-6-8-17(24)22-26/h9-11,26H,3-8,12H2,1-2H3,(H,20,23)(H,21,25)(H,22,24) URLZAKMTSXZUEP-UHFFFAOYSA-N 50044642 CHEMBL3311466 Histone deacetylase 4 Homo sapiens 47 ChEMBL 10.1016/j.bmc.2014.05.001 10.7270/Q24T6M0V 24864038 Tashima, T; Murata, H; Kodama, H Nippon Pharmaceutical Chemicals Co., Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50044642 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50044642&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86581153 313068261 CHEMBL3311466 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50266519 ONC(=O)CCCCCCNC(=O)c1ccc2[nH]c(=O)ccc2c1 InChI=1S/C17H21N3O4/c21-15-9-7-12-11-13(6-8-14(12)19-15)17(23)18-10-4-2-1-3-5-16(22)20-24/h6-9,11,24H,1-5,10H2,(H,18,23)(H,19,21)(H,20,22) UFTSJQJNTKASLO-UHFFFAOYSA-N 50044643 CHEMBL3311471 Histone deacetylase 4 Homo sapiens 280 ChEMBL 10.1016/j.bmc.2014.05.001 10.7270/Q24T6M0V 24864038 Tashima, T; Murata, H; Kodama, H Nippon Pharmaceutical Chemicals Co., Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50044643 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50044643&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118987708 313068262 CHEMBL3311471 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50266520 ONC(=O)CCCCCCNC(=O)c1ccc2NC(=O)CCc2c1 InChI=1S/C17H23N3O4/c21-15-9-7-12-11-13(6-8-14(12)19-15)17(23)18-10-4-2-1-3-5-16(22)20-24/h6,8,11,24H,1-5,7,9-10H2,(H,18,23)(H,19,21)(H,20,22) ITSLNGBJYKFUFZ-UHFFFAOYSA-N 50044644 CHEMBL3311472 Histone deacetylase 4 Homo sapiens 120 ChEMBL 10.1016/j.bmc.2014.05.001 10.7270/Q24T6M0V 24864038 Tashima, T; Murata, H; Kodama, H Nippon Pharmaceutical Chemicals Co., Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50044644 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50044644&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86581004 313068263 CHEMBL3311472 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50266521 CC1(C)CC(=O)Nc2ccc(cc12)C(=O)NCCCCCCC(=O)NO InChI=1S/C19H27N3O4/c1-19(2)12-17(24)21-15-9-8-13(11-14(15)19)18(25)20-10-6-4-3-5-7-16(23)22-26/h8-9,11,26H,3-7,10,12H2,1-2H3,(H,20,25)(H,21,24)(H,22,23) OEQQELYWLWKXKU-UHFFFAOYSA-N 50044645 CHEMBL3311473 Histone deacetylase 4 Homo sapiens 63 ChEMBL 10.1016/j.bmc.2014.05.001 10.7270/Q24T6M0V 24864038 Tashima, T; Murata, H; Kodama, H Nippon Pharmaceutical Chemicals Co., Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50044645 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50044645&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86581005 313068264 CHEMBL3311473 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50266522 Cn1c2ccc(cc2ccc1=O)C(=O)NCCCCCCC(=O)NO InChI=1S/C18H23N3O4/c1-21-15-9-7-14(12-13(15)8-10-17(21)23)18(24)19-11-5-3-2-4-6-16(22)20-25/h7-10,12,25H,2-6,11H2,1H3,(H,19,24)(H,20,22) FVXNWIVUIWQBNB-UHFFFAOYSA-N 50044646 CHEMBL3309284 Histone deacetylase 4 Homo sapiens 86 ChEMBL 10.1016/j.bmc.2014.05.001 10.7270/Q24T6M0V 24864038 Tashima, T; Murata, H; Kodama, H Nippon Pharmaceutical Chemicals Co., Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50044646 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50044646&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117829462 313068265 CHEMBL3309284 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50266523 CN1C(=O)CC(C)(C)c2cc(ccc12)C(=O)NCCCCCCC(=O)NO InChI=1S/C20H29N3O4/c1-20(2)13-18(25)23(3)16-10-9-14(12-15(16)20)19(26)21-11-7-5-4-6-8-17(24)22-27/h9-10,12,27H,4-8,11,13H2,1-3H3,(H,21,26)(H,22,24) KSXJIIICYHHPTD-UHFFFAOYSA-N 50044647 CHEMBL3309286 Histone deacetylase 4 Homo sapiens 280 ChEMBL 10.1016/j.bmc.2014.05.001 10.7270/Q24T6M0V 24864038 Tashima, T; Murata, H; Kodama, H Nippon Pharmaceutical Chemicals Co., Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50044647 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50044647&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117829461 313068266 CHEMBL3309286 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50266524 COc1ccc2cc(ccc2n1)C(=O)NCCCCCCC(=O)NO InChI=1S/C18H23N3O4/c1-25-17-10-8-13-12-14(7-9-15(13)20-17)18(23)19-11-5-3-2-4-6-16(22)21-24/h7-10,12,24H,2-6,11H2,1H3,(H,19,23)(H,21,22) VVZXDYPDBYYVAY-UHFFFAOYSA-N 50044648 CHEMBL3309288 Histone deacetylase 4 Homo sapiens 78 ChEMBL 10.1016/j.bmc.2014.05.001 10.7270/Q24T6M0V 24864038 Tashima, T; Murata, H; Kodama, H Nippon Pharmaceutical Chemicals Co., Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50044648 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50044648&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117829456 313068267 CHEMBL3309288 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50266525 CC1(C)CC(=O)Nc2ccc(cc12)C(=O)NCc1cccc(\C=C\C(=O)NO)c1 InChI=1S/C22H23N3O4/c1-22(2)12-20(27)24-18-8-7-16(11-17(18)22)21(28)23-13-15-5-3-4-14(10-15)6-9-19(26)25-29/h3-11,29H,12-13H2,1-2H3,(H,23,28)(H,24,27)(H,25,26)/b9-6+ ROVKUEFHZPOYAM-RMKNXTFCSA-N 50044649 CHEMBL3309290 Histone deacetylase 4 Homo sapiens 2000 ChEMBL 10.1016/j.bmc.2014.05.001 10.7270/Q24T6M0V 24864038 Tashima, T; Murata, H; Kodama, H Nippon Pharmaceutical Chemicals Co., Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50044649 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50044649&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86581432 313068268 CHEMBL3309290 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50266526 CC1(C)CC(=O)Nc2ccc(cc12)C(=O)NCc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C22H23N3O4/c1-22(2)12-20(27)24-18-9-8-16(11-17(18)22)21(28)23-13-15-5-3-14(4-6-15)7-10-19(26)25-29/h3-11,29H,12-13H2,1-2H3,(H,23,28)(H,24,27)(H,25,26)/b10-7+ FLMAGDPBVLRRSK-JXMROGBWSA-N 50044635 CHEMBL3309291 Histone deacetylase 4 Homo sapiens 380 ChEMBL 10.1016/j.bmc.2014.05.001 10.7270/Q24T6M0V 24864038 Tashima, T; Murata, H; Kodama, H Nippon Pharmaceutical Chemicals Co., Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50044635 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50044635&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86581434 313068254 CHEMBL3309291 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50266527 CC1(C)CC(=O)Nc2ccc(cc12)C(=O)NC[C@H]1CC[C@@H](CC1)\C=C\C(=O)NO InChI=1S/C22H29N3O4/c1-22(2)12-20(27)24-18-9-8-16(11-17(18)22)21(28)23-13-15-5-3-14(4-6-15)7-10-19(26)25-29/h7-11,14-15,29H,3-6,12-13H2,1-2H3,(H,23,28)(H,24,27)(H,25,26)/b10-7+/t14-,15- RIHKXPFNMAZMOA-KTRQRASZSA-N 50044636 CHEMBL3309297 Histone deacetylase 4 Homo sapiens 58 ChEMBL 10.1016/j.bmc.2014.05.001 10.7270/Q24T6M0V 24864038 Tashima, T; Murata, H; Kodama, H Nippon Pharmaceutical Chemicals Co., Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50044636 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50044636&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86291495 313068255 CHEMBL3309297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50266528 CC1(C)CC(=O)Nc2ccc(cc12)C(=O)NC[C@H]1CC[C@H](CCC(=O)NO)CC1 InChI=1S/C22H31N3O4/c1-22(2)12-20(27)24-18-9-8-16(11-17(18)22)21(28)23-13-15-5-3-14(4-6-15)7-10-19(26)25-29/h8-9,11,14-15,29H,3-7,10,12-13H2,1-2H3,(H,23,28)(H,24,27)(H,25,26)/t14-,15- VGDKNUOQFCSMED-SHTZXODSSA-N 50044637 CHEMBL3309298 Histone deacetylase 4 Homo sapiens 220 ChEMBL 10.1016/j.bmc.2014.05.001 10.7270/Q24T6M0V 24864038 Tashima, T; Murata, H; Kodama, H Nippon Pharmaceutical Chemicals Co., Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50044637 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50044637&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86581435 313068256 CHEMBL3309298 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50266529 CC1(C)CC(=O)Nc2ccc(cc12)C(=O)NC[C@H]1CC[C@H](CC1)\C=C\C(=O)NO InChI=1S/C22H29N3O4/c1-22(2)12-20(27)24-18-9-8-16(11-17(18)22)21(28)23-13-15-5-3-14(4-6-15)7-10-19(26)25-29/h7-11,14-15,29H,3-6,12-13H2,1-2H3,(H,23,28)(H,24,27)(H,25,26)/b10-7+/t14-,15+ RIHKXPFNMAZMOA-ONWOKCAKSA-N 50044638 CHEMBL3309299 Histone deacetylase 4 Homo sapiens 750 ChEMBL 10.1016/j.bmc.2014.05.001 10.7270/Q24T6M0V 24864038 Tashima, T; Murata, H; Kodama, H Nippon Pharmaceutical Chemicals Co., Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50044638 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50044638&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86291495 313068257 CHEMBL3309299 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50266530 CC1(C)CC(=O)Nc2ccc(cc12)C(=O)NC[C@@H]1CC[C@H](CCC(=O)NO)CC1 InChI=1S/C22H31N3O4/c1-22(2)12-20(27)24-18-9-8-16(11-17(18)22)21(28)23-13-15-5-3-14(4-6-15)7-10-19(26)25-29/h8-9,11,14-15,29H,3-7,10,12-13H2,1-2H3,(H,23,28)(H,24,27)(H,25,26)/t14-,15+ VGDKNUOQFCSMED-GASCZTMLSA-N 50044639 CHEMBL3309300 Histone deacetylase 4 Homo sapiens 330 ChEMBL 10.1016/j.bmc.2014.05.001 10.7270/Q24T6M0V 24864038 Tashima, T; Murata, H; Kodama, H Nippon Pharmaceutical Chemicals Co., Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50044639 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50044639&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86581435 313068258 CHEMBL3309300 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50276454 C[C@@H]1NC(=O)[C@H]2CCCCCSSCCCCC[C@H](NC(=O)[C@H]3CCCN3C1=O)C(=O)N2 InChI=1S/C22H36N4O4S2/c1-15-22(30)26-12-8-11-18(26)21(29)25-17-10-5-3-7-14-32-31-13-6-2-4-9-16(19(27)23-15)24-20(17)28/h15-18H,2-14H2,1H3,(H,23,27)(H,24,28)(H,25,29)/t15-,16+,17-,18+/m0/s1 UFOGKVCQIBKIPF-XWTMOSNGSA-N 50048858 CHEMBL3310506 Histone deacetylase 4 Homo sapiens 10 ChEMBL 10.1016/j.bmc.2014.06.029 10.7270/Q23F4R9P 24997578 Hoque, MA; Islam, MN; Islam, MS; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50048858 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50048858&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118706554 103979239 CHEMBL3310506 ZINC13745297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50276455 CC(C)[C@@H]1NC(=O)[C@H]2CCCCCSSCCCCC[C@H](NC(=O)[C@H]3CCCN3C1=O)C(=O)N2 InChI=1S/C24H40N4O4S2/c1-16(2)20-24(32)28-13-9-12-19(28)23(31)26-17-10-5-3-7-14-33-34-15-8-4-6-11-18(22(30)27-20)25-21(17)29/h16-20H,3-15H2,1-2H3,(H,25,29)(H,26,31)(H,27,30)/t17-,18+,19+,20-/m0/s1 GHEMSUBEZDZMNW-NMLBUPMWSA-N 50048859 CHEMBL3310507 Histone deacetylase 4 Homo sapiens 8.3 ChEMBL 10.1016/j.bmc.2014.06.029 10.7270/Q23F4R9P 24997578 Hoque, MA; Islam, MN; Islam, MS; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50048859 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50048859&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118706555 103979240 CHEMBL3310507 ZINC13745293 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50276456 O=C1N[C@H]2CCCCCSSCCCCC[C@@H](NC2=O)C(=O)N[C@@H](Cc2ccccc2)C(=O)N2CCC[C@H]12 InChI=1S/C28H40N4O4S2/c33-25-22-14-7-3-9-18-38-37-17-8-2-6-13-21(29-25)26(34)31-23(19-20-11-4-1-5-12-20)28(36)32-16-10-15-24(32)27(35)30-22/h1,4-5,11-12,21-24H,2-3,6-10,13-19H2,(H,29,33)(H,30,35)(H,31,34)/t21-,22+,23+,24-/m1/s1 ZQICYEMFUJEREY-NAVOZUGXSA-N 50048860 CHEMBL3310508 Histone deacetylase 4 Homo sapiens 4.2 ChEMBL 10.1016/j.bmc.2014.06.029 10.7270/Q23F4R9P 24997578 Hoque, MA; Islam, MN; Islam, MS; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50048860 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50048860&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118706556 103979241 CHEMBL3310508 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50276457 C[C@@H]1NC(=O)[C@H]2CCOCCSSCCCCC[C@H](NC(=O)[C@H]3CCCN3C1=O)C(=O)N2 InChI=1S/C21H34N4O5S2/c1-14-21(29)25-9-5-7-17(25)20(28)24-15-6-3-2-4-12-31-32-13-11-30-10-8-16(18(26)22-14)23-19(15)27/h14-17H,2-13H2,1H3,(H,22,26)(H,23,27)(H,24,28)/t14-,15-,16+,17+/m0/s1 KEWVXCHCIIDYGU-MWDXBVQZSA-N 50048861 CHEMBL3310509 Histone deacetylase 4 Homo sapiens 11 ChEMBL 10.1016/j.bmc.2014.06.029 10.7270/Q23F4R9P 24997578 Hoque, MA; Islam, MN; Islam, MS; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50048861 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50048861&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118706557 103979242 CHEMBL3310509 ZINC13745299 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50276458 CC(C)[C@@H]1NC(=O)[C@@H]2CCCCCSSCCCCC[C@H](NC(=O)[C@H]3CCCN3C1=O)C(=O)N2 InChI=1S/C24H40N4O4S2/c1-16(2)20-24(32)28-13-9-12-19(28)23(31)26-17-10-5-3-7-14-33-34-15-8-4-6-11-18(22(30)27-20)25-21(17)29/h16-20H,3-15H2,1-2H3,(H,25,29)(H,26,31)(H,27,30)/t17-,18-,19+,20-/m0/s1 GHEMSUBEZDZMNW-HAGHYFMRSA-N 50048862 CHEMBL3310510 Histone deacetylase 4 Homo sapiens 9.3 ChEMBL 10.1016/j.bmc.2014.06.029 10.7270/Q23F4R9P 24997578 Hoque, MA; Islam, MN; Islam, MS; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50048862 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50048862&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 102140473 103979243 CHEMBL3310510 ZINC13745270 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50276459 CC(C)[C@@H]1NC(=O)[C@H]2Cc3ccccc3CN2C(=O)[C@@H]2CCCCCSSCCCCC[C@@H](NC1=O)C(=O)N2 InChI=1S/C29H42N4O4S2/c1-19(2)25-28(36)30-22-13-5-3-9-15-38-39-16-10-4-6-14-23(31-26(22)34)29(37)33-18-21-12-8-7-11-20(21)17-24(33)27(35)32-25/h7-8,11-12,19,22-25H,3-6,9-10,13-18H2,1-2H3,(H,30,36)(H,31,34)(H,32,35)/t22-,23+,24-,25+/m1/s1 QUONJWHHYGIQCS-RCTAOEEJSA-N 50048863 CHEMBL3310511 Histone deacetylase 4 Homo sapiens 37 ChEMBL 10.1016/j.bmc.2014.06.029 10.7270/Q23F4R9P 24997578 Hoque, MA; Islam, MN; Islam, MS; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50048863 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50048863&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 102140474 103979244 CHEMBL3310511 ZINC13745309 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50272362 ONC(=O)\C=C\c1ccc(cc1)-c1nnc(Cc2cccc3ccccc23)o1 InChI=1S/C22H17N3O3/c26-20(25-27)13-10-15-8-11-17(12-9-15)22-24-23-21(28-22)14-18-6-3-5-16-4-1-2-7-19(16)18/h1-13,27H,14H2,(H,25,26)/b13-10+ LBRVMWDZJHBLGD-JLHYYAGUSA-N 50047965 CHEMBL3314859 Histone deacetylase 4 Homo sapiens >20000 25.00 C ChEMBL 10.1021/jm500303u 10.7270/Q2KK9DFZ 24972008 Valente, S; Trisciuoglio, D; De Luca, T; Nebbioso, A; Labella, D; Lenoci, A; Bigogno, C; Dondio, G; Miceli, M; Brosch, G; Del Bufalo, D; Altucci, L; Mai, A Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50047965 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50047965&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118707835 103978529 CHEMBL3314859 ZINC13828031 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50272363 ONC(=O)\C=C\c1ccc(cc1)-c1nnc(Cc2c[nH]c3ccccc23)o1 InChI=1S/C20H16N4O3/c25-18(24-26)10-7-13-5-8-14(9-6-13)20-23-22-19(27-20)11-15-12-21-17-4-2-1-3-16(15)17/h1-10,12,21,26H,11H2,(H,24,25)/b10-7+ MTSNUBCDRYSBCQ-JXMROGBWSA-N 50047966 CHEMBL3314860 Histone deacetylase 4 Homo sapiens 15200 25.00 C ChEMBL 10.1021/jm500303u 10.7270/Q2KK9DFZ 24972008 Valente, S; Trisciuoglio, D; De Luca, T; Nebbioso, A; Labella, D; Lenoci, A; Bigogno, C; Dondio, G; Miceli, M; Brosch, G; Del Bufalo, D; Altucci, L; Mai, A Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50047966 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50047966&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118707836 103978530 CHEMBL3314860 ZINC13828037 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50272364 ONC(=O)\C=C\c1ccc(Cc2nnc(Cc3cccc4ccccc34)o2)cc1 InChI=1S/C23H19N3O3/c27-21(26-28)13-12-16-8-10-17(11-9-16)14-22-24-25-23(29-22)15-19-6-3-5-18-4-1-2-7-20(18)19/h1-13,28H,14-15H2,(H,26,27)/b13-12+ DQHBWINPWGGELF-OUKQBFOZSA-N 50047967 CHEMBL3314861 Histone deacetylase 4 Homo sapiens >20000 25.00 C ChEMBL 10.1021/jm500303u 10.7270/Q2KK9DFZ 24972008 Valente, S; Trisciuoglio, D; De Luca, T; Nebbioso, A; Labella, D; Lenoci, A; Bigogno, C; Dondio, G; Miceli, M; Brosch, G; Del Bufalo, D; Altucci, L; Mai, A Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50047967 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50047967&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 102366363 103978531 CHEMBL3314861 ZINC13828097 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50272365 ONC(=O)c1ccc(cc1)-c1nnc(Cc2cccc3ccccc23)o1 InChI=1S/C20H15N3O3/c24-19(23-25)14-8-10-15(11-9-14)20-22-21-18(26-20)12-16-6-3-5-13-4-1-2-7-17(13)16/h1-11,25H,12H2,(H,23,24) IEMDXTSVGWZPBE-UHFFFAOYSA-N 50047968 CHEMBL3314862 Histone deacetylase 4 Homo sapiens >20000 25.00 C ChEMBL 10.1021/jm500303u 10.7270/Q2KK9DFZ 24972008 Valente, S; Trisciuoglio, D; De Luca, T; Nebbioso, A; Labella, D; Lenoci, A; Bigogno, C; Dondio, G; Miceli, M; Brosch, G; Del Bufalo, D; Altucci, L; Mai, A Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50047968 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50047968&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118707837 103978532 CHEMBL3314862 ZINC13828101 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50272366 ONC(=O)c1ccc(Cc2nnc(Cc3cccc4ccccc34)o2)cc1 InChI=1S/C21H17N3O3/c25-21(24-26)16-10-8-14(9-11-16)12-19-22-23-20(27-19)13-17-6-3-5-15-4-1-2-7-18(15)17/h1-11,26H,12-13H2,(H,24,25) DDGIZMVSUKBZPG-UHFFFAOYSA-N 50047969 CHEMBL3314863 Histone deacetylase 4 Homo sapiens 7800 25.00 C ChEMBL 10.1021/jm500303u 10.7270/Q2KK9DFZ 24972008 Valente, S; Trisciuoglio, D; De Luca, T; Nebbioso, A; Labella, D; Lenoci, A; Bigogno, C; Dondio, G; Miceli, M; Brosch, G; Del Bufalo, D; Altucci, L; Mai, A Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50047969 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50047969&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 102366364 103978533 CHEMBL3314863 ZINC01551898 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50272367 Nc1ccccc1NC(=O)\C=C\c1ccc(cc1)-c1nnc(Cc2cccc3ccccc23)o1 InChI=1S/C28H22N4O2/c29-24-10-3-4-11-25(24)30-26(33)17-14-19-12-15-21(16-13-19)28-32-31-27(34-28)18-22-8-5-7-20-6-1-2-9-23(20)22/h1-17H,18,29H2,(H,30,33)/b17-14+ HFZJPVYVYYPCDO-SAPNQHFASA-N 50047970 CHEMBL3314864 Histone deacetylase 4 Homo sapiens >20000 25.00 C ChEMBL 10.1021/jm500303u 10.7270/Q2KK9DFZ 24972008 Valente, S; Trisciuoglio, D; De Luca, T; Nebbioso, A; Labella, D; Lenoci, A; Bigogno, C; Dondio, G; Miceli, M; Brosch, G; Del Bufalo, D; Altucci, L; Mai, A Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50047970 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50047970&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118707838 103978534 CHEMBL3314864 ZINC01916023 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50272368 Nc1ccccc1NC(=O)\C=C\c1ccc(cc1)-c1nnc(Cc2ccc3ccccc3c2)o1 InChI=1S/C28H22N4O2/c29-24-7-3-4-8-25(24)30-26(33)16-12-19-9-14-22(15-10-19)28-32-31-27(34-28)18-20-11-13-21-5-1-2-6-23(21)17-20/h1-17H,18,29H2,(H,30,33)/b16-12+ MBVDRTDKRGVQLM-FOWTUZBSSA-N 50047971 CHEMBL3314865 Histone deacetylase 4 Homo sapiens >20000 25.00 C ChEMBL 10.1021/jm500303u 10.7270/Q2KK9DFZ 24972008 Valente, S; Trisciuoglio, D; De Luca, T; Nebbioso, A; Labella, D; Lenoci, A; Bigogno, C; Dondio, G; Miceli, M; Brosch, G; Del Bufalo, D; Altucci, L; Mai, A Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50047971 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50047971&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118707839 103978535 CHEMBL3314865 ZINC13828072 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50272369 Nc1ccccc1NC(=O)\C=C\c1ccc(cc1)-c1nnc(Cc2c[nH]c3ccccc23)o1 InChI=1S/C26H21N5O2/c27-21-6-2-4-8-23(21)29-24(32)14-11-17-9-12-18(13-10-17)26-31-30-25(33-26)15-19-16-28-22-7-3-1-5-20(19)22/h1-14,16,28H,15,27H2,(H,29,32)/b14-11+ PUFWYPJNFHBIRO-SDNWHVSQSA-N 50047972 CHEMBL3314866 Histone deacetylase 4 Homo sapiens >20000 25.00 C ChEMBL 10.1021/jm500303u 10.7270/Q2KK9DFZ 24972008 Valente, S; Trisciuoglio, D; De Luca, T; Nebbioso, A; Labella, D; Lenoci, A; Bigogno, C; Dondio, G; Miceli, M; Brosch, G; Del Bufalo, D; Altucci, L; Mai, A Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50047972 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50047972&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118707840 103978536 CHEMBL3314866 ZINC13828078 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50272370 Nc1ccccc1NC(=O)\C=C\c1ccc(Cc2nnc(Cc3cccc4ccccc34)o2)cc1 InChI=1S/C29H24N4O2/c30-25-10-3-4-11-26(25)31-27(34)17-16-20-12-14-21(15-13-20)18-28-32-33-29(35-28)19-23-8-5-7-22-6-1-2-9-24(22)23/h1-17H,18-19,30H2,(H,31,34)/b17-16+ LZCZMMICURVBRI-WUKNDPDISA-N 50047973 CHEMBL3314867 Histone deacetylase 4 Homo sapiens >20000 25.00 C ChEMBL 10.1021/jm500303u 10.7270/Q2KK9DFZ 24972008 Valente, S; Trisciuoglio, D; De Luca, T; Nebbioso, A; Labella, D; Lenoci, A; Bigogno, C; Dondio, G; Miceli, M; Brosch, G; Del Bufalo, D; Altucci, L; Mai, A Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50047973 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50047973&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118707841 103978537 CHEMBL3314867 ZINC13828038 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50272371 Nc1ccccc1NC(=O)c1ccc(cc1)-c1nnc(Cc2cccc3ccccc23)o1 InChI=1S/C26H20N4O2/c27-22-10-3-4-11-23(22)28-25(31)18-12-14-19(15-13-18)26-30-29-24(32-26)16-20-8-5-7-17-6-1-2-9-21(17)20/h1-15H,16,27H2,(H,28,31) BQOWROLRGWBKOQ-UHFFFAOYSA-N 50047963 CHEMBL3314868 Histone deacetylase 4 Homo sapiens >20000 25.00 C ChEMBL 10.1021/jm500303u 10.7270/Q2KK9DFZ 24972008 Valente, S; Trisciuoglio, D; De Luca, T; Nebbioso, A; Labella, D; Lenoci, A; Bigogno, C; Dondio, G; Miceli, M; Brosch, G; Del Bufalo, D; Altucci, L; Mai, A Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50047963 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50047963&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118707842 103978527 CHEMBL3314868 ZINC13828090 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50272372 Nc1ccccc1NC(=O)c1ccc(Cc2nnc(Cc3cccc4ccccc34)o2)cc1 InChI=1S/C27H22N4O2/c28-23-10-3-4-11-24(23)29-27(32)20-14-12-18(13-15-20)16-25-30-31-26(33-25)17-21-8-5-7-19-6-1-2-9-22(19)21/h1-15H,16-17,28H2,(H,29,32) CRYKCIKWGVLKDT-UHFFFAOYSA-N 50047964 CHEMBL3314869 Histone deacetylase 4 Homo sapiens >20000 25.00 C ChEMBL 10.1021/jm500303u 10.7270/Q2KK9DFZ 24972008 Valente, S; Trisciuoglio, D; De Luca, T; Nebbioso, A; Labella, D; Lenoci, A; Bigogno, C; Dondio, G; Miceli, M; Brosch, G; Del Bufalo, D; Altucci, L; Mai, A Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50047964 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50047964&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 102366365 103978528 CHEMBL3314869 ZINC29473403 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50272373 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 8800 25.00 C ChEMBL 10.1021/jm500303u 10.7270/Q2KK9DFZ 24972008 Valente, S; Trisciuoglio, D; De Luca, T; Nebbioso, A; Labella, D; Lenoci, A; Bigogno, C; Dondio, G; Miceli, M; Brosch, G; Del Bufalo, D; Altucci, L; Mai, A Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50278953 CC[C@H](C)[C@@H]1NC(=O)[C@@H](Cc2ccc(OC)cc2)NC(=O)[C@H](CCCCCC(=O)NO)NC(=O)[C@H]2CCCN2C1=O InChI=1S/C29H43N5O7/c1-4-18(2)25-29(39)34-16-8-10-23(34)28(38)30-21(9-6-5-7-11-24(35)33-40)26(36)31-22(27(37)32-25)17-19-12-14-20(41-3)15-13-19/h12-15,18,21-23,25,40H,4-11,16-17H2,1-3H3,(H,30,38)(H,31,36)(H,32,37)(H,33,35)/t18-,21-,22+,23+,25-/m0/s1 NXTMDUWTQZXRRK-GXCCDKSUSA-N 50051031 CHEMBL2158745 Histone deacetylase 4 Homo sapiens 3.0 ChEMBL 10.1016/j.bmc.2014.06.031 10.7270/Q2K93953 25022972 Islam, MN; Islam, MS; Hoque, MA; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50051031 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50051031&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71458561 313069347 CHEMBL2158745 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50278955 ONC(=O)CCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@@H]2CCCCCCCCCC[C@@H](NC1=O)C(=O)N2 InChI=1S/C27H45N5O6/c33-23(31-38)17-11-7-10-14-20-24(34)28-19-13-8-5-3-1-2-4-6-9-15-21(30-25(19)35)27(37)32-18-12-16-22(32)26(36)29-20/h19-22,38H,1-18H2,(H,28,34)(H,29,36)(H,30,35)(H,31,33)/t19-,20+,21+,22-/m1/s1 BVYNKHHGAJSMBT-CLAROIROSA-N 50309930 6-((1S,7R,10S,13R)-2,8,11,25-Tetraoxo-3,9,12,24-tetraaza-tricyclo[11.10.2.0*3,7*]pentacos-10-yl)-hexanoic acid hydroxyamide::CHEMBL592719 Histone deacetylase 4 Homo sapiens 5.5 ChEMBL 10.1016/j.bmc.2014.06.031 10.7270/Q2K93953 25022972 Islam, MN; Islam, MS; Hoque, MA; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50309930 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50309930&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 46216759 104164291 CHEMBL592719 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50278956 CCCCC[C@H]1NC(=O)[C@H](CCCCCC(=O)NO)NC(=O)[C@H]2CCCN2C(=O)[C@H](CCCCC)NC1=O InChI=1S/C27H47N5O6/c1-3-5-8-13-19-25(35)30-21(15-9-6-4-2)27(37)32-18-12-16-22(32)26(36)29-20(24(34)28-19)14-10-7-11-17-23(33)31-38/h19-22,38H,3-18H2,1-2H3,(H,28,34)(H,29,36)(H,30,35)(H,31,33)/t19-,20+,21+,22-/m1/s1 IYOLVIFIJXUYFW-CLAROIROSA-N 50309933 6-((5S,8R,11S,13aR)-4,7,10,13-Tetraoxo-5,8-dipentyl-tetradecahydro-3a,6,9,12-tetraaza-cyclopentacyclododecen-11-yl)-hexanoic acid hydroxyamide::CHEMBL589906 Histone deacetylase 4 Homo sapiens 12 ChEMBL 10.1016/j.bmc.2014.06.031 10.7270/Q2K93953 25022972 Islam, MN; Islam, MS; Hoque, MA; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50309933 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50309933&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 46230638 104164294 CHEMBL589906 ZINC49746063 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50278957 ONC(=O)CCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@@H]2CCOCCCCOCC[C@@H](NC1=O)C(=O)N2 InChI=1S/C25H41N5O8/c31-21(29-36)9-3-1-2-7-17-22(32)26-18-10-15-37-13-4-5-14-38-16-11-19(28-23(18)33)25(35)30-12-6-8-20(30)24(34)27-17/h17-20,36H,1-16H2,(H,26,32)(H,27,34)(H,28,33)(H,29,31)/t17-,18+,19-,20+/m0/s1 MXKQXLASRORHNH-ZGXWSNOMSA-N 50051032 CHEMBL3309855 Histone deacetylase 4 Homo sapiens 41 ChEMBL 10.1016/j.bmc.2014.06.031 10.7270/Q2K93953 25022972 Islam, MN; Islam, MS; Hoque, MA; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50051032 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50051032&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118706143 313069348 CHEMBL3309855 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50278959 ONC(=O)CCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@@H]2CCCCCCCCCC[C@H](NC1=O)C(=O)N2 InChI=1S/C27H45N5O6/c33-23(31-38)17-11-7-10-14-20-24(34)28-19-13-8-5-3-1-2-4-6-9-15-21(30-25(19)35)27(37)32-18-12-16-22(32)26(36)29-20/h19-22,38H,1-18H2,(H,28,34)(H,29,36)(H,30,35)(H,31,33)/t19-,20-,21-,22+/m0/s1 BVYNKHHGAJSMBT-MYGLTJDJSA-N 50051033 CHEMBL3309856 Histone deacetylase 4 Homo sapiens 26 ChEMBL 10.1016/j.bmc.2014.06.031 10.7270/Q2K93953 25022972 Islam, MN; Islam, MS; Hoque, MA; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50051033 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50051033&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118706144 313069349 CHEMBL3309856 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50278960 ONC(=O)CCCCC[C@@H]1NC(=O)[C@H]2CCCCCCCCCC[C@H](NC(=O)[C@H]3CCCN3C1=O)C(=O)N2 InChI=1S/C27H45N5O6/c33-23(31-38)17-11-7-10-15-21-27(37)32-18-12-16-22(32)26(36)29-20-14-9-6-4-2-1-3-5-8-13-19(25(35)30-21)28-24(20)34/h19-22,38H,1-18H2,(H,28,34)(H,29,36)(H,30,35)(H,31,33)/t19-,20+,21+,22-/m1/s1 FESQCEOPKBAIAM-CLAROIROSA-N 50051034 CHEMBL3309857 Histone deacetylase 4 Homo sapiens 31 ChEMBL 10.1016/j.bmc.2014.06.031 10.7270/Q2K93953 25022972 Islam, MN; Islam, MS; Hoque, MA; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50051034 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50051034&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118706145 313069350 CHEMBL3309857 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50278962 CCCCC[C@@H]1NC(=O)[C@H](CCCCCC(=O)NO)NC(=O)[C@H]2CCCN2C(=O)[C@H](CCCCC)NC1=O InChI=1S/C27H47N5O6/c1-3-5-8-13-19-25(35)30-21(15-9-6-4-2)27(37)32-18-12-16-22(32)26(36)29-20(24(34)28-19)14-10-7-11-17-23(33)31-38/h19-22,38H,3-18H2,1-2H3,(H,28,34)(H,29,36)(H,30,35)(H,31,33)/t19-,20-,21-,22+/m0/s1 IYOLVIFIJXUYFW-MYGLTJDJSA-N 50051035 CHEMBL3309858 Histone deacetylase 4 Homo sapiens 15 ChEMBL 10.1016/j.bmc.2014.06.031 10.7270/Q2K93953 25022972 Islam, MN; Islam, MS; Hoque, MA; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50051035 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50051035&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118706146 313069351 CHEMBL3309858 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50278963 CCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@H](CCCCCC(=O)NO)NC(=O)[C@@H](CCCCC)NC1=O InChI=1S/C27H47N5O6/c1-3-5-8-13-19-25(35)30-21(15-10-7-11-17-23(33)31-38)27(37)32-18-12-16-22(32)26(36)29-20(24(34)28-19)14-9-6-4-2/h19-22,38H,3-18H2,1-2H3,(H,28,34)(H,29,36)(H,30,35)(H,31,33)/t19-,20+,21+,22-/m1/s1 IAXSAHXPKHCCRC-CLAROIROSA-N 50051036 CHEMBL3356087 Histone deacetylase 4 Homo sapiens 43 ChEMBL 10.1016/j.bmc.2014.06.031 10.7270/Q2K93953 25022972 Islam, MN; Islam, MS; Hoque, MA; Kato, T; Nishino, N; Ito, A; Yoshida, M University of Rajshahi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50051036 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50051036&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118721286 313069352 CHEMBL3356087 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50319085 ONC(=O)\C=C\c1ccc2C(=O)N(Cc3ccccc3)C(=O)c2c1 InChI=1S/C18H14N2O4/c21-16(19-24)9-7-12-6-8-14-15(10-12)18(23)20(17(14)22)11-13-4-2-1-3-5-13/h1-10,24H,11H2,(H,19,21)/b9-7+ VNUHFKHIYWNVCQ-VQHVLOKHSA-N 50172787 (E)-3-(2-Benzyl-1,3-dioxo-2,3-dihydro-1H-isoindol-5-yl)-N-hydroxy-acrylamide::3-(2-benzyl-1,3-dioxoisoindolin-5-yl)-N-hydroxyacrylamide::CHEMBL197774 Histone deacetylase 4 Homo sapiens 358 ChEMBL 10.1016/j.bmcl.2005.07.048 10.7270/Q2BC3Z3K 16137884 Shinji, C; Nakamura, T; Maeda, S; Yoshida, M; Hashimoto, Y; Miyachi, H The University of Tokyo Yayoi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50172787 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50172787&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11652703 104058823 CHEMBL197774 ZINC28527909 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50338231 ONC(=O)\C=C\c1ccc(NC(=O)C(Cc2ccccc2)c2ccccc2)cn1 InChI=1S/C23H21N3O3/c27-22(26-29)14-13-19-11-12-20(16-24-19)25-23(28)21(18-9-5-2-6-10-18)15-17-7-3-1-4-8-17/h1-14,16,21,29H,15H2,(H,25,28)(H,26,27)/b14-13+ UQSIPNLHOWORHA-BUHFOSPRSA-N 50087841 CHEMBL3426804 Histone deacetylase 4 Homo sapiens 11700 ChEMBL 10.1021/acs.jmedchem.5b00126 10.7270/Q23X88DK 25905694 Di Pompo, G; Salerno, M; Rotili, D; Valente, S; Zwergel, C; Avnet, S; Lattanzi, G; Baldini, N; Mai, A Istituto Ortopedico Rizzoli (IOR) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50087841 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50087841&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118737400 103986869 CHEMBL3426804 ZINC13493926 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50338232 ONC(=O)CCCCSc1nc(cc(=O)[nH]1)-c1ccc(cc1)-c1ccccc1 InChI=1S/C21H21N3O3S/c25-19(24-27)8-4-5-13-28-21-22-18(14-20(26)23-21)17-11-9-16(10-12-17)15-6-2-1-3-7-15/h1-3,6-7,9-12,14,27H,4-5,8,13H2,(H,24,25)(H,22,23,26) AOFVDNFTELWRHV-UHFFFAOYSA-N 50087845 CHEMBL3426803 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1021/acs.jmedchem.5b00126 10.7270/Q23X88DK 25905694 Di Pompo, G; Salerno, M; Rotili, D; Valente, S; Zwergel, C; Avnet, S; Lattanzi, G; Baldini, N; Mai, A Istituto Ortopedico Rizzoli (IOR) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50087845 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50087845&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 49769453 103986873 CHEMBL3426803 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50338247 ONC(=O)CCCCCOc1no[n+]([O-])c1S(=O)(=O)c1ccccc1 InChI=1S/C14H17N3O7S/c18-12(15-19)9-5-2-6-10-23-13-14(17(20)24-16-13)25(21,22)11-7-3-1-4-8-11/h1,3-4,7-8,19H,2,5-6,9-10H2,(H,15,18) AGDGTFUFKSHWRN-UHFFFAOYSA-N 50087853 CHEMBL3426906 Histone deacetylase 4 Homo sapiens 30 ChEMBL 10.1021/acs.jmedchem.5b00317 10.7270/Q2057HP5 25906087 Duan, W; Li, J; Inks, ES; Chou, CJ; Jia, Y; Chu, X; Li, X; Xu, W; Zhang, Y Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50087853 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50087853&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118737455 103986881 CHEMBL3426906 ZINC29479440 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50338248 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >100 ChEMBL 10.1021/acs.jmedchem.5b00317 10.7270/Q2057HP5 25906087 Duan, W; Li, J; Inks, ES; Chou, CJ; Jia, Y; Chu, X; Li, X; Xu, W; Zhang, Y Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50355535 CC(C=CC(=O)NO)C=C(C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20) ALCVRKZFLFWUAZ-UHFFFAOYSA-N 19130 (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide::CHEMBL99::TSA::Trichostatin A (TSA) Histone deacetylase 4 Homo sapiens 34 ChEMBL 10.1021/jm060554y 10.7270/Q2M61JWX 16884291 Suzuki, T; Kouketsu, A; Itoh, Y; Hisakawa, S; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19130 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19130&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 91895926 46519165 46024 CHEMBL99 7005 ZINC05579377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50355537 CC(C)(C)OC(=O)N[C@@H](CCCCCS)C(=O)NC1CCCCCC1 InChI=1S/C19H36N2O3S/c1-19(2,3)24-18(23)21-16(13-9-6-10-14-25)17(22)20-15-11-7-4-5-8-12-15/h15-16,25H,4-14H2,1-3H3,(H,20,22)(H,21,23)/t16-/m0/s1 RTVMPAGMFUPGRI-INIZCTEOSA-N 19136 CHEMBL379049::tert-butyl N-[(1S)-1-(cycloheptylcarbamoyl)-6-sulfanylhexyl]carbamate::thiolate analogue, 18a Histone deacetylase 4 Homo sapiens 840 ChEMBL 10.1021/jm060554y 10.7270/Q2M61JWX 16884291 Suzuki, T; Kouketsu, A; Itoh, Y; Hisakawa, S; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19136 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19136&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11844893 46519171 CHEMBL379049 ZINC14969983 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50355540 CC(C)(C)OC(=O)N[C@@H](CCCCCS)C(=O)NC1CCCCC1 InChI=1S/C18H34N2O3S/c1-18(2,3)23-17(22)20-15(12-8-5-9-13-24)16(21)19-14-10-6-4-7-11-14/h14-15,24H,4-13H2,1-3H3,(H,19,21)(H,20,22)/t15-/m0/s1 NREURQUIJSGJMZ-HNNXBMFYSA-N 19135 CHEMBL209551::tert-butyl N-[(1S)-1-(cyclohexylcarbamoyl)-6-sulfanylhexyl]carbamate::thiolate analogue, 17a Histone deacetylase 4 Homo sapiens 1140 ChEMBL 10.1021/jm060554y 10.7270/Q2M61JWX 16884291 Suzuki, T; Kouketsu, A; Itoh, Y; Hisakawa, S; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19135 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19135&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11844892 46519170 CHEMBL209551 ZINC14969979 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50355542 CC(C)(C)OC(=O)N[C@@H](CCCCCS)C(=O)NC1CCCC1 InChI=1S/C17H32N2O3S/c1-17(2,3)22-16(21)19-14(11-5-4-8-12-23)15(20)18-13-9-6-7-10-13/h13-14,23H,4-12H2,1-3H3,(H,18,20)(H,19,21)/t14-/m0/s1 IKSFNOMXHPMYIQ-AWEZNQCLSA-N 19134 CHEMBL213934::tert-butyl N-[(1S)-1-(cyclopentylcarbamoyl)-6-sulfanylhexyl]carbamate::thiolate analogue, 16a Histone deacetylase 4 Homo sapiens 1030 ChEMBL 10.1021/jm060554y 10.7270/Q2M61JWX 16884291 Suzuki, T; Kouketsu, A; Itoh, Y; Hisakawa, S; Maeda, S; Yoshida, M; Nakagawa, H; Miyata, N Nagoya City University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19134 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19134&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11844891 46519169 CHEMBL213934 ZINC14969975 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50377004 C[C@@]12Nc3ccccc3[C@]1(O)CCN2Cc1ccc(\C=C\C(N)=O)cc1 InChI=1S/C21H23N3O2/c1-20-21(26,17-4-2-3-5-18(17)23-20)12-13-24(20)14-16-8-6-15(7-9-16)10-11-19(22)25/h2-11,23,26H,12-14H2,1H3,(H2,22,25)/b11-10+/t20-,21+/m0/s1 GSUOTZHCHGUHCC-HRZVIGLNSA-N 50103602 CHEMBL3526396 Histone deacetylase 4 Homo sapiens 1000 ChEMBL 10.1124/dmd.111.043620 10.7270/Q2SF2XX8 22344701 Fredenhagen, A; Kittelmann, M; Oberer, L; Kuhn, A; Kühnöl, J; Délémonté, T; Aichholz, R; Wang, P; Atadja, P; Shultz, MD Novartis Institutes for BioMedical Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50103602 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50103602&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118753027 318590132 CHEMBL3526396 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50377010 Cc1[nH]c2cc(O)ccc2c1CCNCc1ccc(\C=C\C(N)=O)cc1 InChI=1S/C21H23N3O2/c1-14-18(19-8-7-17(25)12-20(19)24-14)10-11-23-13-16-4-2-15(3-5-16)6-9-21(22)26/h2-9,12,23-25H,10-11,13H2,1H3,(H2,22,26)/b9-6+ UBAQJMHJQGDBBO-RMKNXTFCSA-N 50103603 CHEMBL3526942 Histone deacetylase 4 Homo sapiens 4600 ChEMBL 10.1124/dmd.111.043620 10.7270/Q2SF2XX8 22344701 Fredenhagen, A; Kittelmann, M; Oberer, L; Kuhn, A; Kühnöl, J; Délémonté, T; Aichholz, R; Wang, P; Atadja, P; Shultz, MD Novartis Institutes for BioMedical Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50103603 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50103603&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118753189 318590133 CHEMBL3526942 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50370636 C\C=C1/NC(=O)[C@@H](CS)NC(=O)[C@H](CC(=O)C[C@H](OC(=O)[C@@H](NC1=O)C(C)C)\C=C\CCS)C(C)C InChI=1S/C25H39N3O6S2/c1-6-19-23(31)28-21(15(4)5)25(33)34-17(9-7-8-10-35)11-16(29)12-18(14(2)3)22(30)27-20(13-36)24(32)26-19/h6-7,9,14-15,17-18,20-21,35-36H,8,10-13H2,1-5H3,(H,26,32)(H,27,30)(H,28,31)/b9-7+,19-6-/t17-,18-,20-,21+/m1/s1 UPCFDQLGZODPFB-BXJZLCHMSA-N 50354086 FK-228::Istodax::ROMIDEPSIN Histone deacetylase 4 Homo sapiens 647 ChEMBL 10.1021/ml500170r 10.7270/Q2RV0QFK 25147612 Salvador, LA; Park, H; Al-Awadhi, FH; Liu, Y; Kim, B; Zeller, SL; Chen, QY; Hong, J; Luesch, H University of Florida http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50354086 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50354086&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 49863499 136360772 ZINC58575686 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50377016 C[C@@]12Nc3ccccc3[C@]1(O)CCN2Cc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C21H23N3O3/c1-20-21(26,17-4-2-3-5-18(17)22-20)12-13-24(20)14-16-8-6-15(7-9-16)10-11-19(25)23-27/h2-11,22,26-27H,12-14H2,1H3,(H,23,25)/b11-10+/t20-,21+/m0/s1 XSPCNQCXKLBQPJ-HRZVIGLNSA-N 50103604 CHEMBL3526395 Histone deacetylase 4 Homo sapiens 230 ChEMBL 10.1124/dmd.111.043620 10.7270/Q2SF2XX8 22344701 Fredenhagen, A; Kittelmann, M; Oberer, L; Kuhn, A; Kühnöl, J; Délémonté, T; Aichholz, R; Wang, P; Atadja, P; Shultz, MD Novartis Institutes for BioMedical Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50103604 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50103604&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118753026 318590134 CHEMBL3526395 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50377023 Cc1[nH]c2ccccc2c1CCNCc1ccc(\C=C\C(N)=O)cc1 InChI=1S/C21H23N3O/c1-15-18(19-4-2-3-5-20(19)24-15)12-13-23-14-17-8-6-16(7-9-17)10-11-21(22)25/h2-11,23-24H,12-14H2,1H3,(H2,22,25)/b11-10+ VOZMMIFGJRFSNT-ZHACJKMWSA-N 50103605 CHEMBL3527525 Histone deacetylase 4 Homo sapiens 18000 ChEMBL 10.1124/dmd.111.043620 10.7270/Q2SF2XX8 22344701 Fredenhagen, A; Kittelmann, M; Oberer, L; Kuhn, A; Kühnöl, J; Délémonté, T; Aichholz, R; Wang, P; Atadja, P; Shultz, MD Novartis Institutes for BioMedical Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50103605 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50103605&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 24888322 318590135 CHEMBL3527525 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50377028 Cc1[nH]c2ccccc2c1CCNCc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C21H23N3O2/c1-15-18(19-4-2-3-5-20(19)23-15)12-13-22-14-17-8-6-16(7-9-17)10-11-21(25)24-26/h2-11,22-23,26H,12-14H2,1H3,(H,24,25)/b11-10+ FPOHNWQLNRZRFC-ZHACJKMWSA-N 29589 Faridak::LBH-589::LBH-589B::Panobinostat::US10722597, Compound Panobinostat Histone deacetylase 4 Homo sapiens 200 ChEMBL 10.1124/dmd.111.043620 10.7270/Q2SF2XX8 22344701 Fredenhagen, A; Kittelmann, M; Oberer, L; Kuhn, A; Kühnöl, J; Délémonté, T; Aichholz, R; Wang, P; Atadja, P; Shultz, MD Novartis Institutes for BioMedical Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=29589 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=29589&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search LBH 5EF8 6918837 81055018 ZINC22010649 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50391601 ONC(=O)\C=C\c1ccc2CN(Cc3ccccc3)C(=O)c2c1 InChI=1S/C18H16N2O3/c21-17(19-23)9-7-13-6-8-15-12-20(18(22)16(15)10-13)11-14-4-2-1-3-5-14/h1-10,23H,11-12H2,(H,19,21)/b9-7+ HQKPXSLXHXNAIC-VQHVLOKHSA-N 50216515 3-(2-benzyl-3-oxoisoindolin-5-yl)-N-hydroxyacrylamide::CHEMBL247217 Histone deacetylase 4 Homo sapiens 220 ChEMBL 10.1016/j.bmcl.2007.06.038 10.7270/Q2SF2VW0 17588744 Lee, S; Shinji, C; Ogura, K; Shimizu, M; Maeda, S; Sato, M; Yoshida, M; Hashimoto, Y; Miyachi, H The University of Tokyo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50216515 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50216515&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23649315 104090864 CHEMBL247217 ZINC28951906 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50391609 CC(C)(C)c1ccc(CN2Cc3ccc(\C=C\C(=O)NO)cc3C2=O)cc1 InChI=1S/C22H24N2O3/c1-22(2,3)18-9-5-16(6-10-18)13-24-14-17-8-4-15(7-11-20(25)23-27)12-19(17)21(24)26/h4-12,27H,13-14H2,1-3H3,(H,23,25)/b11-7+ FCBXDOAZFCPVJO-YRNVUSSQSA-N 50216519 3-(2-(4-tert-butylbenzyl)-3-oxoisoindolin-5-yl)-N-hydroxyacrylamide::CHEMBL247218 Histone deacetylase 4 Homo sapiens 180 ChEMBL 10.1016/j.bmcl.2007.06.038 10.7270/Q2SF2VW0 17588744 Lee, S; Shinji, C; Ogura, K; Shimizu, M; Maeda, S; Sato, M; Yoshida, M; Hashimoto, Y; Miyachi, H The University of Tokyo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50216519 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50216519&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44442437 104090868 CHEMBL247218 ZINC28951908 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50391611 ONC(=O)\C=C\c1ccc2CN(Cc3ccc(cc3)-c3cccnc3)C(=O)c2c1 InChI=1S/C23H19N3O3/c27-22(25-29)10-6-16-3-9-20-15-26(23(28)21(20)12-16)14-17-4-7-18(8-5-17)19-2-1-11-24-13-19/h1-13,29H,14-15H2,(H,25,27)/b10-6+ IALIYKZOWZSJRW-UXBLZVDNSA-N 50216518 3-(2-(4-(pyridin-3-yl)benzyl)-3-oxoisoindolin-5-yl)-N-hydroxyacrylamide::CHEMBL247654 Histone deacetylase 4 Homo sapiens 56 ChEMBL 10.1016/j.bmcl.2007.06.038 10.7270/Q2SF2VW0 17588744 Lee, S; Shinji, C; Ogura, K; Shimizu, M; Maeda, S; Sato, M; Yoshida, M; Hashimoto, Y; Miyachi, H The University of Tokyo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50216518 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50216518&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23626081 104090867 CHEMBL247654 ZINC28951911 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50391613 CC(C=CC(=O)NO)C=C(C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20) ALCVRKZFLFWUAZ-UHFFFAOYSA-N 19130 (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide::CHEMBL99::TSA::Trichostatin A (TSA) Histone deacetylase 4 Homo sapiens 29 ChEMBL 10.1016/j.bmcl.2007.06.038 10.7270/Q2SF2VW0 17588744 Lee, S; Shinji, C; Ogura, K; Shimizu, M; Maeda, S; Sato, M; Yoshida, M; Hashimoto, Y; Miyachi, H The University of Tokyo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19130 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19130&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 91895926 46519165 46024 CHEMBL99 7005 ZINC05579377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50391616 ONC(=O)\C=C\c1ccc2CN(Cc3ccc(cc3)-c3ccccc3)C(=O)c2c1 InChI=1S/C24H20N2O3/c27-23(25-29)13-9-17-6-12-21-16-26(24(28)22(21)14-17)15-18-7-10-20(11-8-18)19-4-2-1-3-5-19/h1-14,29H,15-16H2,(H,25,27)/b13-9+ BVZHTKWRPZSTLC-UKTHLTGXSA-N 50216517 3-(2-biphenyl-4-ylmethyl-3-oxo-2,3-dihydro-1H-isoindol-5-yl)-N-hydroxy-acrylamide::CHEMBL247653 Histone deacetylase 4 Homo sapiens 98 ChEMBL 10.1016/j.bmcl.2007.06.038 10.7270/Q2SF2VW0 17588744 Lee, S; Shinji, C; Ogura, K; Shimizu, M; Maeda, S; Sato, M; Yoshida, M; Hashimoto, Y; Miyachi, H The University of Tokyo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50216517 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50216517&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44442438 104090866 CHEMBL247653 ZINC28951909 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50391617 ONC(=O)\C=C\c1ccc2CN(Cc3ccc(cc3)-c3ccncc3)C(=O)c2c1 InChI=1S/C23H19N3O3/c27-22(25-29)8-4-16-1-7-20-15-26(23(28)21(20)13-16)14-17-2-5-18(6-3-17)19-9-11-24-12-10-19/h1-13,29H,14-15H2,(H,25,27)/b8-4+ IFRRSKDLVRTGSJ-XBXARRHUSA-N 50216516 3-(2-(4-(pyridin-4-yl)benzyl)-3-oxoisoindolin-5-yl)-N-hydroxyacrylamide::CHEMBL246199 Histone deacetylase 4 Homo sapiens 2100 ChEMBL 10.1016/j.bmcl.2007.06.038 10.7270/Q2SF2VW0 17588744 Lee, S; Shinji, C; Ogura, K; Shimizu, M; Maeda, S; Sato, M; Yoshida, M; Hashimoto, Y; Miyachi, H The University of Tokyo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50216516 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50216516&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44442439 104090865 CHEMBL246199 ZINC28951913 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50380978 Cn1cc(CNCC2CCN(CC2)c2ncc(cn2)C(=O)NO)c2ccccc12 InChI=1S/C21H26N6O2/c1-26-14-17(18-4-2-3-5-19(18)26)11-22-10-15-6-8-27(9-7-15)21-23-12-16(13-24-21)20(28)25-29/h2-5,12-15,22,29H,6-11H2,1H3,(H,25,28) PAWIYAYFNXQGAP-UHFFFAOYSA-N 50105327 JNJ-26481585::Quisinostat Histone deacetylase 4 Homo sapiens 0.300000 ChEMBL 10.1016/j.bmc.2014.12.066 10.7270/Q2B859V9 25637120 Carrillo, AK; Guiguemde, WA; Guy, RK St. Jude Children's Research Hospital http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105327 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105327&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search GOK 7Q1B,6HSK,6HSH 11538455 318590494 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50380981 Cc1[nH]c2ccccc2c1CCNCc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C21H23N3O2/c1-15-18(19-4-2-3-5-20(19)23-15)12-13-22-14-17-8-6-16(7-9-17)10-11-21(25)24-26/h2-11,22-23,26H,12-14H2,1H3,(H,24,25)/b11-10+ FPOHNWQLNRZRFC-ZHACJKMWSA-N 29589 Faridak::LBH-589::LBH-589B::Panobinostat::US10722597, Compound Panobinostat Histone deacetylase 4 Homo sapiens 550 ChEMBL 10.1016/j.bmc.2014.12.066 10.7270/Q2B859V9 25637120 Carrillo, AK; Guiguemde, WA; Guy, RK St. Jude Children's Research Hospital http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=29589 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=29589&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search LBH 5EF8 6918837 81055018 ZINC22010649 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50380986 ONC(=O)\C=C\c1cccc(c1)S(=O)(=O)Nc1ccccc1 InChI=1S/C15H14N2O4S/c18-15(16-19)10-9-12-5-4-8-14(11-12)22(20,21)17-13-6-2-1-3-7-13/h1-11,17,19H,(H,16,18)/b10-9+ NCNRHFGMJRPRSK-MDZDMXLPSA-N 25150 (2E)-N-hydroxy-3-[3-(phenylsulfamoyl)phenyl]prop-2-enamide::Belinosta::Belinostat::PXD-101::PXD101 Histone deacetylase 4 Homo sapiens 380 ChEMBL 10.1016/j.bmc.2014.12.066 10.7270/Q2B859V9 25637120 Carrillo, AK; Guiguemde, WA; Guy, RK St. Jude Children's Research Hospital http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25150 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25150&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5OG 5EEN 6918638 56374291 61076 ZINC03818726 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50380994 OCCN(CCc1c[nH]c2ccccc12)Cc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C22H25N3O3/c26-14-13-25(12-11-19-15-23-21-4-2-1-3-20(19)21)16-18-7-5-17(6-8-18)9-10-22(27)24-28/h1-10,15,23,26,28H,11-14,16H2,(H,24,27)/b10-9+ BWDQBBCUWLSASG-MDZDMXLPSA-N 19428 (2E)-N-hydroxy-3-(4-{[(2-hydroxyethyl)[2-(1H-indol-3-yl)ethyl]amino]methyl}phenyl)prop-2-enamide::(E)-N-hydroxy-3-[4-[[2-hydroxyethyl-[2-(1H-indol-3-yl)ethyl]amino]methyl]phenyl]prop-2-enamide::CHEMBL356066::Dacinostat::LAQ-824::NVP-LAQ824 Histone deacetylase 4 Homo sapiens 2250 ChEMBL 10.1016/j.bmc.2014.12.066 10.7270/Q2B859V9 25637120 Carrillo, AK; Guiguemde, WA; Guy, RK St. Jude Children's Research Hospital http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19428 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19428&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6445533 46519450 CHEMBL356066 ZINC01494627 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50380995 OCc1ccc(cc1)[C@@H]1C[C@H](CSc2nc(c(o2)-c2ccccc2)-c2ccccc2)O[C@@H](O1)c1ccc(NC(=O)CCCCCCC(=O)NO)cc1 InChI=1S/C41H43N3O7S/c45-26-28-17-19-29(20-18-28)35-25-34(27-52-41-43-38(30-11-5-3-6-12-30)39(51-41)31-13-7-4-8-14-31)49-40(50-35)32-21-23-33(24-22-32)42-36(46)15-9-1-2-10-16-37(47)44-48/h3-8,11-14,17-24,34-35,40,45,48H,1-2,9-10,15-16,25-27H2,(H,42,46)(H,44,47)/t34-,35+,40+/m1/s1 BHUZLJOUHMBZQY-YXQOSMAKSA-N 22449 CHEMBL356769::N-(4-{(2R,4R,6S)-4-{[(4,5-diphenyl-1,3-oxazol-2-yl)sulfanyl]methyl}-6-[4-(hydroxymethyl)phenyl]-1,3-dioxan-2-yl}phenyl)-N -hydroxyoctanediamide::Tubacin::US9249087, Tubastatin A Histone deacetylase 4 Homo sapiens 9124 ChEMBL 10.1016/j.bmc.2014.12.066 10.7270/Q2B859V9 25637120 Carrillo, AK; Guiguemde, WA; Guy, RK St. Jude Children's Research Hospital http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=22449 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=22449&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6675804 49846263 CHEMBL356769 7374 ZINC27551136 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50380996 ONC(=O)\C=C\C#Cc1ccc(NS(=O)(=O)c2ccccc2)cc1 InChI=1S/C17H14N2O4S/c20-17(18-21)9-5-4-6-14-10-12-15(13-11-14)19-24(22,23)16-7-2-1-3-8-16/h1-3,5,7-13,19,21H,(H,18,20)/b9-5+ IVTKCTFTVKYWIQ-WEVVVXLNSA-N 50123957 (E)-5-(3-Benzenesulfonylamino-phenyl)-pent-2-en-4-ynoic acid hydroxyamide::(E)-5-(4-Benzenesulfonylamino-phenyl)-pent-2-en-4-ynoic acid hydroxyamide::5-(4-Benzenesulfonylamino-phenyl)-pent-2-en-4-ynoic acid hydroxyamide::CHEMBL314389::Oxamflatin Histone deacetylase 4 Homo sapiens 2033 ChEMBL 10.1016/j.bmc.2014.12.066 10.7270/Q2B859V9 25637120 Carrillo, AK; Guiguemde, WA; Guy, RK St. Jude Children's Research Hospital http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50123957 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50123957&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 10154438 104016324 CHEMBL314389 ZINC26500270 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50380997 C[C@H](\C=C(/C)\C=C\C(=O)NO)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1 RTKIYFITIVXBLE-QEQCGCAPSA-N 50005711 CHEBI:46024::GNF-Pf-1011::TRICHOSTATIN::Trichostatin A::Trichostatin A (TSA)::US10011611, Trichostatin A::US10722597, Compound Trichostatin::US11535598, Compound Trichostatin A::US9265734, TSA Histone deacetylase 4 Homo sapiens 1400 ChEMBL 10.1016/j.bmc.2014.12.066 10.7270/Q2B859V9 25637120 Carrillo, AK; Guiguemde, WA; Guy, RK St. Jude Children's Research Hospital http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 444732 242056952 DB04297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50380998 CCCCc1nc2cc(\C=C\C(=O)NO)ccc2n1CCN(CC)CC InChI=1S/C20H30N4O2/c1-4-7-8-19-21-17-15-16(10-12-20(25)22-26)9-11-18(17)24(19)14-13-23(5-2)6-3/h9-12,15,26H,4-8,13-14H2,1-3H3,(H,22,25)/b12-10+ JHDKZFFAIZKUCU-ZRDIBKRKSA-N 50105330 CHEMBL1851943 Histone deacetylase 4 Homo sapiens 16 ChEMBL 10.1016/j.bmc.2014.12.066 10.7270/Q2B859V9 25637120 Carrillo, AK; Guiguemde, WA; Guy, RK St. Jude Children's Research Hospital http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105330 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105330&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 49855250 318590496 CHEMBL1851943 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50380999 CCN(CC)Cc1ccc2cc(COC(=O)Nc3ccc(cc3)C(=O)NO)ccc2c1 InChI=1S/C24H27N3O4/c1-3-27(4-2)15-17-5-7-21-14-18(6-8-20(21)13-17)16-31-24(29)25-22-11-9-19(10-12-22)23(28)26-30/h5-14,30H,3-4,15-16H2,1-2H3,(H,25,29)(H,26,28) YALNUENQHAQXEA-UHFFFAOYSA-N 50105329 CHEMBL1213492 Histone deacetylase 4 Homo sapiens 1050 ChEMBL 10.1016/j.bmc.2014.12.066 10.7270/Q2B859V9 25637120 Carrillo, AK; Guiguemde, WA; Guy, RK St. Jude Children's Research Hospital http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105329 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105329&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search QCM 6UOC 9804992 318590495 CHEMBL1213492 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50383257 C=CCCCCCC[n+]1cccc(CCCCCCCCCCCC[n+]2cccc(CCCCC=C)c2)c1 InChI=1S/C36H58N2/c1-3-5-7-9-17-21-29-37-32-24-28-36(34-37)26-20-16-14-12-10-11-13-15-18-22-30-38-31-23-27-35(33-38)25-19-8-6-4-2/h3-4,23-24,27-28,31-34H,1-2,5-22,25-26,29-30H2/q+2 OYMYAUNGVBPOMQ-UHFFFAOYSA-N 50211062 3-(hex-5-enyl)-1-{12-[1-(oct-7-enyl)pyridinium-3-yl]dodecyl}-pyridinium chloride iodide::CHEMBL226817 Histone deacetylase 4 Homo sapiens >200000 ChEMBL 10.1021/jm070028m 10.7270/Q2FX795K 17447750 Perez-Balado, C; Nebbioso, A; Rodriguez-Grana, P; Minichiello, A; Miceli, M; Altucci, L; de Lera, AR Universidade de Vigo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50211062 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50211062&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 16658996 104087344 CHEMBL226817 ZINC28644660 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50383259 C=CCCCCCC[n+]1cccc(CCCCCCCCCCCC[n+]2cccc(CCCC=C)c2)c1 InChI=1S/C35H56N2/c1-3-5-7-8-16-20-28-37-31-23-27-35(33-37)25-19-15-13-11-9-10-12-14-17-21-29-36-30-22-26-34(32-36)24-18-6-4-2/h3-4,22-23,26-27,30-33H,1-2,5-21,24-25,28-29H2/q+2 MFLWWIMYHTZJAJ-UHFFFAOYSA-N 50211063 1-(oct-7-enyl)-3-{12-[3-(pent-4-enyl)pyridinium-1-yl]dodecyl}-pyridinium chloride iodide::CHEMBL226556 Histone deacetylase 4 Homo sapiens 540 ChEMBL 10.1021/jm070028m 10.7270/Q2FX795K 17447750 Perez-Balado, C; Nebbioso, A; Rodriguez-Grana, P; Minichiello, A; Miceli, M; Altucci, L; de Lera, AR Universidade de Vigo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50211063 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50211063&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 16659045 104087345 CHEMBL226556 ZINC28644543 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50409365 OC(=O)c1cccc(=S)n1O InChI=1S/C6H5NO3S/c8-6(9)4-2-1-3-5(11)7(4)10/h1-3,10H,(H,8,9) BNYCWOPXGQKREA-UHFFFAOYSA-N 50119287 CHEMBL3617543 Histone deacetylase 4 Homo sapiens 71000 ChEMBL 10.1016/j.bmcl.2015.07.065 10.7270/Q2930VZB 26264503 Muthyala, R; Shin, WS; Xie, J; Sham, YY University of Minnesota http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50119287 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50119287&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 59585196 319565813 CHEMBL3617543 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50409382 OC(=O)[C@H](NC(=O)c1cccc(=S)n1O)c1ccccc1 InChI=1S/C14H12N2O4S/c17-13(10-7-4-8-11(21)16(10)20)15-12(14(18)19)9-5-2-1-3-6-9/h1-8,12,20H,(H,15,17)(H,18,19)/t12-/m1/s1 MUTGTTZIVAJIJK-GFCCVEGCSA-N 50014161 CHEMBL3260858::US11491146, Compound 5 Histone deacetylase 4 Homo sapiens 64000 ChEMBL 10.1016/j.bmcl.2015.07.065 10.7270/Q2930VZB 26264503 Muthyala, R; Shin, WS; Xie, J; Sham, YY University of Minnesota http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50014161 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50014161&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86294747 103926183 CHEMBL3260858 ZINC26656113 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50409384 C[C@H](\C=C(/C)\C=C\C(=O)NO)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1 RTKIYFITIVXBLE-QEQCGCAPSA-N 50005711 CHEBI:46024::GNF-Pf-1011::TRICHOSTATIN::Trichostatin A::Trichostatin A (TSA)::US10011611, Trichostatin A::US10722597, Compound Trichostatin::US11535598, Compound Trichostatin A::US9265734, TSA Histone deacetylase 4 Homo sapiens 9100 ChEMBL 10.1016/j.bmcl.2015.07.065 10.7270/Q2930VZB 26264503 Muthyala, R; Shin, WS; Xie, J; Sham, YY University of Minnesota http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 444732 242056952 DB04297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50409385 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 76000 ChEMBL 10.1016/j.bmcl.2015.07.065 10.7270/Q2930VZB 26264503 Muthyala, R; Shin, WS; Xie, J; Sham, YY University of Minnesota http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50400937 C[C@@H]1NC(=O)[C@@](C)(Cc2ccccc2)NC(=O)[C@H](CCCCCSSc2ccccn2)NC(=O)[C@H]2CCCN2C1=O InChI=1S/C30H39N5O4S2/c1-21-28(38)35-18-11-15-24(35)27(37)33-23(14-7-4-10-19-40-41-25-16-8-9-17-31-25)26(36)34-30(2,29(39)32-21)20-22-12-5-3-6-13-22/h3,5-6,8-9,12-13,16-17,21,23-24H,4,7,10-11,14-15,18-20H2,1-2H3,(H,32,39)(H,33,37)(H,34,36)/t21-,23-,24+,30+/m0/s1 ITTWBEZYTYPCGB-HVGAQBFTSA-N 50222731 CHEMBL393261::cyclo(-L-Am7(S2Py)-D-2MePhe-L-Ala-D-Pro-) Histone deacetylase 4 Homo sapiens 70 ChEMBL 10.1016/j.bmc.2007.08.041 10.7270/Q2BG2NQK 17881232 Shivashimpi, GM; Amagai, S; Kato, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50222731 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50222731&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44437873 104094979 CHEMBL393261 C15496 ZINC28876422 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50400943 C[C@@H]1NC(=O)[C@]2(CCc3ccccc23)NC(=O)[C@H](CCCCCSSc2ccccn2)NC(=O)[C@H]2CCCN2C1=O InChI=1S/C30H37N5O4S2/c1-20-28(38)35-18-9-13-24(35)27(37)33-23(12-3-2-8-19-40-41-25-14-6-7-17-31-25)26(36)34-30(29(39)32-20)16-15-21-10-4-5-11-22(21)30/h4-7,10-11,14,17,20,23-24H,2-3,8-9,12-13,15-16,18-19H2,1H3,(H,32,39)(H,33,37)(H,34,36)/t20-,23-,24+,30+/m0/s1 ZGCIQVPLYZBUHQ-AEPSZFNXSA-N 50222726 CHEMBL393260::cyclo(-L-Am7(S2Py)-L-A1in-L-Ala-D-Pro-) Histone deacetylase 4 Homo sapiens 25 ChEMBL 10.1016/j.bmc.2007.08.041 10.7270/Q2BG2NQK 17881232 Shivashimpi, GM; Amagai, S; Kato, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50222726 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50222726&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44437872 104094974 CHEMBL393260 C15496 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50400945 C[C@@H]1NC(=O)C2(Cc3ccccc3C2)NC(=O)[C@H](CCCCCSSc2ccccn2)NC(=O)[C@H]2CCCN2C1=O InChI=1S/C30H37N5O4S2/c1-20-28(38)35-16-9-13-24(35)27(37)33-23(12-3-2-8-17-40-41-25-14-6-7-15-31-25)26(36)34-30(29(39)32-20)18-21-10-4-5-11-22(21)19-30/h4-7,10-11,14-15,20,23-24H,2-3,8-9,12-13,16-19H2,1H3,(H,32,39)(H,33,37)(H,34,36)/t20-,23-,24+/m0/s1 RKZORBYVFSJNHI-NKKJXINNSA-N 50222728 CHEMBL394261::cyclo(-L-Am7(S2Py)-A2in-L-Ala-D-Pro-) Histone deacetylase 4 Homo sapiens 1.6 ChEMBL 10.1016/j.bmc.2007.08.041 10.7270/Q2BG2NQK 17881232 Shivashimpi, GM; Amagai, S; Kato, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50222728 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50222728&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44437869 104094976 CHEMBL394261 C15496 ZINC28876412 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50400947 CC1(C)NC(=O)[C@H](CCCCCSSc2ccccn2)NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC1=O InChI=1S/C30H39N5O4S2/c1-30(2)29(39)33-23(20-21-12-5-3-6-13-21)28(38)35-18-11-15-24(35)27(37)32-22(26(36)34-30)14-7-4-10-19-40-41-25-16-8-9-17-31-25/h3,5-6,8-9,12-13,16-17,22-24H,4,7,10-11,14-15,18-20H2,1-2H3,(H,32,37)(H,33,39)(H,34,36)/t22-,23-,24+/m0/s1 GNIYZHFLRFNYMZ-KMDXXIMOSA-N 50222732 (5S,11S,13aR)-5-benzyl-8,8-dimethyl-11-[5-(pyridin-2-yldisulfanyl)-pentyl]-decahydro-3a,6,9,12-tetraaza-cyclopentacyclododecene-4,7,10,13-tetraone::CHEMBL238829::cyclo(-L-Am7(S2Py)-Aib-L-Phe-D-Pro-) Histone deacetylase 4 Homo sapiens 1.8 ChEMBL 10.1016/j.bmc.2007.08.041 10.7270/Q2BG2NQK 17881232 Shivashimpi, GM; Amagai, S; Kato, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50222732 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50222732&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44437868 104094980 CHEMBL238829 C15496 ZINC28876406 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50400957 CC1(C)NC(=O)[C@H](CCCCCSSc2ccccn2)NC(=O)[C@H]2CCCN2C(=O)[C@H](CO)NC1=O InChI=1S/C24H35N5O5S2/c1-24(2)23(34)27-17(15-30)22(33)29-13-8-10-18(29)21(32)26-16(20(31)28-24)9-4-3-7-14-35-36-19-11-5-6-12-25-19/h5-6,11-12,16-18,30H,3-4,7-10,13-15H2,1-2H3,(H,26,32)(H,27,34)(H,28,31)/t16-,17-,18+/m0/s1 HNLHPMBNXUOXHG-OKZBNKHCSA-N 50222733 CHEMBL393961::cyclo(-L-Am7(S2Py)-Aib-L-Ser-D-Pro-) Histone deacetylase 4 Homo sapiens 4 ChEMBL 10.1016/j.bmc.2007.08.041 10.7270/Q2BG2NQK 17881232 Shivashimpi, GM; Amagai, S; Kato, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50222733 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50222733&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44437880 104094981 CHEMBL393961 C15496 ZINC28876460 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50400960 CC1(C)NC(=O)[C@H](CCCCCSSc2ccccn2)NC(=O)[C@H]2CCCN2C(=O)[C@H](COCc2ccccc2)NC1=O InChI=1S/C31H41N5O5S2/c1-31(2)30(40)34-24(21-41-20-22-12-5-3-6-13-22)29(39)36-18-11-15-25(36)28(38)33-23(27(37)35-31)14-7-4-10-19-42-43-26-16-8-9-17-32-26/h3,5-6,8-9,12-13,16-17,23-25H,4,7,10-11,14-15,18-21H2,1-2H3,(H,33,38)(H,34,40)(H,35,37)/t23-,24-,25+/m0/s1 UAUCMCUCWAXYRK-CCDWMCETSA-N 50222736 CHEMBL241555::cyclo(-L-Am7(S2Py)-Aib-L-Ser(Bzl)-D-Pro-) Histone deacetylase 4 Homo sapiens 1.6 ChEMBL 10.1016/j.bmc.2007.08.041 10.7270/Q2BG2NQK 17881232 Shivashimpi, GM; Amagai, S; Kato, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50222736 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50222736&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44437879 104094984 CHEMBL241555 C15496 ZINC28876454 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50400961 C[C@@H]1NC(=O)[C@@]2(CCc3ccccc23)NC(=O)[C@H](CCCCCSSc2ccccn2)NC(=O)[C@H]2CCCN2C1=O InChI=1S/C30H37N5O4S2/c1-20-28(38)35-18-9-13-24(35)27(37)33-23(12-3-2-8-19-40-41-25-14-6-7-17-31-25)26(36)34-30(29(39)32-20)16-15-21-10-4-5-11-22(21)30/h4-7,10-11,14,17,20,23-24H,2-3,8-9,12-13,15-16,18-19H2,1H3,(H,32,39)(H,33,37)(H,34,36)/t20-,23-,24+,30-/m0/s1 ZGCIQVPLYZBUHQ-KGPFVPCYSA-N 50222735 CHEMBL390991::cyclo(-L-Am7(S2Py)-D-A1in-L-Ala-D-Pro-) Histone deacetylase 4 Homo sapiens 2.4 ChEMBL 10.1016/j.bmc.2007.08.041 10.7270/Q2BG2NQK 17881232 Shivashimpi, GM; Amagai, S; Kato, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50222735 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50222735&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44437870 104094983 CHEMBL390991 C15496 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50400964 C[C@H]1CN2Cc3ccccc3C[C@@H]2C(=O)N[C@@H](CCCCCSSc2ccccn2)C(=O)NC(C)(C)C(=O)N1 InChI=1S/C29H39N5O3S2/c1-20-18-34-19-22-12-7-6-11-21(22)17-24(34)27(36)32-23(26(35)33-29(2,3)28(37)31-20)13-5-4-10-16-38-39-25-14-8-9-15-30-25/h6-9,11-12,14-15,20,23-24H,4-5,10,13,16-19H2,1-3H3,(H,31,37)(H,32,36)(H,33,35)/t20-,23-,24+/m0/s1 ALYDIERJMKHYLO-NKKJXINNSA-N 50222737 CHEMBL238587::cyclo(-L-Am7(S2Py)-Aib-L-Ala-D-Tic-) Histone deacetylase 4 Homo sapiens 4.2 ChEMBL 10.1016/j.bmc.2007.08.041 10.7270/Q2BG2NQK 17881232 Shivashimpi, GM; Amagai, S; Kato, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50222737 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50222737&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44437875 104094985 CHEMBL238587 C15496 ZINC28876433 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50400965 C[C@@H]1NC(=O)C(C)(C)NC(=O)[C@H](CCCCCSSc2ccccn2)NC(=O)[C@H]2CCCN2C1=O InChI=1S/C24H35N5O4S2/c1-16-22(32)29-14-9-11-18(29)21(31)27-17(20(30)28-24(2,3)23(33)26-16)10-5-4-8-15-34-35-19-12-6-7-13-25-19/h6-7,12-13,16-18H,4-5,8-11,14-15H2,1-3H3,(H,26,33)(H,27,31)(H,28,30)/t16-,17-,18+/m0/s1 SNOZDSAKXKVXTD-OKZBNKHCSA-N 50222727 (5S,11S,13aR)-5,8,8-trimethyl-11-[5-(pyridin-2-yldisulfanyl)-pentyl]-decahydro-3a,6,9,12-tetraaza-cyclopetacyclododecene-4,7,10,13-tetraone::CHEMBL238596::cyclo(-L-Am7(S2Py)-Aib-L-Ala-D-Pro-) Histone deacetylase 4 Homo sapiens 5.2 ChEMBL 10.1016/j.bmc.2007.08.041 10.7270/Q2BG2NQK 17881232 Shivashimpi, GM; Amagai, S; Kato, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50222727 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50222727&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44437883 104094975 CHEMBL238596 C15496 ZINC28876465 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50400967 CC1(C)NC(=O)[C@H](CCCCCSSc2ccccn2)NC(=O)[C@H]2CCCN2C(=O)[C@@H](NC1=O)c1ccccc1 InChI=1S/C29H37N5O4S2/c1-29(2)28(38)32-24(20-12-5-3-6-13-20)27(37)34-18-11-15-22(34)26(36)31-21(25(35)33-29)14-7-4-10-19-39-40-23-16-8-9-17-30-23/h3,5-6,8-9,12-13,16-17,21-22,24H,4,7,10-11,14-15,18-19H2,1-2H3,(H,31,36)(H,32,38)(H,33,35)/t21-,22+,24-/m0/s1 MAESVPGWPSVAHM-ZDXQCDESSA-N 50222734 CHEMBL428737::cyclo(-L-Am7(S2Py)-Aib-L-Phg-D-Pro-) Histone deacetylase 4 Homo sapiens 56 ChEMBL 10.1016/j.bmc.2007.08.041 10.7270/Q2BG2NQK 17881232 Shivashimpi, GM; Amagai, S; Kato, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50222734 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50222734&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44437876 104094982 CHEMBL428737 C15496 ZINC28876438 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50400970 CC1(C)NC(=O)[C@H](CCCCCSSc2ccccn2)NC(=O)[C@H]2CCCN2C(=O)[C@H](CCCc2ccccc2)NC1=O InChI=1S/C32H43N5O4S2/c1-32(2)31(41)35-25(17-11-15-23-13-5-3-6-14-23)30(40)37-21-12-18-26(37)29(39)34-24(28(38)36-32)16-7-4-10-22-42-43-27-19-8-9-20-33-27/h3,5-6,8-9,13-14,19-20,24-26H,4,7,10-12,15-18,21-22H2,1-2H3,(H,34,39)(H,35,41)(H,36,38)/t24-,25-,26+/m0/s1 DIIWIWBDXZTFQP-KKUQBAQOSA-N 50222729 CHEMBL391384::cyclo(-L-Am7(S2Py)-Aib-L-Ph5-D-Pro-) Histone deacetylase 4 Homo sapiens 2.7 ChEMBL 10.1016/j.bmc.2007.08.041 10.7270/Q2BG2NQK 17881232 Shivashimpi, GM; Amagai, S; Kato, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50222729 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50222729&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44437878 104094977 CHEMBL391384 C15496 ZINC28876449 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50400971 C[C@@H]1NC(=O)[C@](C)(Cc2ccccc2)NC(=O)[C@H](CCCCCSSc2ccccn2)NC(=O)[C@H]2CCCN2C1=O InChI=1S/C30H39N5O4S2/c1-21-28(38)35-18-11-15-24(35)27(37)33-23(14-7-4-10-19-40-41-25-16-8-9-17-31-25)26(36)34-30(2,29(39)32-21)20-22-12-5-3-6-13-22/h3,5-6,8-9,12-13,16-17,21,23-24H,4,7,10-11,14-15,18-20H2,1-2H3,(H,32,39)(H,33,37)(H,34,36)/t21-,23-,24+,30-/m0/s1 ITTWBEZYTYPCGB-GAOIQBMKSA-N 50222730 CHEMBL393464::cyclo(-L-Am7(S2Py)-L-2MePhe-L-Ala-D-Pro-) Histone deacetylase 4 Homo sapiens 2.2 ChEMBL 10.1016/j.bmc.2007.08.041 10.7270/Q2BG2NQK 17881232 Shivashimpi, GM; Amagai, S; Kato, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50222730 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50222730&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44437874 104094978 CHEMBL393464 C15496 ZINC28876428 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50400973 CC(C=CC(=O)NO)C=C(C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20) ALCVRKZFLFWUAZ-UHFFFAOYSA-N 19130 (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide::CHEMBL99::TSA::Trichostatin A (TSA) Histone deacetylase 4 Homo sapiens 2 ChEMBL 10.1016/j.bmc.2007.08.041 10.7270/Q2BG2NQK 17881232 Shivashimpi, GM; Amagai, S; Kato, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19130 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19130&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 91895926 46519165 46024 CHEMBL99 7005 ZINC05579377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50400974 CC1(C)NC(=O)[C@H](CCCCCSSc2ccccn2)NC(=O)[C@H]2CCCN2C(=O)[C@H](CCc2ccccc2)NC1=O InChI=1S/C31H41N5O4S2/c1-31(2)30(40)34-24(18-17-22-12-5-3-6-13-22)29(39)36-20-11-15-25(36)28(38)33-23(27(37)35-31)14-7-4-10-21-41-42-26-16-8-9-19-32-26/h3,5-6,8-9,12-13,16,19,23-25H,4,7,10-11,14-15,17-18,20-21H2,1-2H3,(H,33,38)(H,34,40)(H,35,37)/t23-,24-,25+/m0/s1 VOORCQROXYSHCG-CCDWMCETSA-N 50222738 CHEMBL391383::cyclo(-L-Am7(S2Py)-Aib-L-Ph4-D-Pro-) Histone deacetylase 4 Homo sapiens 3.2 ChEMBL 10.1016/j.bmc.2007.08.041 10.7270/Q2BG2NQK 17881232 Shivashimpi, GM; Amagai, S; Kato, T; Nishino, N; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50222738 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50222738&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44437877 104094986 CHEMBL391383 C15496 ZINC28876443 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50402033 CC(C)C[C@@H]1NC(=O)C(C)(C)NC(=O)[C@H](CCCCCSSc2ccccn2)NC(=O)[C@H]2CCCN2C1=O InChI=1S/C27H41N5O4S2/c1-18(2)17-20-25(35)32-15-10-12-21(32)24(34)29-19(23(33)31-27(3,4)26(36)30-20)11-6-5-9-16-37-38-22-13-7-8-14-28-22/h7-8,13-14,18-21H,5-6,9-12,15-17H2,1-4H3,(H,29,34)(H,30,36)(H,31,33)/t19-,20-,21+/m0/s1 NBFXEUJDLBNSLS-PCCBWWKXSA-N 50223504 (5S,11S,13aR)-5-isobutyl-8,8-dimethyl-11-[5-(pyridin-2-yldisulfanyl)-pentyl]-decahydro-3a,6,9,12-tetraaza-cyclopentacyclododecene-4,7,10,13-etraone::CHEMBL253309 Histone deacetylase 4 Homo sapiens 33 ChEMBL 10.1016/j.bmc.2007.09.021 10.7270/Q2RJ4J77 17900911 Nishino, N; Shivashimpi, GM; Soni, PB; Bhuiyan, MP; Kato, T; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50223504 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50223504&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44445958 104095541 CHEMBL253309 C15496 ZINC28975743 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50402036 CCCC[C@@H]1NC(=O)C(C)(C)NC(=O)[C@H](CCCCCSSc2ccccn2)NC(=O)[C@H]2CCCN2C1=O InChI=1S/C27H41N5O4S2/c1-4-5-12-20-25(35)32-17-11-14-21(32)24(34)29-19(23(33)31-27(2,3)26(36)30-20)13-7-6-10-18-37-38-22-15-8-9-16-28-22/h8-9,15-16,19-21H,4-7,10-14,17-18H2,1-3H3,(H,29,34)(H,30,36)(H,31,33)/t19-,20-,21+/m0/s1 QQWGTLPTAWCCOA-PCCBWWKXSA-N 50223506 (5S,11S,13aR)-5-butyl-8,8-dimethyl-11-[5-(pyridin-2-yldisulfanyl)-pentyl]-decahydro-3a,6,9,12-tetraaza-cyclopentacyclododecene-4,7,10,13-tetraone::CHEMBL401837 Histone deacetylase 4 Homo sapiens 24 ChEMBL 10.1016/j.bmc.2007.09.021 10.7270/Q2RJ4J77 17900911 Nishino, N; Shivashimpi, GM; Soni, PB; Bhuiyan, MP; Kato, T; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50223506 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50223506&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44445956 104095543 CHEMBL401837 C15496 ZINC28975731 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50402039 C[C@@H]1NC(=O)C(C)(C)NC(=O)[C@H](CCCCCSSc2ccccn2)NC(=O)[C@H]2CCCN2C1=O InChI=1S/C24H35N5O4S2/c1-16-22(32)29-14-9-11-18(29)21(31)27-17(20(30)28-24(2,3)23(33)26-16)10-5-4-8-15-34-35-19-12-6-7-13-25-19/h6-7,12-13,16-18H,4-5,8-11,14-15H2,1-3H3,(H,26,33)(H,27,31)(H,28,30)/t16-,17-,18+/m0/s1 SNOZDSAKXKVXTD-OKZBNKHCSA-N 50222727 (5S,11S,13aR)-5,8,8-trimethyl-11-[5-(pyridin-2-yldisulfanyl)-pentyl]-decahydro-3a,6,9,12-tetraaza-cyclopetacyclododecene-4,7,10,13-tetraone::CHEMBL238596::cyclo(-L-Am7(S2Py)-Aib-L-Ala-D-Pro-) Histone deacetylase 4 Homo sapiens 52 ChEMBL 10.1016/j.bmc.2007.09.021 10.7270/Q2RJ4J77 17900911 Nishino, N; Shivashimpi, GM; Soni, PB; Bhuiyan, MP; Kato, T; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50222727 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50222727&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44437883 104094975 CHEMBL238596 C15496 ZINC28876465 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50402041 CC(C=CC(=O)NO)C=C(C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20) ALCVRKZFLFWUAZ-UHFFFAOYSA-N 19130 (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide::CHEMBL99::TSA::Trichostatin A (TSA) Histone deacetylase 4 Homo sapiens 200 ChEMBL 10.1016/j.bmc.2007.09.021 10.7270/Q2RJ4J77 17900911 Nishino, N; Shivashimpi, GM; Soni, PB; Bhuiyan, MP; Kato, T; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19130 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19130&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 91895926 46519165 46024 CHEMBL99 7005 ZINC05579377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50402042 CC1(C)NC(=O)[C@H](CCCCCSSc2ccccn2)NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC1=O InChI=1S/C30H39N5O4S2/c1-30(2)29(39)33-23(20-21-12-5-3-6-13-21)28(38)35-18-11-15-24(35)27(37)32-22(26(36)34-30)14-7-4-10-19-40-41-25-16-8-9-17-31-25/h3,5-6,8-9,12-13,16-17,22-24H,4,7,10-11,14-15,18-20H2,1-2H3,(H,32,37)(H,33,39)(H,34,36)/t22-,23-,24+/m0/s1 GNIYZHFLRFNYMZ-KMDXXIMOSA-N 50222732 (5S,11S,13aR)-5-benzyl-8,8-dimethyl-11-[5-(pyridin-2-yldisulfanyl)-pentyl]-decahydro-3a,6,9,12-tetraaza-cyclopentacyclododecene-4,7,10,13-tetraone::CHEMBL238829::cyclo(-L-Am7(S2Py)-Aib-L-Phe-D-Pro-) Histone deacetylase 4 Homo sapiens 18 ChEMBL 10.1016/j.bmc.2007.09.021 10.7270/Q2RJ4J77 17900911 Nishino, N; Shivashimpi, GM; Soni, PB; Bhuiyan, MP; Kato, T; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50222732 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50222732&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44437868 104094980 CHEMBL238829 C15496 ZINC28876406 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50402043 O=C1N[C@@H](CCCCCSSc2ccccn2)C(=O)N[C@@H]2CCCCCCCCCCCC[C@H](NC2=O)C(=O)N2CCC[C@H]12 InChI=1S/C33H51N5O4S2/c39-30-26(18-12-9-15-24-43-44-29-21-13-14-22-34-29)36-32(41)28-20-16-23-38(28)33(42)27-19-11-8-6-4-2-1-3-5-7-10-17-25(35-30)31(40)37-27/h13-14,21-22,25-28H,1-12,15-20,23-24H2,(H,35,39)(H,36,41)(H,37,40)/t25-,26+,27+,28-/m1/s1 FKFLKOYVFNNGEX-WXIAYYLYSA-N 50223507 (1R,14S,20R,23S)-23-[5-(Pyridin-2-yldisulfanyl)-pentyl]-16,22,25,27-tetraaza-tricyclo[12.11.2.0 16,20]heptacosane-15,21,24,26-tetraone::CHEMBL404172 Histone deacetylase 4 Homo sapiens 20 ChEMBL 10.1016/j.bmc.2007.09.021 10.7270/Q2RJ4J77 17900911 Nishino, N; Shivashimpi, GM; Soni, PB; Bhuiyan, MP; Kato, T; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50223507 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50223507&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 24882475 104095544 CHEMBL404172 C15496 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50402045 CC[C@H](C)[C@@H]1NC(=O)C(C)(C)NC(=O)[C@H](CCCCCSSc2ccccn2)NC(=O)[C@H]2CCCN2C1=O InChI=1S/C27H41N5O4S2/c1-5-18(2)22-25(35)32-16-11-13-20(32)24(34)29-19(23(33)31-27(3,4)26(36)30-22)12-7-6-10-17-37-38-21-14-8-9-15-28-21/h8-9,14-15,18-20,22H,5-7,10-13,16-17H2,1-4H3,(H,29,34)(H,30,36)(H,31,33)/t18-,19-,20+,22-/m0/s1 AAWQZDISLGHBGI-KEZQHZCBSA-N 50223505 (5S,11S,13aR)-5-((S)-sec-butyl)-8,8-dimethyl-11-[5-(pyridin-2-yldisulfanyl)-pentyl]-decahydro-3a,6,9,12-tetraaza-cyclopentacyclododecene-4,7,10,13-tetraone::CHEMBL253308 Histone deacetylase 4 Homo sapiens 23 ChEMBL 10.1016/j.bmc.2007.09.021 10.7270/Q2RJ4J77 17900911 Nishino, N; Shivashimpi, GM; Soni, PB; Bhuiyan, MP; Kato, T; Maeda, S; Nishino, TG; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50223505 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50223505&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44445957 104095542 CHEMBL253308 C15496 ZINC28975737 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50409697 C[C@@H](NC(=O)c1cccc(=S)n1O)C(O)=O InChI=1S/C9H10N2O4S/c1-5(9(13)14)10-8(12)6-3-2-4-7(16)11(6)15/h2-5,15H,1H3,(H,10,12)(H,13,14)/t5-/m1/s1 CGTALJWGXQTLPE-RXMQYKEDSA-N 50014160 CHEMBL3260857 Histone deacetylase 4 Homo sapiens 100000 ChEMBL 10.1016/j.bmcl.2015.07.065 10.7270/Q2930VZB 26264503 Muthyala, R; Shin, WS; Xie, J; Sham, YY University of Minnesota http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50014160 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50014160&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86294741 103926182 CHEMBL3260857 ZINC26645818 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50412962 Nc1ccccc1NC(=O)c1ccc(s1)-c1cn(CCc2cccc(c2)[N+]([O-])=O)nn1 InChI=1S/C21H18N6O3S/c22-16-6-1-2-7-17(16)23-21(28)20-9-8-19(31-20)18-13-26(25-24-18)11-10-14-4-3-5-15(12-14)27(29)30/h1-9,12-13H,10-11,22H2,(H,23,28) AXAUXMXVFLCQQK-UHFFFAOYSA-N 50121211 CHEMBL3622375 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.5b00229 10.7270/Q2QZ2CSD 26086931 Zhan, P; Itoh, Y; Suzuki, T; Liu, X Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50121211 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50121211&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71721558 319566163 CHEMBL3622375 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50412967 Nc1ccccc1NC(=O)c1ccc(cc1)-c1cn(CCc2ccsc2)nn1 InChI=1S/C21H19N5OS/c22-18-3-1-2-4-19(18)23-21(27)17-7-5-16(6-8-17)20-13-26(25-24-20)11-9-15-10-12-28-14-15/h1-8,10,12-14H,9,11,22H2,(H,23,27) LBLSLSOENGWIHL-UHFFFAOYSA-N 50121210 CHEMBL3622374 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.5b00229 10.7270/Q2QZ2CSD 26086931 Zhan, P; Itoh, Y; Suzuki, T; Liu, X Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50121210 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50121210&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71721946 319566162 CHEMBL3622374 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50407621 Nc1ccccc1NC(=O)c1ccc(CNC(=O)OCc2cccnc2)cc1 InChI=1S/C21H20N4O3/c22-18-5-1-2-6-19(18)25-20(26)17-9-7-15(8-10-17)13-24-21(27)28-14-16-4-3-11-23-12-16/h1-12H,13-14,22H2,(H,24,27)(H,25,26) INVTYAOGFAGBOE-UHFFFAOYSA-N 19410 CHEMBL27759::MS-275::US11377423, MS-275::US11672788, Compound Entinostat::US9265734, MS-275::US9796664, Compound MS-275::benzamide-type inhibitor, 3::pyridin-3-ylmethyl N-({4-[(2-aminophenyl)carbamoyl]phenyl}methyl)carbamate Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2007.11.047 10.7270/Q28W3D1M 18060775 Witter, DJ; Harrington, P; Wilson, KJ; Chenard, M; Fleming, JC; Haines, B; Kral, AM; Secrist, JP; Miller, TA Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19410 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19410&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4261 46519433 CHEMBL27759 7007 ZINC01488870 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50407625 COC(=O)NCc1ccc(cc1)C(=O)Nc1cc(ccc1N)-c1cccs1 InChI=1S/C20H19N3O3S/c1-26-20(25)22-12-13-4-6-14(7-5-13)19(24)23-17-11-15(8-9-16(17)21)18-3-2-10-27-18/h2-11H,12,21H2,1H3,(H,22,25)(H,23,24) XPYFYVJCMDDGKF-UHFFFAOYSA-N 50229193 CHEMBL400721::US9096559, 17::methyl 4-((2-amino-5-(thiophen-2-yl)phenyl)carbamoyl)benzylcarbamate Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2007.11.047 10.7270/Q28W3D1M 18060775 Witter, DJ; Harrington, P; Wilson, KJ; Chenard, M; Fleming, JC; Haines, B; Kral, AM; Secrist, JP; Miller, TA Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50229193 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50229193&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44447194 104098087 CHEMBL400721 ZINC29039255 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50407646 Nc1ccc(cc1NC(=O)c1ccc(CNC(=O)OCc2cccnc2)cc1)-c1cccs1 InChI=1S/C25H22N4O3S/c26-21-10-9-20(23-4-2-12-33-23)13-22(21)29-24(30)19-7-5-17(6-8-19)15-28-25(31)32-16-18-3-1-11-27-14-18/h1-14H,15-16,26H2,(H,28,31)(H,29,30) ASIJNKHQTPQFCQ-UHFFFAOYSA-N 19412 CHEMBL235674::benzamide-type inhibitor, 4::pyridin-3-ylmethyl N-[(4-{[2-amino-5-(thiophen-2-yl)phenyl]carbamoyl}phenyl)methyl]carbamate Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2007.11.047 10.7270/Q28W3D1M 18060775 Witter, DJ; Harrington, P; Wilson, KJ; Chenard, M; Fleming, JC; Haines, B; Kral, AM; Secrist, JP; Miller, TA Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19412 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19412&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 23648260 46519434 CHEMBL235674 ZINC14970778 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50407651 COC(=O)NCc1ccc(cc1)C(=O)Nc1cc(ccc1N)-c1ccccc1 InChI=1S/C22H21N3O3/c1-28-22(27)24-14-15-7-9-17(10-8-15)21(26)25-20-13-18(11-12-19(20)23)16-5-3-2-4-6-16/h2-13H,14,23H2,1H3,(H,24,27)(H,25,26) QLRRIESOGZTMDR-UHFFFAOYSA-N 50229192 CHEMBL398420::US9096559, 14f::US9096559, 9::[4-(4-amino-biphenyl-3-ylcarbamoyl)-benzyl]-carbamic acid methyl ester Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2007.11.047 10.7270/Q28W3D1M 18060775 Witter, DJ; Harrington, P; Wilson, KJ; Chenard, M; Fleming, JC; Haines, B; Kral, AM; Secrist, JP; Miller, TA Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50229192 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50229192&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25032862 104098086 CHEMBL398420 ZINC29039034 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50407664 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2007.11.047 10.7270/Q28W3D1M 18060775 Witter, DJ; Harrington, P; Wilson, KJ; Chenard, M; Fleming, JC; Haines, B; Kral, AM; Secrist, JP; Miller, TA Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50407667 CCOC(=O)NCc1ccc(cc1)C(=O)Nc1cc(ccc1N)-c1cccs1 InChI=1S/C21H21N3O3S/c1-2-27-21(26)23-13-14-5-7-15(8-6-14)20(25)24-18-12-16(9-10-17(18)22)19-4-3-11-28-19/h3-12H,2,13,22H2,1H3,(H,23,26)(H,24,25) OQUHEOGMDDNVOX-UHFFFAOYSA-N 50229197 CHEMBL399494::US9096559, 16::ethyl 4-((2-amino-5-(thiophen-2-yl)phenyl)carbamoyl)benzylcarbamate Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2007.11.047 10.7270/Q28W3D1M 18060775 Witter, DJ; Harrington, P; Wilson, KJ; Chenard, M; Fleming, JC; Haines, B; Kral, AM; Secrist, JP; Miller, TA Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50229197 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50229197&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25155956 104098091 CHEMBL399494 ZINC29039041 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50400430 Nc1ccccc1NC(=O)c1ccc(CNC2=N[C@@H]([C@@H](O2)c2ccccc2)c2ccccc2)cc1 InChI=1S/C29H26N4O2/c30-24-13-7-8-14-25(24)32-28(34)23-17-15-20(16-18-23)19-31-29-33-26(21-9-3-1-4-10-21)27(35-29)22-11-5-2-6-12-22/h1-18,26-27H,19,30H2,(H,31,33)(H,32,34)/t26-,27+/m1/s1 FYAWEPJUGYZQDE-SXOMAYOGSA-N 50113971 CHEMBL3605506 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.5b00545 10.7270/Q26T0PFV 26287310 Marson, CM; Matthews, CJ; Atkinson, SJ; Lamadema, N; Thomas, NS University College London http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50113971 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50113971&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122186557 104008185 CHEMBL3605506 ZINC00003218 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50422481 C\C=C1/NC(=O)[C@@H](CS)NC(=O)[C@H](CC(=O)C[C@H](OC(=O)[C@@H](NC1=O)C(C)C)\C=C\CCS)C(C)C InChI=1S/C25H39N3O6S2/c1-6-19-23(31)28-21(15(4)5)25(33)34-17(9-7-8-10-35)11-16(29)12-18(14(2)3)22(30)27-20(13-36)24(32)26-19/h6-7,9,14-15,17-18,20-21,35-36H,8,10-13H2,1-5H3,(H,26,32)(H,27,30)(H,28,31)/b9-7+,19-6-/t17-,18-,20-,21+/m1/s1 UPCFDQLGZODPFB-BXJZLCHMSA-N 50354086 FK-228::Istodax::ROMIDEPSIN Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.5b01044 10.7270/Q2DF6T01 26331334 Yao, Y; Tu, Z; Liao, C; Wang, Z; Li, S; Yao, H; Li, Z; Jiang, S Guangzhou Institute of Biomedicine and Health http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50354086 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50354086&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 49863499 136360772 ZINC58575686 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50422482 C\C=C1/NC(=O)[C@H](CS)NC(=O)[C@H](NC(=O)C[C@H](OC(=O)[C@@H](NC1=O)C(C)C)\C=C\CCS)C(C)C InChI=1S/C24H38N4O6S2/c1-6-16-21(30)28-20(14(4)5)24(33)34-15(9-7-8-10-35)11-18(29)27-19(13(2)3)23(32)26-17(12-36)22(31)25-16/h6-7,9,13-15,17,19-20,35-36H,8,10-12H2,1-5H3,(H,25,31)(H,26,32)(H,27,29)(H,28,30)/b9-7+,16-6-/t15-,17+,19-,20+/m1/s1 MEJLVLMAJJRLCR-IWIVBDIWSA-N 50123617 CHEMBL3622726 Histone deacetylase 4 Homo sapiens 9570 ChEMBL 10.1021/acs.jmedchem.5b01044 10.7270/Q2DF6T01 26331334 Yao, Y; Tu, Z; Liao, C; Wang, Z; Li, S; Yao, H; Li, Z; Jiang, S Guangzhou Institute of Biomedicine and Health http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50123617 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50123617&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122192003 321902037 CHEMBL3622726 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50422483 C\C=C1/NC(=O)c2csc(n2)[C@H](NC(=O)C[C@H](OC(=O)[C@@H](NC1=O)C(C)C)\C=C\CCS)C(C)C InChI=1S/C24H34N4O5S2/c1-6-16-21(30)28-20(14(4)5)24(32)33-15(9-7-8-10-34)11-18(29)27-19(13(2)3)23-26-17(12-35-23)22(31)25-16/h6-7,9,12-15,19-20,34H,8,10-11H2,1-5H3,(H,25,31)(H,27,29)(H,28,30)/b9-7+,16-6-/t15-,19-,20+/m1/s1 IRBKIKHESMDKHL-HGLBEQJOSA-N 50123618 CHEMBL3622727 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.5b01044 10.7270/Q2DF6T01 26331334 Yao, Y; Tu, Z; Liao, C; Wang, Z; Li, S; Yao, H; Li, Z; Jiang, S Guangzhou Institute of Biomedicine and Health http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50123618 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50123618&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122192004 321902038 CHEMBL3622727 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50422484 CCCCCCCC(=O)SCC\C=C\[C@@H]1CC(=O)N[C@H](C(C)C)c2nc(cs2)C(=O)N\C(=C/C)C(=O)N[C@@H](C(C)C)C(=O)O1 InChI=1S/C32H48N4O6S2/c1-7-9-10-11-12-16-26(38)43-17-14-13-15-22-18-25(37)35-27(20(3)4)31-34-24(19-44-31)30(40)33-23(8-2)29(39)36-28(21(5)6)32(41)42-22/h8,13,15,19-22,27-28H,7,9-12,14,16-18H2,1-6H3,(H,33,40)(H,35,37)(H,36,39)/b15-13+,23-8-/t22-,27-,28+/m1/s1 QNCUBQATMINDNK-GOBIJVEYSA-N 50123619 CHEMBL3622728 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.5b01044 10.7270/Q2DF6T01 26331334 Yao, Y; Tu, Z; Liao, C; Wang, Z; Li, S; Yao, H; Li, Z; Jiang, S Guangzhou Institute of Biomedicine and Health http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50123619 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50123619&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122192005 321902039 CHEMBL3622728 C05752 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50422485 C\C=C1/NC(=O)c2csc(CNC(=O)C[C@H](OC(=O)[C@@H](NC1=O)C(C)C)\C=C\CCS)n2 InChI=1S/C21H28N4O5S2/c1-4-14-19(27)25-18(12(2)3)21(29)30-13(7-5-6-8-31)9-16(26)22-10-17-23-15(11-32-17)20(28)24-14/h4-5,7,11-13,18,31H,6,8-10H2,1-3H3,(H,22,26)(H,24,28)(H,25,27)/b7-5+,14-4-/t13-,18+/m1/s1 PWOYGNLEMBIIES-LCHKFDHZSA-N 50123620 CHEMBL3622729 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.5b01044 10.7270/Q2DF6T01 26331334 Yao, Y; Tu, Z; Liao, C; Wang, Z; Li, S; Yao, H; Li, Z; Jiang, S Guangzhou Institute of Biomedicine and Health http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50123620 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50123620&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60151224 321902040 CHEMBL3622729 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50422486 CCCCCCCC(=O)SCC\C=C\[C@@H]1CC(=O)NCc2nc(cs2)C(=O)N\C(=C/C)C(=O)N[C@@H](C(C)C)C(=O)O1 InChI=1S/C29H42N4O6S2/c1-5-7-8-9-10-14-25(35)40-15-12-11-13-20-16-23(34)30-17-24-31-22(18-41-24)28(37)32-21(6-2)27(36)33-26(19(3)4)29(38)39-20/h6,11,13,18-20,26H,5,7-10,12,14-17H2,1-4H3,(H,30,34)(H,32,37)(H,33,36)/b13-11+,21-6-/t20-,26+/m1/s1 WCZYLKXWWUKEBA-QUDUTUPQSA-N 50123628 CHEMBL3622730 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.5b01044 10.7270/Q2DF6T01 26331334 Yao, Y; Tu, Z; Liao, C; Wang, Z; Li, S; Yao, H; Li, Z; Jiang, S Guangzhou Institute of Biomedicine and Health http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50123628 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50123628&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60152596 104016055 CHEMBL3622730 C05752 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50422487 C\C=C1/NC(=O)c2csc(CNC(=O)C[C@H](OC(=O)[C@@H](NC1=O)C(C)C)\C=C\CCSC(C)=O)n2 InChI=1S/C23H30N4O6S2/c1-5-16-21(30)27-20(13(2)3)23(32)33-15(8-6-7-9-34-14(4)28)10-18(29)24-11-19-25-17(12-35-19)22(31)26-16/h5-6,8,12-13,15,20H,7,9-11H2,1-4H3,(H,24,29)(H,26,31)(H,27,30)/b8-6+,16-5-/t15-,20+/m1/s1 AJEJWONOGKARDP-HQRKCSHCSA-N 50123634 CHEMBL3622731 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.5b01044 10.7270/Q2DF6T01 26331334 Yao, Y; Tu, Z; Liao, C; Wang, Z; Li, S; Yao, H; Li, Z; Jiang, S Guangzhou Institute of Biomedicine and Health http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50123634 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50123634&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60151225 104016061 CHEMBL3622731 C04334 ZINC36184552 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50422488 CCCCCCCC(=O)SCC\C=C\[C@@H]1CC(=O)NCc2nc(cs2)C2=N[C@@](C)(CS2)C(=O)N[C@@H](C(C)C)C(=O)O1 InChI=1S/C29H42N4O5S3/c1-5-6-7-8-9-13-24(35)39-14-11-10-12-20-15-22(34)30-16-23-31-21(17-40-23)26-33-29(4,18-41-26)28(37)32-25(19(2)3)27(36)38-20/h10,12,17,19-20,25H,5-9,11,13-16,18H2,1-4H3,(H,30,34)(H,32,37)/b12-10+/t20-,25+,29+/m1/s1 AXESYCSCGBQJBL-SZPBEECKSA-N 50322422 CHEMBL1173445::Largazole Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.5b01044 10.7270/Q2DF6T01 26331334 Yao, Y; Tu, Z; Liao, C; Wang, Z; Li, S; Yao, H; Li, Z; Jiang, S Guangzhou Institute of Biomedicine and Health http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50322422 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50322422&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 24757913 104143951 CHEMBL1173445 C05752 ZINC56861395 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50422489 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.5b01044 10.7270/Q2DF6T01 26331334 Yao, Y; Tu, Z; Liao, C; Wang, Z; Li, S; Yao, H; Li, Z; Jiang, S Guangzhou Institute of Biomedicine and Health http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50425851 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 101 ChEMBL 10.1016/j.ejmech.2008.06.020 10.7270/Q2BG2NTX 18672316 Andrianov, V; Gailite, V; Lola, D; Loza, E; Semenikhina, V; Kalvinsh, I; Finn, P; Petersen, KD; Ritchie, JW; Khan, N; Tumber, A; Collins, LS; Vadlamudi, SM; Bjorkling, F; Sehested, M Institute of Organic Synthesis http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50425852 C\C(\C=C\c1ccccc1)=C/C(=O)NCCCCCC(=O)NO InChI=1S/C18H24N2O3/c1-15(11-12-16-8-4-2-5-9-16)14-18(22)19-13-7-3-6-10-17(21)20-23/h2,4-5,8-9,11-12,14,23H,3,6-7,10,13H2,1H3,(H,19,22)(H,20,21)/b12-11+,15-14+ FIMYEORZUZGRFU-TVYVBBRWSA-N 50268042 (2E,4E)-N-[6-(Hydroxyamino)-6-oxohexyl]-3-methyl-5-phenyl-2,4-pentadienamide::CHEMBL490018 Histone deacetylase 4 Homo sapiens 3.7 ChEMBL 10.1016/j.ejmech.2008.06.020 10.7270/Q2BG2NTX 18672316 Andrianov, V; Gailite, V; Lola, D; Loza, E; Semenikhina, V; Kalvinsh, I; Finn, P; Petersen, KD; Ritchie, JW; Khan, N; Tumber, A; Collins, LS; Vadlamudi, SM; Bjorkling, F; Sehested, M Institute of Organic Synthesis http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50268042 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50268042&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 42599455 104114656 CHEMBL490018 ZINC45498626 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50425853 ONC(=O)CCCCCNC(=O)\C=C\c1ccc2cccnc2c1 InChI=1S/C18H21N3O3/c22-17(20-11-3-1-2-6-18(23)21-24)10-8-14-7-9-15-5-4-12-19-16(15)13-14/h4-5,7-10,12-13,24H,1-3,6,11H2,(H,20,22)(H,21,23)/b10-8+ IXKLILPHPNZHNB-CSKARUKUSA-N 50268063 (E)-N-[6-(Hydroxyamino)-6-oxohexyl]-3-(7-quinolinyl)-2-propenamide::CHEMBL484073 Histone deacetylase 4 Homo sapiens 5.3 ChEMBL 10.1016/j.ejmech.2008.06.020 10.7270/Q2BG2NTX 18672316 Andrianov, V; Gailite, V; Lola, D; Loza, E; Semenikhina, V; Kalvinsh, I; Finn, P; Petersen, KD; Ritchie, JW; Khan, N; Tumber, A; Collins, LS; Vadlamudi, SM; Bjorkling, F; Sehested, M Institute of Organic Synthesis http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50268063 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50268063&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 42599456 104114665 CHEMBL484073 ZINC40420873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50425854 ONC(=O)CCCCCNC(=O)C=C1c2ccccc2-c2ccccc12 InChI=1S/C21H22N2O3/c24-20(23-26)12-2-1-7-13-22-21(25)14-19-17-10-5-3-8-15(17)16-9-4-6-11-18(16)19/h3-6,8-11,14,26H,1-2,7,12-13H2,(H,22,25)(H,23,24) UYZBNNODRNHVBB-UHFFFAOYSA-N 50268097 6-{[2-(9H-Fluoren-9-yliden)acetyl]amino}-N-hydroxyhexanamide::CHEMBL485514 Histone deacetylase 4 Homo sapiens 1.2 ChEMBL 10.1016/j.ejmech.2008.06.020 10.7270/Q2BG2NTX 18672316 Andrianov, V; Gailite, V; Lola, D; Loza, E; Semenikhina, V; Kalvinsh, I; Finn, P; Petersen, KD; Ritchie, JW; Khan, N; Tumber, A; Collins, LS; Vadlamudi, SM; Bjorkling, F; Sehested, M Institute of Organic Synthesis http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50268097 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50268097&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 9924543 104114678 CHEMBL485514 ZINC03817863 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50425855 ONC(=O)CCCCCNC(=O)\C=C\c1ccc(Cl)cc1F InChI=1S/C15H18ClFN2O3/c16-12-7-5-11(13(17)10-12)6-8-14(20)18-9-3-1-2-4-15(21)19-22/h5-8,10,22H,1-4,9H2,(H,18,20)(H,19,21)/b8-6+ MMHPCBFDYDBBIL-SOFGYWHQSA-N 50268121 (E)-3-(4-Chloro-2-fluorophenyl)-N-[6-(hydroxyamino)-6-oxohexyl]-2-propenamide::CHEMBL484489 Histone deacetylase 4 Homo sapiens 4.3 ChEMBL 10.1016/j.ejmech.2008.06.020 10.7270/Q2BG2NTX 18672316 Andrianov, V; Gailite, V; Lola, D; Loza, E; Semenikhina, V; Kalvinsh, I; Finn, P; Petersen, KD; Ritchie, JW; Khan, N; Tumber, A; Collins, LS; Vadlamudi, SM; Bjorkling, F; Sehested, M Institute of Organic Synthesis http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50268121 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50268121&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 9923508 104114690 CHEMBL484489 ZINC34028639 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50428007 Cc1ccc(cc1)C(=O)\C=C\c1ccc(\C=C\C(=O)NO)o1 InChI=1S/C17H15NO4/c1-12-2-4-13(5-3-12)16(19)10-8-14-6-7-15(22-14)9-11-17(20)18-21/h2-11,21H,1H3,(H,18,20)/b10-8+,11-9+ MVZUYPMOSUQGTG-GFULKKFKSA-N 50244813 (E)-N-Hydroxy-3-(5-((E)-3-oxo-3-p-tolylprop-1-enyl)furan-2-yl)acrylamide::CHEMBL445955 Histone deacetylase 4 Homo sapiens 1100 ChEMBL 10.1016/j.bmc.2008.07.066 10.7270/Q22V2FX3 18701301 Su, H; Nebbioso, A; Carafa, V; Chen, Y; Yang, B; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50244813 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50244813&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25141401 104100738 CHEMBL445955 ZINC40833608 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50428026 ONC(=O)c1ccccc1NC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C21H25N3O4/c25-19(22-16-10-4-3-5-11-16)14-6-1-2-7-15-20(26)23-18-13-9-8-12-17(18)21(27)24-28/h3-5,8-13,28H,1-2,6-7,14-15H2,(H,22,25)(H,23,26)(H,24,27) WRXIPQCKJYKVSR-UHFFFAOYSA-N 50240935 CHEMBL181459::N1-(2-(hydroxycarbamoyl)phenyl)-N8-phenyloctanediamide::Octanedioic acid (2-hydroxycarbamoyl-phenyl)-amide phenylamide Histone deacetylase 4 Homo sapiens 550 ChEMBL 10.1016/j.bmc.2008.07.066 10.7270/Q22V2FX3 18701301 Su, H; Nebbioso, A; Carafa, V; Chen, Y; Yang, B; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50240935 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50240935&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44228659 104098511 CHEMBL181459 ZINC28135855 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50428027 COc1cc(\C=C\c2ccc(o2)C(=O)NO)ccc1OCc1ccccc1 InChI=1S/C21H19NO5/c1-25-20-13-15(7-9-17-10-12-19(27-17)21(23)22-24)8-11-18(20)26-14-16-5-3-2-4-6-16/h2-13,24H,14H2,1H3,(H,22,23)/b9-7+ WAIPGINZUGAKDT-VQHVLOKHSA-N 50244922 (E)-5-(4-(Benzyloxy)-3-methoxystyryl)-N-hydroxyfuran-2-carboxamide::CHEMBL472347 Histone deacetylase 4 Homo sapiens 10250 ChEMBL 10.1016/j.bmc.2008.07.066 10.7270/Q22V2FX3 18701301 Su, H; Nebbioso, A; Carafa, V; Chen, Y; Yang, B; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50244922 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50244922&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562080 104100817 CHEMBL472347 ZINC40407005 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50428028 CN(C)c1ccc(\C=C\c2ccc(o2)C(=O)NO)cc1 InChI=1S/C15H16N2O3/c1-17(2)12-6-3-11(4-7-12)5-8-13-9-10-14(20-13)15(18)16-19/h3-10,19H,1-2H3,(H,16,18)/b8-5+ MNPXTXIBMBMRDV-VMPITWQZSA-N 50244921 (E)-5-(4-(Dimethylamino)styryl)-N-hydroxyfuran-2-carboxamide::CHEMBL472346 Histone deacetylase 4 Homo sapiens 50580 ChEMBL 10.1016/j.bmc.2008.07.066 10.7270/Q22V2FX3 18701301 Su, H; Nebbioso, A; Carafa, V; Chen, Y; Yang, B; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50244921 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50244921&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562079 104100816 CHEMBL472346 ZINC40914040 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50428029 COc1cccc(\C=C\c2ccc(o2)C(=O)NO)c1O InChI=1S/C14H13NO5/c1-19-11-4-2-3-9(13(11)16)5-6-10-7-8-12(20-10)14(17)15-18/h2-8,16,18H,1H3,(H,15,17)/b6-5+ GLLHYSARUQFBGV-AATRIKPKSA-N 50244920 (E)-N-Hydroxy-5-(2-hydroxy-3-methoxystyryl)furan-2-carboxamide::CHEMBL513589 Histone deacetylase 4 Homo sapiens 42810 ChEMBL 10.1016/j.bmc.2008.07.066 10.7270/Q22V2FX3 18701301 Su, H; Nebbioso, A; Carafa, V; Chen, Y; Yang, B; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50244920 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50244920&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562078 104100815 CHEMBL513589 ZINC40914038 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50428030 ONC(=O)c1ccc(\C=C\c2cccc(Cl)c2Cl)o1 InChI=1S/C13H9Cl2NO3/c14-10-3-1-2-8(12(10)15)4-5-9-6-7-11(19-9)13(17)16-18/h1-7,18H,(H,16,17)/b5-4+ ARBOFPOZABCYOJ-SNAWJCMRSA-N 50244919 (E)-5-(2,3-Dichlorostyryl)-N-hydroxyfuran-2-carboxamide::CHEMBL447964 Histone deacetylase 4 Homo sapiens 49280 ChEMBL 10.1016/j.bmc.2008.07.066 10.7270/Q22V2FX3 18701301 Su, H; Nebbioso, A; Carafa, V; Chen, Y; Yang, B; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50244919 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50244919&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562077 104100814 CHEMBL447964 ZINC40834667 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50428031 ONC(=O)c1ccc(\C=C\c2ccc3OCOc3c2)o1 InChI=1S/C14H11NO5/c16-14(15-17)12-6-4-10(20-12)3-1-9-2-5-11-13(7-9)19-8-18-11/h1-7,17H,8H2,(H,15,16)/b3-1+ KZRFIVSATZSKSX-HNQUOIGGSA-N 50244918 (E)-5-(2-(Benzo[d][1,3]dioxol-5-yl)vinyl)-N-hydroxyfuran-2-carboxamide::CHEMBL472345 Histone deacetylase 4 Homo sapiens 85600 ChEMBL 10.1016/j.bmc.2008.07.066 10.7270/Q22V2FX3 18701301 Su, H; Nebbioso, A; Carafa, V; Chen, Y; Yang, B; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50244918 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50244918&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562076 104100813 CHEMBL472345 ZINC40914036 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50428032 ONC(=O)c1ccc(\C=C\c2ccccc2O)o1 InChI=1S/C13H11NO4/c15-11-4-2-1-3-9(11)5-6-10-7-8-12(18-10)13(16)14-17/h1-8,15,17H,(H,14,16)/b6-5+ JYWPGDYURGSVMW-AATRIKPKSA-N 50244874 (E)-N-Hydroxy-5-(2-hydroxystyryl)furan-2-carboxamide::CHEMBL472532 Histone deacetylase 4 Homo sapiens 74240 ChEMBL 10.1016/j.bmc.2008.07.066 10.7270/Q22V2FX3 18701301 Su, H; Nebbioso, A; Carafa, V; Chen, Y; Yang, B; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50244874 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50244874&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562040 104100782 CHEMBL472532 ZINC40406383 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50428033 ONC(=O)c1ccc(\C=C\c2ccc(O)cc2)o1 InChI=1S/C13H11NO4/c15-10-4-1-9(2-5-10)3-6-11-7-8-12(18-11)13(16)14-17/h1-8,15,17H,(H,14,16)/b6-3+ ZXMWCNGIVVSWOO-ZZXKWVIFSA-N 50244873 (E)-N-Hydroxy-5-(4-hydroxystyryl)furan-2-carboxamide::CHEMBL512179 Histone deacetylase 4 Homo sapiens 57060 ChEMBL 10.1016/j.bmc.2008.07.066 10.7270/Q22V2FX3 18701301 Su, H; Nebbioso, A; Carafa, V; Chen, Y; Yang, B; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50244873 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50244873&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562039 104100781 CHEMBL512179 ZINC40914041 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50428034 ONC(=O)c1ccc(\C=C\c2ccccc2)o1 InChI=1S/C13H11NO3/c15-13(14-16)12-9-8-11(17-12)7-6-10-4-2-1-3-5-10/h1-9,16H,(H,14,15)/b7-6+ USPQQLCGNXDFDP-VOTSOKGWSA-N 50244872 (E)-N-Hydroxy-5-styrylfuran-2-carboxamide::CHEMBL505199 Histone deacetylase 4 Homo sapiens 47170 ChEMBL 10.1016/j.bmc.2008.07.066 10.7270/Q22V2FX3 18701301 Su, H; Nebbioso, A; Carafa, V; Chen, Y; Yang, B; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50244872 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50244872&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562038 104100780 CHEMBL505199 ZINC40980715 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50428035 ONC(=O)\C=C\c1ccc(\C=C\C(=O)c2ccccc2)o1 InChI=1S/C16H13NO4/c18-15(12-4-2-1-3-5-12)10-8-13-6-7-14(21-13)9-11-16(19)17-20/h1-11,20H,(H,17,19)/b10-8+,11-9+ DHXIUUKDDYVBSZ-GFULKKFKSA-N 50244871 (E)-N-Hydroxy-3-(5-((E)-3-oxo-3-phenylprop-1-enyl)-furan-2-yl)acrylamide::CHEMBL442661 Histone deacetylase 4 Homo sapiens 22780 ChEMBL 10.1016/j.bmc.2008.07.066 10.7270/Q22V2FX3 18701301 Su, H; Nebbioso, A; Carafa, V; Chen, Y; Yang, B; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50244871 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50244871&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562037 104100779 CHEMBL442661 ZINC40828445 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50428036 ONC(=O)\C=C\c1ccc(\C=C\C(=O)c2ccc(F)cc2)o1 InChI=1S/C16H12FNO4/c17-12-3-1-11(2-4-12)15(19)9-7-13-5-6-14(22-13)8-10-16(20)18-21/h1-10,21H,(H,18,20)/b9-7+,10-8+ HNJNJIAKOLHXPC-FIFLTTCUSA-N 50244870 (E)-3-(5-((E)-3-(4-Fluorophenyl)-3-oxoprop-1-enyl)furan-2-yl)-N-hydroxyacrylamide::CHEMBL472533 Histone deacetylase 4 Homo sapiens 7680 ChEMBL 10.1016/j.bmc.2008.07.066 10.7270/Q22V2FX3 18701301 Su, H; Nebbioso, A; Carafa, V; Chen, Y; Yang, B; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50244870 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50244870&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562036 104100778 CHEMBL472533 ZINC40897871 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50428037 ONC(=O)\C=C\c1ccc(\C=C\C(=O)c2ccc(Cl)cc2Cl)o1 InChI=1S/C16H11Cl2NO4/c17-10-1-6-13(14(18)9-10)15(20)7-4-11-2-3-12(23-11)5-8-16(21)19-22/h1-9,22H,(H,19,21)/b7-4+,8-5+ SFUBGQMBVDXPJZ-NSLJXJERSA-N 50244869 (E)-3-(5-((E)-3-(2,4-Dichlorophenyl)-3-oxoprop-1-enyl)-furan-2-yl)-N-hydroxyacrylamide::CHEMBL471495 Histone deacetylase 4 Homo sapiens 8190.0 ChEMBL 10.1016/j.bmc.2008.07.066 10.7270/Q22V2FX3 18701301 Su, H; Nebbioso, A; Carafa, V; Chen, Y; Yang, B; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50244869 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50244869&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562035 104100777 CHEMBL471495 ZINC40893033 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50428038 ONC(=O)\C=C\c1ccc(\C=C\C(=O)c2cc(Cl)ccc2Cl)o1 InChI=1S/C16H11Cl2NO4/c17-10-1-6-14(18)13(9-10)15(20)7-4-11-2-3-12(23-11)5-8-16(21)19-22/h1-9,22H,(H,19,21)/b7-4+,8-5+ KARALHKIYYSJRK-NSLJXJERSA-N 50244868 (E)-3-(5-((E)-3-(2,5-Dichlorophenyl)-3-oxoprop-1-enyl)-furan-2-yl)-N-hydroxyacrylamide::CHEMBL471494 Histone deacetylase 4 Homo sapiens 4310 ChEMBL 10.1016/j.bmc.2008.07.066 10.7270/Q22V2FX3 18701301 Su, H; Nebbioso, A; Carafa, V; Chen, Y; Yang, B; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50244868 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50244868&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562034 104100776 CHEMBL471494 ZINC40893030 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50428039 ONC(=O)\C=C\c1ccc(\C=C\C(=O)c2ccc3ccccc3c2)o1 InChI=1S/C20H15NO4/c22-19(16-6-5-14-3-1-2-4-15(14)13-16)11-9-17-7-8-18(25-17)10-12-20(23)21-24/h1-13,24H,(H,21,23)/b11-9+,12-10+ ZPCAMDITBGELPH-WGDLNXRISA-N 50244818 (E)-N-Hydroxy-3-(5-((E)-3-(naphthalen-2-yl)-3-oxoprop-1-enyl)furan-2-yl)acrylamide::CHEMBL461763 Histone deacetylase 4 Homo sapiens 4380 ChEMBL 10.1016/j.bmc.2008.07.066 10.7270/Q22V2FX3 18701301 Su, H; Nebbioso, A; Carafa, V; Chen, Y; Yang, B; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50244818 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50244818&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44561976 104100743 CHEMBL461763 ZINC40873210 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50428040 COc1ccc2cc(ccc2c1)C(=O)\C=C\c1ccc(\C=C\C(=O)NO)o1 InChI=1S/C21H17NO5/c1-26-19-5-4-14-12-16(3-2-15(14)13-19)20(23)10-8-17-6-7-18(27-17)9-11-21(24)22-25/h2-13,25H,1H3,(H,22,24)/b10-8+,11-9+ WPZRRDIPOGPABO-GFULKKFKSA-N 50244817 (E)-N-Hydroxy-3-(5-((E)-3-(6-methoxynaphthalen-2-yl)-3-oxoprop-1-enyl)furan-2-yl)acrylamide::CHEMBL518165 Histone deacetylase 4 Homo sapiens 4040 ChEMBL 10.1016/j.bmc.2008.07.066 10.7270/Q22V2FX3 18701301 Su, H; Nebbioso, A; Carafa, V; Chen, Y; Yang, B; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50244817 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50244817&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44561975 104100742 CHEMBL518165 ZINC40392352 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50428041 ONC(=O)\C=C\c1ccc(\C=C\C(=O)c2ccc(Cl)cc2)o1 InChI=1S/C16H12ClNO4/c17-12-3-1-11(2-4-12)15(19)9-7-13-5-6-14(22-13)8-10-16(20)18-21/h1-10,21H,(H,18,20)/b9-7+,10-8+ BNFLWSDPHSRREU-FIFLTTCUSA-N 50244816 (E)-3-(5-((E)-3-(4-Chlorophenyl)-3-oxoprop-1-enyl)furan-2-yl)-N-hydroxyacrylamide::CHEMBL459677 Histone deacetylase 4 Homo sapiens 6030 ChEMBL 10.1016/j.bmc.2008.07.066 10.7270/Q22V2FX3 18701301 Su, H; Nebbioso, A; Carafa, V; Chen, Y; Yang, B; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50244816 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50244816&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44561974 104100741 CHEMBL459677 ZINC40864789 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50428042 ONC(=O)\C=C\c1ccc(\C=C\C(=O)c2cccc(Cl)c2)o1 InChI=1S/C16H12ClNO4/c17-12-3-1-2-11(10-12)15(19)8-6-13-4-5-14(22-13)7-9-16(20)18-21/h1-10,21H,(H,18,20)/b8-6+,9-7+ CRBAZYVHOGXXRG-CDJQDVQCSA-N 50244815 (E)-3-(5-((E)-3-(3-Chlorophenyl)-3-oxoprop-1-enyl)furan-2-yl)-N-hydroxyacrylamide::CHEMBL504669 Histone deacetylase 4 Homo sapiens 12910 ChEMBL 10.1016/j.bmc.2008.07.066 10.7270/Q22V2FX3 18701301 Su, H; Nebbioso, A; Carafa, V; Chen, Y; Yang, B; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50244815 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50244815&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44561973 104100740 CHEMBL504669 ZINC40834300 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50428043 CC(C)c1ccc(cc1)C(=O)\C=C\c1ccc(\C=C\C(=O)NO)o1 InChI=1S/C19H19NO4/c1-13(2)14-3-5-15(6-4-14)18(21)11-9-16-7-8-17(24-16)10-12-19(22)20-23/h3-13,23H,1-2H3,(H,20,22)/b11-9+,12-10+ UXLRQPFMGDXYTD-WGDLNXRISA-N 50244814 (E)-N-Hydroxy-3-(5-((E)-3-(4-isopropylphenyl)-3-oxoprop-1-enyl)furan-2-yl)acrylamide::CHEMBL462131 Histone deacetylase 4 Homo sapiens 4890 ChEMBL 10.1016/j.bmc.2008.07.066 10.7270/Q22V2FX3 18701301 Su, H; Nebbioso, A; Carafa, V; Chen, Y; Yang, B; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50244814 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50244814&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44561972 104100739 CHEMBL462131 ZINC40873044 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436358 FC(F)(F)C(=O)c1ccc(s1)-c1nc(COc2ccc(cc2)-c2nnco2)no1 InChI=1S/C17H9F3N4O4S/c18-17(19,20)14(25)11-5-6-12(29-11)16-22-13(24-28-16)7-26-10-3-1-9(2-4-10)15-23-21-8-27-15/h1-6,8H,7H2 JVTOOESMFVITDU-UHFFFAOYSA-N 50245989 1-(5-(3-((4-(1,3,4-oxadiazol-2-yl)phenoxy)methyl)-1,2,4-oxadiazol-5-yl)thiophen-2-yl)-2,2,2-trifluoroethanone::CHEMBL518821 Histone deacetylase 4 Homo sapiens 7 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50245989 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50245989&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562802 104101532 CHEMBL518821 ZINC40395793 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436359 FC(F)(F)C(=O)c1ccc(s1)-c1nc(Cc2cccs2)no1 InChI=1S/C13H7F3N2O2S2/c14-13(15,16)11(19)8-3-4-9(22-8)12-17-10(18-20-12)6-7-2-1-5-21-7/h1-5H,6H2 AVTYXXHFKLUIQU-UHFFFAOYSA-N 50245986 2,2,2-trifluoro-1-(5-(3-(thiophen-2-ylmethyl)-1,2,4-oxadiazol-5-yl)thiophen-2-yl)ethanone::CHEMBL504161 Histone deacetylase 4 Homo sapiens 15 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50245986 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50245986&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562799 104101529 CHEMBL504161 ZINC40379001 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436360 FC(F)(F)C(=O)c1ccc(s1)-c1nc(CN2C(=O)COc3ccccc23)no1 InChI=1S/C17H10F3N3O4S/c18-17(19,20)15(25)11-5-6-12(28-11)16-21-13(22-27-16)7-23-9-3-1-2-4-10(9)26-8-14(23)24/h1-6H,7-8H2 ASCINMAZWGAFOZ-UHFFFAOYSA-N 50245988 4-((5-(5-(2,2,2-trifluoroacetyl)thiophen-2-yl)-1,2,4-oxadiazol-3-yl)methyl)-2H-benzo[b][1,4]oxazin-3(4H)-one::CHEMBL462203 Histone deacetylase 4 Homo sapiens 15 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50245988 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50245988&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562801 104101531 CHEMBL462203 ZINC40874115 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436361 CS(=O)(=O)Cc1noc(n1)-c1ccc(s1)C(=O)C(F)(F)F InChI=1S/C10H7F3N2O4S2/c1-21(17,18)4-7-14-9(19-15-7)6-3-2-5(20-6)8(16)10(11,12)13/h2-3H,4H2,1H3 AQCULNMHTOBDQM-UHFFFAOYSA-N 50246033 2,2,2-Trifluoro-1-(5-{3-[(methylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl}thiophen-2-yl)ethanone::2,2,2-trifluoro-1-(5-(3-(methylsulfonylmethyl)-1,2,4-oxadiazol-5-yl)thiophen-2-yl)ethanone::CHEMBL512516 Histone deacetylase 4 Homo sapiens 30 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50246033 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50246033&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 17747371 104101565 CHEMBL512516 ZINC40395523 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436362 CCCS(=O)(=O)Cc1noc(n1)-c1ccc(s1)C(=O)C(F)(F)F InChI=1S/C12H11F3N2O4S2/c1-2-5-23(19,20)6-9-16-11(21-17-9)8-4-3-7(22-8)10(18)12(13,14)15/h3-4H,2,5-6H2,1H3 ANGRBZMMPDQGNC-UHFFFAOYSA-N 50246034 2,2,2-Trifluoro-1-(5-{3-[(propylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl}thiophen-2-yl)ethanone::2,2,2-trifluoro-1-(5-(3-(propylsulfonylmethyl)-1,2,4-oxadiazol-5-yl)thiophen-2-yl)ethanone::CHEMBL471173 Histone deacetylase 4 Homo sapiens 30 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50246034 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50246034&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25168856 104101566 CHEMBL471173 ZINC40893744 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436363 FC(F)(F)C(=O)c1ccc(s1)-c1nc(CS(=O)(=O)c2cccs2)no1 InChI=1S/C13H7F3N2O4S3/c14-13(15,16)11(19)7-3-4-8(24-7)12-17-9(18-22-12)6-25(20,21)10-2-1-5-23-10/h1-5H,6H2 GJBRKLVHIOIDHV-UHFFFAOYSA-N 50246035 2,2,2-Trifluoro-1-(5-{3-[(thiophen-2-ylsulfonyl)methyl]-1,2,4-oxadiazol-5-yl}thiophen-2-yl)ethanone::2,2,2-trifluoro-1-(5-(3-((thiophen-2-ylsulfonyl)methyl)-1,2,4-oxadiazol-5-yl)thiophen-2-yl)ethanone::CHEMBL471174 Histone deacetylase 4 Homo sapiens 35 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50246035 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50246035&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44541235 104101567 CHEMBL471174 ZINC40893747 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436364 FC(F)(F)C(=O)c1ccc(s1)-c1nc(CC(=O)N2CCCC2)no1 InChI=1S/C14H12F3N3O3S/c15-14(16,17)12(22)8-3-4-9(24-8)13-18-10(19-23-13)7-11(21)20-5-1-2-6-20/h3-4H,1-2,5-7H2 TYVAUJDHKZVDDN-UHFFFAOYSA-N 50245987 2,2,2-trifluoro-1-(5-(3-(2-oxo-2-(pyrrolidin-1-yl)ethyl)-1,2,4-oxadiazol-5-yl)thiophen-2-yl)ethanone::CHEMBL462202 Histone deacetylase 4 Homo sapiens 60 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50245987 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50245987&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562800 104101530 CHEMBL462202 ZINC40393570 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436365 Fc1ccc(CS(=O)(=O)Cc2noc(n2)-c2ccc(s2)C(=O)C(F)(F)F)cc1 InChI=1S/C16H10F4N2O4S2/c17-10-3-1-9(2-4-10)7-28(24,25)8-13-21-15(26-22-13)12-6-5-11(27-12)14(23)16(18,19)20/h1-6H,7-8H2 YQEDPXDHNQVERX-UHFFFAOYSA-N 50246036 2,2,2-Trifluoro-1-[5-(3-{[(4-fluorobenzyl)sulfonyl]methyl}-1,2,4-oxadiazol-5-yl)thiophen-2-yl]ethanone::2,2,2-trifluoro-1-(5-(3-((4-fluorobenzylsulfonyl)methyl)-1,2,4-oxadiazol-5-yl)thiophen-2-yl)ethanone::CHEMBL512517 Histone deacetylase 4 Homo sapiens 60 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50246036 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50246036&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562840 104101568 CHEMBL512517 ZINC40395524 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436366 FC(F)(F)C(=O)c1ccc(s1)-c1nc(no1)-c1cccnc1 InChI=1S/C13H6F3N3O2S/c14-13(15,16)10(20)8-3-4-9(22-8)12-18-11(19-21-12)7-2-1-5-17-6-7/h1-6H OQXFPVADHVSUEH-UHFFFAOYSA-N 50245943 2,2,2-trifluoro-1-(5-(3-(pyridin-3-yl)-1,2,4-oxadiazol-5-yl)thiophen-2-yl)ethanone::CHEMBL462370 Histone deacetylase 4 Homo sapiens 70 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50245943 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50245943&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562767 104101493 CHEMBL462370 ZINC40873902 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436367 Cc1noc(n1)-c1ccc(s1)C(=O)C(F)(F)F InChI=1S/C9H5F3N2O2S/c1-4-13-8(16-14-4)6-3-2-5(17-6)7(15)9(10,11)12/h2-3H,1H3 PHNUPEDOQIENBU-UHFFFAOYSA-N 50246037 2,2,2-trifluoro-1-(5-(3-methyl-1,2,4-oxadiazol-5-yl)thiophen-2-yl)ethanone::CHEMBL471344 Histone deacetylase 4 Homo sapiens 75 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50246037 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50246037&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25168576 104101569 CHEMBL471344 ZINC40401237 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436368 C[C@@H](NC(=O)c1ccc(s1)C(=O)C(F)(F)F)c1ccccc1 InChI=1S/C15H12F3NO2S/c1-9(10-5-3-2-4-6-10)19-14(21)12-8-7-11(22-12)13(20)15(16,17)18/h2-9H,1H3,(H,19,21)/t9-/m1/s1 DPKHRWMGXRDLLO-SECBINFHSA-N 25158 CHEMBL507716::N-[(1R)-1-phenylethyl]-5-(2,2,2-trifluoroacetyl)thiophene-2-carboxamide::thiophene derivative, 3d Histone deacetylase 4 Homo sapiens 76 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25158 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25158&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 15984018 56374299 CHEMBL507716 ZINC29069811 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436369 FC(F)(F)C(=O)c1ccc(s1)-c1nc(no1)-c1ccccn1 InChI=1S/C13H6F3N3O2S/c14-13(15,16)10(20)8-4-5-9(22-8)12-18-11(19-21-12)7-3-1-2-6-17-7/h1-6H UWMKQNCALZOYBT-UHFFFAOYSA-N 50245942 2,2,2-trifluoro-1-(5-(3-(pyridin-2-yl)-1,2,4-oxadiazol-5-yl)thiophen-2-yl)ethanone::CHEMBL512043 Histone deacetylase 4 Homo sapiens 90 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50245942 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50245942&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562766 104101492 CHEMBL512043 ZINC40391598 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436370 FC(F)(F)C(=O)c1ccc(s1)-c1nc(no1)-c1cccs1 InChI=1S/C12H5F3N2O2S2/c13-12(14,15)9(18)6-3-4-8(21-6)11-16-10(17-19-11)7-2-1-5-20-7/h1-5H HYKSAOKILFBKEU-UHFFFAOYSA-N 50245778 2,2,2-trifluoro-1-(5-(3-(thiophen-2-yl)-1,2,4-oxadiazol-5-yl)thiophen-2-yl)ethanone::CHEMBL454671 Histone deacetylase 4 Homo sapiens 95 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50245778 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50245778&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562606 104101354 CHEMBL454671 ZINC40848216 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436371 FC(F)(F)C(=O)c1ccc(s1)-c1nc(no1)-c1ccccc1 InChI=1S/C14H7F3N2O2S/c15-14(16,17)11(20)9-6-7-10(22-9)13-18-12(19-21-13)8-4-2-1-3-5-8/h1-7H LWIULHWFDLYIGE-UHFFFAOYSA-N 50246519 2,2,2-trifluoro-1-(5-(3-phenyl-1,2,4-oxadiazol-5-yl)thiophen-2-yl)ethanone::CHEMBL462210 Histone deacetylase 4 Homo sapiens 110 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50246519 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50246519&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44563236 104101926 CHEMBL462210 ZINC40866074 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436372 Cc1ccc(cc1)-c1noc(n1)-c1ccc(s1)C(=O)C(F)(F)F InChI=1S/C15H9F3N2O2S/c1-8-2-4-9(5-3-8)13-19-14(22-20-13)11-7-6-10(23-11)12(21)15(16,17)18/h2-7H,1H3 BZRIFGXMSJPZSX-UHFFFAOYSA-N 50245776 2,2,2-trifluoro-1-(5-(3-p-tolyl-1,2,4-oxadiazol-5-yl)thiophen-2-yl)ethanone::CHEMBL453953 Histone deacetylase 4 Homo sapiens 110 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50245776 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50245776&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562604 104101352 CHEMBL453953 ZINC40380148 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436373 Fc1ccc(-c2noc(n2)-c2ccc(s2)C(=O)C(F)(F)F)c(F)c1 InChI=1S/C14H5F5N2O2S/c15-6-1-2-7(8(16)5-6)12-20-13(23-21-12)10-4-3-9(24-10)11(22)14(17,18)19/h1-5H ZODJGPAXHPYDLJ-UHFFFAOYSA-N 50245939 1-(5-(3-(2,4-difluorophenyl)-1,2,4-oxadiazol-5-yl)thiophen-2-yl)-2,2,2-trifluoroethanone::CHEMBL460088 Histone deacetylase 4 Homo sapiens 120 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50245939 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50245939&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562763 104101489 CHEMBL460088 ZINC40861187 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436375 C[C@H](NC(=O)c1ccc(s1)C(=O)C(F)(F)F)c1ccccc1 InChI=1S/C15H12F3NO2S/c1-9(10-5-3-2-4-6-10)19-14(21)12-8-7-11(22-12)13(20)15(16,17)18/h2-9H,1H3,(H,19,21)/t9-/m0/s1 DPKHRWMGXRDLLO-VIFPVBQESA-N 25159 CHEMBL462208::N-[(1S)-1-phenylethyl]-5-(2,2,2-trifluoroacetyl)thiophene-2-carboxamide::thiophene derivative, 3e Histone deacetylase 4 Homo sapiens 170 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25159 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25159&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023798 56374300 CHEMBL462208 ZINC29069818 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436377 FC(F)(F)C(=O)c1ccc(s1)-c1nc(no1)-c1ccc(cc1)C(F)(F)F InChI=1S/C15H6F6N2O2S/c16-14(17,18)8-3-1-7(2-4-8)12-22-13(25-23-12)10-6-5-9(26-10)11(24)15(19,20)21/h1-6H BEILZWUUQVPWGE-UHFFFAOYSA-N 50245839 2,2,2-trifluoro-1-(5-(3-(4-(trifluoromethyl)phenyl)-1,2,4-oxadiazol-5-yl)thiophen-2-yl)ethanone::CHEMBL517869 Histone deacetylase 4 Homo sapiens 200 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50245839 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50245839&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562657 104101403 CHEMBL517869 ZINC40391863 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436379 Fc1ccc(cc1)-c1noc(n1)-c1ccc(s1)C(=O)C(F)(F)F InChI=1S/C14H6F4N2O2S/c15-8-3-1-7(2-4-8)12-19-13(22-20-12)10-6-5-9(23-10)11(21)14(16,17)18/h1-6H YOHGFGBUOGYNHX-UHFFFAOYSA-N 50245938 2,2,2-trifluoro-1-(5-(3-(4-fluorophenyl)-1,2,4-oxadiazol-5-yl)thiophen-2-yl)ethanone::CHEMBL450362 Histone deacetylase 4 Homo sapiens 220 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50245938 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50245938&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562762 104101488 CHEMBL450362 ZINC40379248 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436382 FC(F)(F)C(=O)c1ccc(s1)-c1nc(no1)-c1ccc(Cl)cc1Cl InChI=1S/C14H5Cl2F3N2O2S/c15-6-1-2-7(8(16)5-6)12-20-13(23-21-12)10-4-3-9(24-10)11(22)14(17,18)19/h1-5H RUWUMOMQAUPQAM-UHFFFAOYSA-N 50245940 1-(5-(3-(2,4-dichlorophenyl)-1,2,4-oxadiazol-5-yl)thiophen-2-yl)-2,2,2-trifluoroethanone::CHEMBL461141 Histone deacetylase 4 Homo sapiens 240 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50245940 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50245940&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562764 104101490 CHEMBL461141 ZINC40865445 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436384 FC(F)(F)C(=O)c1ccc(s1)C(=O)NCc1ccccc1 InChI=1S/C14H10F3NO2S/c15-14(16,17)12(19)10-6-7-11(21-10)13(20)18-8-9-4-2-1-3-5-9/h1-7H,8H2,(H,18,20) MAHDYMLFMJRXOZ-UHFFFAOYSA-N 50246470 CHEMBL455455::N-benzyl-5-(2,2,2-trifluoroacetyl)thiophene-2-carboxamide Histone deacetylase 4 Homo sapiens 243 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50246470 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50246470&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44563197 104101895 CHEMBL455455 ZINC40846757 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436385 Cc1ccc(cc1)-c1nnc(o1)-c1ccc(s1)C(=O)C(F)(F)F InChI=1S/C15H9F3N2O2S/c1-8-2-4-9(5-3-8)13-19-20-14(22-13)11-7-6-10(23-11)12(21)15(16,17)18/h2-7H,1H3 HZCZPYKKBAOQBJ-UHFFFAOYSA-N 50245777 2,2,2-trifluoro-1-(5-(5-p-tolyl-1,3,4-oxadiazol-2-yl)thiophen-2-yl)ethanone::CHEMBL509207 Histone deacetylase 4 Homo sapiens 270 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50245777 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50245777&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562605 104101353 CHEMBL509207 ZINC40848215 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436387 Cc1cccc(c1)-c1noc(n1)-c1ccc(s1)C(=O)C(F)(F)F InChI=1S/C15H9F3N2O2S/c1-8-3-2-4-9(7-8)13-19-14(22-20-13)11-6-5-10(23-11)12(21)15(16,17)18/h2-7H,1H3 XGEHSSFSEZXGQR-UHFFFAOYSA-N 50245780 2,2,2-trifluoro-1-(5-(3-m-tolyl-1,2,4-oxadiazol-5-yl)thiophen-2-yl)ethanone::CHEMBL509445 Histone deacetylase 4 Homo sapiens 280 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50245780 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50245780&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562608 104101356 CHEMBL509445 ZINC40380783 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436389 FC(F)(F)C(=O)c1ccc(s1)-c1nc(no1)-c1cccc(c1)C(F)(F)F InChI=1S/C15H6F6N2O2S/c16-14(17,18)8-3-1-2-7(6-8)12-22-13(25-23-12)10-5-4-9(26-10)11(24)15(19,20)21/h1-6H BNCPNGFUQKXKQH-UHFFFAOYSA-N 50245781 2,2,2-trifluoro-1-(5-(3-(3-(trifluoromethyl)phenyl)-1,2,4-oxadiazol-5-yl)thiophen-2-yl)ethanone::CHEMBL455395 Histone deacetylase 4 Homo sapiens 320 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50245781 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50245781&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562609 104101357 CHEMBL455395 ZINC40846751 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436396 FC(F)(F)C(=O)c1ccc(s1)-c1nnc(o1)-c1ccccc1 InChI=1S/C14H7F3N2O2S/c15-14(16,17)11(20)9-6-7-10(22-9)13-19-18-12(21-13)8-4-2-1-3-5-8/h1-7H LXLLDZJAYOJSSU-UHFFFAOYSA-N 50246520 2,2,2-trifluoro-1-(5-(5-phenyl-1,3,4-oxadiazol-2-yl)thiophen-2-yl)ethanone::CHEMBL462223 Histone deacetylase 4 Homo sapiens 420 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50246520 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50246520&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44563237 104101927 CHEMBL462223 ZINC40392856 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436397 FC(F)(F)C(=O)c1ccc(s1)-c1nnc(o1)-c1cccs1 InChI=1S/C12H5F3N2O2S2/c13-12(14,15)9(18)6-3-4-8(21-6)11-17-16-10(19-11)7-2-1-5-20-7/h1-5H SDZYIFVVCCKFKG-UHFFFAOYSA-N 50245779 2,2,2-trifluoro-1-(5-(5-(thiophen-2-yl)-1,3,4-oxadiazol-2-yl)thiophen-2-yl)ethanone::CHEMBL454672 Histone deacetylase 4 Homo sapiens 450 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50245779 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50245779&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562607 104101355 CHEMBL454672 ZINC40379955 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436402 CN(Cc1ccccc1)C(=O)c1ccc(s1)C(=O)C(F)(F)F InChI=1S/C15H12F3NO2S/c1-19(9-10-5-3-2-4-6-10)14(21)12-8-7-11(22-12)13(20)15(16,17)18/h2-8H,9H2,1H3 CEBFXUYKCDHZEP-UHFFFAOYSA-N 25157 CHEMBL462209::N-benzyl-N-methyl-5-(2,2,2-trifluoroacetyl)thiophene-2-carboxamide::thiophene derivative, 3c Histone deacetylase 4 Homo sapiens 510 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25157 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25157&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023797 56374298 CHEMBL462209 ZINC29069825 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436408 FC(F)(F)C(=O)c1ccc(s1)-c1nc(no1)-c1ccncc1 InChI=1S/C13H6F3N3O2S/c14-13(15,16)10(20)8-1-2-9(22-8)12-18-11(19-21-12)7-3-5-17-6-4-7/h1-6H LMQNGVNXXKVSAT-UHFFFAOYSA-N 50245985 2,2,2-trifluoro-1-(5-(3-(pyridin-4-yl)-1,2,4-oxadiazol-5-yl)thiophen-2-yl)ethanone::CHEMBL461333 Histone deacetylase 4 Homo sapiens 590 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50245985 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50245985&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562798 104101528 CHEMBL461333 ZINC40861292 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436423 FC(F)(F)C(=O)c1ccc(s1)-c1ncc(s1)-c1ccccc1 InChI=1S/C15H8F3NOS2/c16-15(17,18)13(20)10-6-7-11(21-10)14-19-8-12(22-14)9-4-2-1-3-5-9/h1-8H YBIMQPGGWANZSL-UHFFFAOYSA-N 50246521 2,2,2-trifluoro-1-(5-(5-phenylthiazol-2-yl)thiophen-2-yl)ethanone::CHEMBL505259 Histone deacetylase 4 Homo sapiens 1500 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50246521 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50246521&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 17747368 104101928 CHEMBL505259 ZINC40835484 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436424 CCNC(=O)c1ccc(s1)C(=O)C(F)(F)F InChI=1S/C9H8F3NO2S/c1-2-13-8(15)6-4-3-5(16-6)7(14)9(10,11)12/h3-4H,2H2,1H3,(H,13,15) XYMSMXPTPHUKFO-UHFFFAOYSA-N 25155 CHEMBL462146::N-ethyl-5-(2,2,2-trifluoroacetyl)thiophene-2-carboxamide::thiophene derivative, 3a Histone deacetylase 4 Homo sapiens 1700 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25155 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25155&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023795 56374296 CHEMBL462146 ZINC29069849 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50437401 Oc1ccc(cc1NC(=O)c1ccccc1)-c1ccccc1 InChI=1S/C19H15NO2/c21-18-12-11-16(14-7-3-1-4-8-14)13-17(18)20-19(22)15-9-5-2-6-10-15/h1-13,21H,(H,20,22) INXWGOLWSBWSOQ-UHFFFAOYSA-N 50232005 CHEMBL269935::N-(4-hydroxy-biphenyl-3-yl)-benzamide::N-(4-hydroxybiphenyl-3-yl)benzamide Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2008.10.052 10.7270/Q23R0SQ2 18951790 Methot, JL; Hamblett, CL; Mampreian, DM; Jung, J; Harsch, A; Szewczak, AA; Dahlberg, WK; Middleton, RE; Hughes, B; Fleming, JC; Wang, H; Kral, AM; Ozerova, N; Cruz, JC; Haines, B; Chenard, M; Kenific, CM; Secrist, JP; Miller, TA Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50232005 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50232005&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44454650 104055386 CHEMBL269935 ZINC29127807 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50436471 CC(C)(C)c1ccc(cc1)-c1noc(n1)-c1ccc(s1)C(=O)C(F)(F)F InChI=1S/C18H15F3N2O2S/c1-17(2,3)11-6-4-10(5-7-11)15-22-16(25-23-15)13-9-8-12(26-13)14(24)18(19,20)21/h4-9H,1-3H3 OYODCWRDYHHIFP-UHFFFAOYSA-N 50245941 1-(5-(3-(4-tert-butylphenyl)-1,2,4-oxadiazol-5-yl)thiophen-2-yl)-2,2,2-trifluoroethanone::CHEMBL461142 Histone deacetylase 4 Homo sapiens >2000 ChEMBL 10.1016/j.bmcl.2008.09.076 10.7270/Q2TD9X6G 18930398 Muraglia, E; Altamura, S; Branca, D; Cecchetti, O; Ferrigno, F; Orsale, MV; Palumbi, MC; Rowley, M; Scarpelli, R; Steinkuhler, C; Jones, P IRBM-Merck Research Laboratories Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50245941 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50245941&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44562765 104101491 CHEMBL461142 ZINC40865447 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50448576 ONC(=O)\C=C\c1ccc2n(CCN3CCCC3)c(CCc3ccccc3)nc2c1 InChI=1S/C24H28N4O2/c29-24(26-30)13-10-20-8-11-22-21(18-20)25-23(12-9-19-6-2-1-3-7-19)28(22)17-16-27-14-4-5-15-27/h1-3,6-8,10-11,13,18,30H,4-5,9,12,14-17H2,(H,26,29)/b13-10+ RCDIZKAYZBEALO-JLHYYAGUSA-N 50248476 CHEMBL491316::N-hydroxy-3-(2-phenethyl-1-(2-(pyrrolidin-1-yl)ethyl)-1H-benzo[d]imidazol-5-yl)acrylamide::N-hydroxy-3-[2-phenethyl-1-(2-pyrrolidin-1-ylethyl)-1H-benzimidazol-5-yl]acrylamide::SB-639::US10201527, Compound 72::US10736881, Compound 72::US8551988, 72 Histone deacetylase 4 Homo sapiens 9.6 ChEMBL 10.1016/j.bmcl.2009.01.041 10.7270/Q2FT8KX3 19181524 Wang, H; Yu, N; Song, H; Chen, D; Zou, Y; Deng, W; Lye, PL; Chang, J; Ng, M; Sun, ET; Sangthongpitag, K; Wang, X; Wu, X; Khng, HH; Fang, L; Goh, SK; Ong, WC; Bonday, Z; Stunkel, W; Poulsen, A; Entzeroth, M S*BIO Pte Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50248476 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50248476&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6918877 104103127 CHEMBL491316 ZINC38192628 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50452253 CCOP(=O)(CNCc1ccc(cc1)C(=O)Nc1cc(ccc1N)-c1cccs1)OCC InChI=1S/C23H28N3O4PS/c1-3-29-31(28,30-4-2)16-25-15-17-7-9-18(10-8-17)23(27)26-21-14-19(11-12-20(21)24)22-6-5-13-32-22/h5-14,25H,3-4,15-16,24H2,1-2H3,(H,26,27) SDFJPCASBWGULI-UHFFFAOYSA-N 50278515 CHEMBL470225::diethyl(4-(2-amino-5-(thiophen-2-yl)phenylcarbamoyl)benzylamino)methylphosphonate Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2009.02.009 10.7270/Q2QV3MDQ 19268585 Heidebrecht, RW; Chenard, M; Close, J; Dahlberg, WK; Fleming, J; Grimm, JB; Hamill, JE; Harsch, A; Haines, BB; Hughes, B; Kral, AM; Middleton, RE; Mushti, C; Ozerova, N; Szewczak, AA; Wang, H; Wilson, K; Witter, DJ; Secrist, JP; Miller, TA Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50278515 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50278515&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 42601485 104120808 CHEMBL470225 ZINC40892902 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50457755 ONC(=O)\C=C\c1ccc(cc1)C(F)(F)F InChI=1S/C10H8F3NO2/c11-10(12,13)8-4-1-7(2-5-8)3-6-9(15)14-16/h1-6,16H,(H,14,15)/b6-3+ ABKAFUZUCJSIKV-ZZXKWVIFSA-N 50140176 CHEMBL3394285 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmc.2015.12.035 10.7270/Q2Q52RG0 26753813 Ai, T; Qiu, L; Xie, J; Geraghty, RJ; Chen, L University of Minnesota http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50140176 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50140176&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 53374826 336952480 CHEMBL3394285 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50459100 COc1ccc2[nH]c(C)c(CC(=O)N[C@@H](CCCCCC(N)=O)c3nc(c[nH]3)-c3ccc4ccccc4c3)c2c1 InChI=1S/C32H35N5O3/c1-20-25(26-17-24(40-2)14-15-27(26)35-20)18-31(39)36-28(10-4-3-5-11-30(33)38)32-34-19-29(37-32)23-13-12-21-8-6-7-9-22(21)16-23/h6-9,12-17,19,28,35H,3-5,10-11,18H2,1-2H3,(H2,33,38)(H,34,37)(H,36,39)/t28-/m0/s1 QZLKZEZKQRUHEU-NDEPHWFRSA-N 50258626 (S)-7-(2-(5-methoxy-2-methyl-1H-indol-3-yl)acetamido)-7-(5-(naphthalen-2-yl)-1H-imidazol-2-yl)heptanamide::CHEMBL466215 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.bmcl.2009.04.011 10.7270/Q2P84BSJ 19410459 Attenni, B; Ontoria, JM; Cruz, JC; Rowley, M; Schultz-Fademrecht, C; Steinkuhler, C; Jones, P IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50258626 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50258626&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11657529 104109252 CHEMBL466215 ZINC43152309 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50459101 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.bmcl.2009.04.011 10.7270/Q2P84BSJ 19410459 Attenni, B; Ontoria, JM; Cruz, JC; Rowley, M; Schultz-Fademrecht, C; Steinkuhler, C; Jones, P IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50462342 ONC(=O)\C=C\c1ccc(\C=C(\CNC2CC2)c2ccc(F)cc2)cc1 InChI=1S/C21H21FN2O2/c22-19-8-6-17(7-9-19)18(14-23-20-10-11-20)13-16-3-1-15(2-4-16)5-12-21(25)24-26/h1-9,12-13,20,23,26H,10-11,14H2,(H,24,25)/b12-5+,18-13- NODIYCZWVUUEMT-HTZRGULJSA-N 50143215 CHEMBL3758457 Histone deacetylase 4 Homo sapiens 319 ChEMBL 10.1016/j.ejmech.2015.11.014 10.7270/Q2J9687D 26689485 Kachhadia, V; Rajagopal, S; Ponpandian, T; Vignesh, R; Anandhan, K; Prabhu, D; Rajendran, P; Nidhyanandan, S; Roy, AM; Ahamed, FA; Surendran, N; Rajagopal, S; Narayanan, S; Gopalan, B Orchid Chemicals & Pharmaceuticals Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50143215 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50143215&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 21020209 85381075 CHEMBL3758457 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50463566 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 2139 ChEMBL 10.1016/j.ejmech.2016.01.013 10.7270/Q20C4XM5 26814680 Wen, J; Bao, Y; Niu, Q; Yang, J; Fan, Y; Li, J; Jing, Y; Zhao, L; Liu, D Shenyang Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50463567 SCCCCCCNC(=O)c1cc(n[nH]1)-c1ccncc1 InChI=1S/C15H20N4OS/c20-15(17-7-3-1-2-4-10-21)14-11-13(18-19-14)12-5-8-16-9-6-12/h5-6,8-9,11,21H,1-4,7,10H2,(H,17,20)(H,18,19) KYZMEJZVXICXQX-UHFFFAOYSA-N 50143997 CHEMBL3759562 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2016.01.013 10.7270/Q20C4XM5 26814680 Wen, J; Bao, Y; Niu, Q; Yang, J; Fan, Y; Li, J; Jing, Y; Zhao, L; Liu, D Shenyang Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50143997 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50143997&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44304778 85397438 CHEMBL3759562 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50463568 SCCCCCCNC(=O)c1cc(n[nH]1)-c1cccnc1 InChI=1S/C15H20N4OS/c20-15(17-8-3-1-2-4-9-21)14-10-13(18-19-14)12-6-5-7-16-11-12/h5-7,10-11,21H,1-4,8-9H2,(H,17,20)(H,18,19) UMHAIDYPJKYSES-UHFFFAOYSA-N 50143996 CHEMBL3758882 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2016.01.013 10.7270/Q20C4XM5 26814680 Wen, J; Bao, Y; Niu, Q; Yang, J; Fan, Y; Li, J; Jing, Y; Zhao, L; Liu, D Shenyang Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50143996 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50143996&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44304486 85396842 CHEMBL3758882 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50463569 SCCCCCCNC(=O)c1cc(n[nH]1)-c1cnccn1 InChI=1S/C14H19N5OS/c20-14(17-5-3-1-2-4-8-21)12-9-11(18-19-12)13-10-15-6-7-16-13/h6-7,9-10,21H,1-5,8H2,(H,17,20)(H,18,19) GYWQCXUVPDWXRB-UHFFFAOYSA-N 50144216 CHEMBL3760013 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2016.01.013 10.7270/Q20C4XM5 26814680 Wen, J; Bao, Y; Niu, Q; Yang, J; Fan, Y; Li, J; Jing, Y; Zhao, L; Liu, D Shenyang Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50144216 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50144216&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 127028943 340095396 CHEMBL3760013 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50453804 COC(=O)c1ccc(CO\N=C\c2ccc(\C=C\C(=O)NO)cc2)cc1 InChI=1S/C19H18N2O5/c1-25-19(23)17-9-6-16(7-10-17)13-26-20-12-15-4-2-14(3-5-15)8-11-18(22)21-24/h2-12,24H,13H2,1H3,(H,21,22)/b11-8+,20-12+ IHHUORPGTIDVFD-JOESBUEISA-N 50278221 CHEMBL471043::methyl 4-((4-(3-(hydroxyamino)-3-oxoprop-1-enyl)benzylideneaminooxy)methyl)benzoate Histone deacetylase 4 Homo sapiens 12900 ChEMBL 10.1016/j.bmcl.2009.02.029 10.7270/Q2154GX2 19285395 Giannini, G; Marzi, M; Pezzi, R; Brunetti, T; Battistuzzi, G; Marzo, MD; Cabri, W; Vesci, L; Pisano, C R&D Sigma-Tau SpA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50278221 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50278221&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44138033 104120599 CHEMBL471043 ZINC40896774 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50453815 ONC(=O)\C=C\c1ccc(\C=N\OCCN2CCOCC2)cc1 InChI=1S/C16H21N3O4/c20-16(18-21)6-5-14-1-3-15(4-2-14)13-17-23-12-9-19-7-10-22-11-8-19/h1-6,13,21H,7-12H2,(H,18,20)/b6-5+,17-13+ KKMCPDKFGBXVNL-WDGODYKHSA-N 50278222 CHEMBL472631::N-hydroxy-3-(4-((2-morpholinoethoxyimino)methyl)phenyl)acrylamide::ST-3050 Histone deacetylase 4 Homo sapiens 16100.0 ChEMBL 10.1016/j.bmcl.2009.02.029 10.7270/Q2154GX2 19285395 Giannini, G; Marzi, M; Pezzi, R; Brunetti, T; Battistuzzi, G; Marzo, MD; Cabri, W; Vesci, L; Pisano, C R&D Sigma-Tau SpA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50278222 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50278222&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44591988 104120600 CHEMBL472631 ZINC40408107 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50453826 ONC(=O)\C=C\c1ccc(cc1)-c1cc(CN2CCOCC2)on1 InChI=1S/C17H19N3O4/c21-17(18-22)6-3-13-1-4-14(5-2-13)16-11-15(24-19-16)12-20-7-9-23-10-8-20/h1-6,11,22H,7-10,12H2,(H,18,21)/b6-3+ HMZAFAMGNRZJEH-ZZXKWVIFSA-N 50278344 CHEMBL470843::N-hydroxy-3-(4-(5-(morpholinomethyl)isoxazol-3-yl)phenyl)acrylamide hydrochloride Histone deacetylase 4 Homo sapiens 11900 ChEMBL 10.1016/j.bmcl.2009.02.029 10.7270/Q2154GX2 19285395 Giannini, G; Marzi, M; Pezzi, R; Brunetti, T; Battistuzzi, G; Marzo, MD; Cabri, W; Vesci, L; Pisano, C R&D Sigma-Tau SpA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50278344 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50278344&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44592060 104120684 CHEMBL470843 ZINC40892968 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50453837 CC(C=CC(=O)NO)C=C(C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20) ALCVRKZFLFWUAZ-UHFFFAOYSA-N 19130 (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide::CHEMBL99::TSA::Trichostatin A (TSA) Histone deacetylase 4 Homo sapiens 12 ChEMBL 10.1016/j.bmcl.2009.02.029 10.7270/Q2154GX2 19285395 Giannini, G; Marzi, M; Pezzi, R; Brunetti, T; Battistuzzi, G; Marzo, MD; Cabri, W; Vesci, L; Pisano, C R&D Sigma-Tau SpA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19130 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19130&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 91895926 46519165 46024 CHEMBL99 7005 ZINC05579377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50453848 ONC(=O)\C=C\c1ccc(\C=N\OCc2c(F)c(F)c(F)c(F)c2F)cc1 InChI=1S/C17H11F5N2O3/c18-13-11(14(19)16(21)17(22)15(13)20)8-27-23-7-10-3-1-9(2-4-10)5-6-12(25)24-26/h1-7,26H,8H2,(H,24,25)/b6-5+,23-7+ ATRIOAVZXXVRHX-UDVGQSQZSA-N 50278219 CHEMBL471041::N-hydroxy-3-(4-((perfluorobenzyloxyimino)methyl)phenyl)acrylamide::ST-2986 Histone deacetylase 4 Homo sapiens 38800 ChEMBL 10.1016/j.bmcl.2009.02.029 10.7270/Q2154GX2 19285395 Giannini, G; Marzi, M; Pezzi, R; Brunetti, T; Battistuzzi, G; Marzo, MD; Cabri, W; Vesci, L; Pisano, C R&D Sigma-Tau SpA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50278219 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50278219&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44138031 104120597 CHEMBL471041 ZINC40896383 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50453859 ONC(=O)\C=C\c1ccc(\C=N\OCc2ccc(cc2)[N+]([O-])=O)cc1 InChI=1S/C17H15N3O5/c21-17(19-22)10-7-13-1-3-14(4-2-13)11-18-25-12-15-5-8-16(9-6-15)20(23)24/h1-11,22H,12H2,(H,19,21)/b10-7+,18-11+ IWWFFHDXUHSRDM-PFMZDYLOSA-N 50278220 CHEMBL471042::N-hydroxy-3-(4-((4-nitrobenzyloxyimino)methyl)phenyl)acrylamide::ST-2987 Histone deacetylase 4 Homo sapiens 2040 ChEMBL 10.1016/j.bmcl.2009.02.029 10.7270/Q2154GX2 19285395 Giannini, G; Marzi, M; Pezzi, R; Brunetti, T; Battistuzzi, G; Marzo, MD; Cabri, W; Vesci, L; Pisano, C R&D Sigma-Tau SpA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50278220 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50278220&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44138032 104120598 CHEMBL471042 ZINC40896386 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50462552 CC(=O)SCCCCCCNC(=O)c1cc(nn1C)-c1ccc(F)cc1 InChI=1S/C19H24FN3O2S/c1-14(24)26-12-6-4-3-5-11-21-19(25)18-13-17(22-23(18)2)15-7-9-16(20)10-8-15/h7-10,13H,3-6,11-12H2,1-2H3,(H,21,25) GFEBTUQSIHJLIH-UHFFFAOYSA-N 50143422 CHEMBL3759869 Histone deacetylase 4 Homo sapiens 10000 ChEMBL 10.1016/j.bmcl.2015.12.007 10.7270/Q251413S 26706171 Wen, J; Niu, Q; Liu, J; Bao, Y; Yang, J; Luan, S; Fan, Y; Liu, D; Zhao, L Shenyang Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50143422 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50143422&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 9562061 104032616 CHEMBL3759869 C04334 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50474118 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 354 ChEMBL 10.1016/j.ejmech.2016.02.003 10.7270/Q2ZS2ZDZ 26890114 Gong, CJ; Gao, AH; Zhang, YM; Su, MB; Chen, F; Sheng, L; Zhou, YB; Li, JY; Li, J; Nan, FJ Shanghai Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50474119 ONC(=O)CCCCNC(=O)c1nc(sc1C1CC1)-c1nccs1 InChI=1S/C15H18N4O3S2/c20-10(19-22)3-1-2-6-16-13(21)11-12(9-4-5-9)24-15(18-11)14-17-7-8-23-14/h7-9,22H,1-6H2,(H,16,21)(H,19,20) MVJAEZIEZVJAFM-UHFFFAOYSA-N 50020897 CHEMBL3287255::US9216962, CFH367-C Histone deacetylase 4 Homo sapiens 158 ChEMBL 10.1016/j.ejmech.2016.02.003 10.7270/Q2ZS2ZDZ 26890114 Gong, CJ; Gao, AH; Zhang, YM; Su, MB; Chen, F; Sheng, L; Zhou, YB; Li, JY; Li, J; Nan, FJ Shanghai Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50020897 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50020897&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71468161 103931612 CHEMBL3287255 ZINC27739204 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50474122 CC(C)Cc1sc(nc1C(=O)NCCCCC(=O)NO)-c1nccs1 InChI=1S/C16H22N4O3S2/c1-10(2)9-11-13(19-16(25-11)15-18-7-8-24-15)14(22)17-6-4-3-5-12(21)20-23/h7-8,10,23H,3-6,9H2,1-2H3,(H,17,22)(H,20,21) BFMAQRHQZHOUNR-UHFFFAOYSA-N 50020890 CHEMBL3287250::US9216962, CFH382 Histone deacetylase 4 Homo sapiens 185 ChEMBL 10.1016/j.ejmech.2016.02.003 10.7270/Q2ZS2ZDZ 26890114 Gong, CJ; Gao, AH; Zhang, YM; Su, MB; Chen, F; Sheng, L; Zhou, YB; Li, JY; Li, J; Nan, FJ Shanghai Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50020890 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50020890&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71467962 242042329 CHEMBL3287250 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50474123 Nc1ccccc1NC(=O)CCCCNC(=O)c1nc(sc1C1CC1)-c1nccs1 InChI=1S/C21H23N5O2S2/c22-14-5-1-2-6-15(14)25-16(27)7-3-4-10-23-19(28)17-18(13-8-9-13)30-21(26-17)20-24-11-12-29-20/h1-2,5-6,11-13H,3-4,7-10,22H2,(H,23,28)(H,25,27) AMSKTFZUOYSDNP-UHFFFAOYSA-N 50151273 CHEMBL3770345 Histone deacetylase 4 Homo sapiens 2092 ChEMBL 10.1016/j.ejmech.2016.02.003 10.7270/Q2ZS2ZDZ 26890114 Gong, CJ; Gao, AH; Zhang, YM; Su, MB; Chen, F; Sheng, L; Zhou, YB; Li, JY; Li, J; Nan, FJ Shanghai Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50151273 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50151273&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11257669 85603793 CHEMBL3770345 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50474131 ONC(=O)NCCCCNC(=O)c1nc(sc1C1CC1)-c1nccs1 InChI=1S/C15H19N5O3S2/c21-12(16-5-1-2-6-18-15(22)20-23)10-11(9-3-4-9)25-14(19-10)13-17-7-8-24-13/h7-9,23H,1-6H2,(H,16,21)(H2,18,20,22) LOFLAOJBVCUQIM-UHFFFAOYSA-N 50151274 CHEMBL3771123 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2016.02.003 10.7270/Q2ZS2ZDZ 26890114 Gong, CJ; Gao, AH; Zhang, YM; Su, MB; Chen, F; Sheng, L; Zhou, YB; Li, JY; Li, J; Nan, FJ Shanghai Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50151274 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50151274&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11246576 85603454 CHEMBL3771123 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50474141 FC(F)(F)c1nc(no1)-c1cccc(c1)C(=O)NCCCCCNC(=O)c1nc(sc1C1CC1)-c1nccs1 InChI=1S/C25H23F3N6O3S2/c26-25(27,28)24-33-19(34-37-24)15-5-4-6-16(13-15)20(35)29-9-2-1-3-10-30-21(36)17-18(14-7-8-14)39-23(32-17)22-31-11-12-38-22/h4-6,11-14H,1-3,7-10H2,(H,29,35)(H,30,36) UORHYZNTANQQFJ-UHFFFAOYSA-N 50151275 CHEMBL3769706 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2016.02.003 10.7270/Q2ZS2ZDZ 26890114 Gong, CJ; Gao, AH; Zhang, YM; Su, MB; Chen, F; Sheng, L; Zhou, YB; Li, JY; Li, J; Nan, FJ Shanghai Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50151275 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50151275&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44396303 85603176 CHEMBL3769706 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50474145 OC(CCCCNC(=O)c1nc(sc1C1CC1)-c1nccs1)C(F)(F)F InChI=1S/C16H18F3N3O2S2/c17-16(18,19)10(23)3-1-2-6-20-13(24)11-12(9-4-5-9)26-15(22-11)14-21-7-8-25-14/h7-10,23H,1-6H2,(H,20,24) GBPHFTRLBOABLQ-UHFFFAOYSA-N 50151276 CHEMBL3770755 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2016.02.003 10.7270/Q2ZS2ZDZ 26890114 Gong, CJ; Gao, AH; Zhang, YM; Su, MB; Chen, F; Sheng, L; Zhou, YB; Li, JY; Li, J; Nan, FJ Shanghai Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50151276 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50151276&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11750608 85603286 CHEMBL3770755 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50474146 FC(F)(F)C(=O)CCCCNC(=O)c1nc(sc1C1CC1)-c1nccs1 InChI=1S/C16H16F3N3O2S2/c17-16(18,19)10(23)3-1-2-6-20-13(24)11-12(9-4-5-9)26-15(22-11)14-21-7-8-25-14/h7-9H,1-6H2,(H,20,24) OHRUWOKDVPCLPC-UHFFFAOYSA-N 50151277 CHEMBL3770287 Histone deacetylase 4 Homo sapiens 32 ChEMBL 10.1016/j.ejmech.2016.02.003 10.7270/Q2ZS2ZDZ 26890114 Gong, CJ; Gao, AH; Zhang, YM; Su, MB; Chen, F; Sheng, L; Zhou, YB; Li, JY; Li, J; Nan, FJ Shanghai Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50151277 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50151277&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11440517 85603443 CHEMBL3770287 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50474169 FC(F)(F)C(=O)CCCCNC(=O)c1nc(sc1Cc1ccccc1)-c1nccs1 InChI=1S/C20H18F3N3O2S2/c21-20(22,23)15(27)8-4-5-9-24-17(28)16-14(12-13-6-2-1-3-7-13)30-19(26-16)18-25-10-11-29-18/h1-3,6-7,10-11H,4-5,8-9,12H2,(H,24,28) JJZFDILZILDRTQ-UHFFFAOYSA-N 50151283 CHEMBL3771288 Histone deacetylase 4 Homo sapiens 68 ChEMBL 10.1016/j.ejmech.2016.02.003 10.7270/Q2ZS2ZDZ 26890114 Gong, CJ; Gao, AH; Zhang, YM; Su, MB; Chen, F; Sheng, L; Zhou, YB; Li, JY; Li, J; Nan, FJ Shanghai Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50151283 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50151283&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11375675 85603363 CHEMBL3771288 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50474170 Cc1cnc(s1)-c1nc(C(=O)NCCCCC(=O)C(F)(F)F)c(s1)C1CC1 InChI=1S/C17H18F3N3O2S2/c1-9-8-22-15(26-9)16-23-12(13(27-16)10-5-6-10)14(25)21-7-3-2-4-11(24)17(18,19)20/h8,10H,2-7H2,1H3,(H,21,25) GJSCCYDUKNGSLB-UHFFFAOYSA-N 50151282 CHEMBL3770555 Histone deacetylase 4 Homo sapiens 32 ChEMBL 10.1016/j.ejmech.2016.02.003 10.7270/Q2ZS2ZDZ 26890114 Gong, CJ; Gao, AH; Zhang, YM; Su, MB; Chen, F; Sheng, L; Zhou, YB; Li, JY; Li, J; Nan, FJ Shanghai Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50151282 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50151282&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11086495 85605924 CHEMBL3770555 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50474171 FC(F)(F)C(=O)CCCCNC(=O)c1nc(sc1C1CC1)-c1nc2CCCCc2s1 InChI=1S/C20H22F3N3O2S2/c21-20(22,23)14(27)7-3-4-10-24-17(28)15-16(11-8-9-11)30-19(26-15)18-25-12-5-1-2-6-13(12)29-18/h11H,1-10H2,(H,24,28) ZUPRHDPCDWVJDA-UHFFFAOYSA-N 50151281 CHEMBL3770504 Histone deacetylase 4 Homo sapiens 23 ChEMBL 10.1016/j.ejmech.2016.02.003 10.7270/Q2ZS2ZDZ 26890114 Gong, CJ; Gao, AH; Zhang, YM; Su, MB; Chen, F; Sheng, L; Zhou, YB; Li, JY; Li, J; Nan, FJ Shanghai Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50151281 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50151281&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 10005113 85603102 CHEMBL3770504 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50474172 CC(C)Cc1sc(nc1C(=O)NCCCCC(=O)C(F)(F)F)-c1nccs1 InChI=1S/C17H20F3N3O2S2/c1-10(2)9-11-13(23-16(27-11)15-22-7-8-26-15)14(25)21-6-4-3-5-12(24)17(18,19)20/h7-8,10H,3-6,9H2,1-2H3,(H,21,25) AZLBBFOVLFWKTC-UHFFFAOYSA-N 50151280 CHEMBL3771366 Histone deacetylase 4 Homo sapiens 120 ChEMBL 10.1016/j.ejmech.2016.02.003 10.7270/Q2ZS2ZDZ 26890114 Gong, CJ; Gao, AH; Zhang, YM; Su, MB; Chen, F; Sheng, L; Zhou, YB; Li, JY; Li, J; Nan, FJ Shanghai Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50151280 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50151280&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11453120 85603699 CHEMBL3771366 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50474173 FC(F)(F)C(=O)CCCCCNC(=O)c1nc(sc1C1CC1)-c1nccs1 InChI=1S/C17H18F3N3O2S2/c18-17(19,20)11(24)4-2-1-3-7-21-14(25)12-13(10-5-6-10)27-16(23-12)15-22-8-9-26-15/h8-10H,1-7H2,(H,21,25) WCRZTBRZXCWGKV-UHFFFAOYSA-N 50151279 CHEMBL3770531 Histone deacetylase 4 Homo sapiens 133 ChEMBL 10.1016/j.ejmech.2016.02.003 10.7270/Q2ZS2ZDZ 26890114 Gong, CJ; Gao, AH; Zhang, YM; Su, MB; Chen, F; Sheng, L; Zhou, YB; Li, JY; Li, J; Nan, FJ Shanghai Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50151279 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50151279&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11270786 85603506 CHEMBL3770531 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50474174 FC(F)(F)C(=O)CCCNC(=O)c1nc(sc1C1CC1)-c1nccs1 InChI=1S/C15H14F3N3O2S2/c16-15(17,18)9(22)2-1-5-19-12(23)10-11(8-3-4-8)25-14(21-10)13-20-6-7-24-13/h6-8H,1-5H2,(H,19,23) UVCSQKKFUYQSGT-UHFFFAOYSA-N 50151278 CHEMBL3769815 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2016.02.003 10.7270/Q2ZS2ZDZ 26890114 Gong, CJ; Gao, AH; Zhang, YM; Su, MB; Chen, F; Sheng, L; Zhou, YB; Li, JY; Li, J; Nan, FJ Shanghai Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50151278 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50151278&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11453258 85603580 CHEMBL3769815 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50474367 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1 InChI=1S/C24H27N5O3/c30-22(28-32)15-9-1-2-10-16-25-23(31)19-17-26-24(27-18-19)29(20-11-5-3-6-12-20)21-13-7-4-8-14-21/h3-8,11-14,17-18,32H,1-2,9-10,15-16H2,(H,25,31)(H,28,30) QGZYDVAGYRLSKP-UHFFFAOYSA-N 50439674 RICOLINOSTAT::US10858323, Compound 2::US11207431, Example E::US8609678, 2-(diphenylamino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [26] Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.5b01342 10.7270/Q2T155H3 26443078 Yang, Z; Wang, T; Wang, F; Niu, T; Liu, Z; Chen, X; Long, C; Tang, M; Cao, D; Wang, X; Xiang, W; Yi, Y; Ma, L; You, J; Chen, L Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50439674 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50439674&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search AH4 5WGL 53340666 175451991 ZINC89630354 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50474368 COc1ccc(cc1OCCCC(=O)NO)N(C)c1nc(C)nc2ccccc12 InChI=1S/C21H24N4O4/c1-14-22-17-8-5-4-7-16(17)21(23-14)25(2)15-10-11-18(28-3)19(13-15)29-12-6-9-20(26)24-27/h4-5,7-8,10-11,13,27H,6,9,12H2,1-3H3,(H,24,26) FWXZZFONXWYSEF-UHFFFAOYSA-N 50151375 CHEMBL3774414 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.5b01342 10.7270/Q2T155H3 26443078 Yang, Z; Wang, T; Wang, F; Niu, T; Liu, Z; Chen, X; Long, C; Tang, M; Cao, D; Wang, X; Xiang, W; Yi, Y; Ma, L; You, J; Chen, L Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50151375 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50151375&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122550211 104039553 CHEMBL3774414 ZINC00007744 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50474369 Cc1[nH]c2ccccc2c1CCNCc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C21H23N3O2/c1-15-18(19-4-2-3-5-20(19)23-15)12-13-22-14-17-8-6-16(7-9-17)10-11-21(25)24-26/h2-11,22-23,26H,12-14H2,1H3,(H,24,25)/b11-10+ FPOHNWQLNRZRFC-ZHACJKMWSA-N 29589 Faridak::LBH-589::LBH-589B::Panobinostat::US10722597, Compound Panobinostat Histone deacetylase 4 Homo sapiens 338 ChEMBL 10.1021/acs.jmedchem.5b01342 10.7270/Q2T155H3 26443078 Yang, Z; Wang, T; Wang, F; Niu, T; Liu, Z; Chen, X; Long, C; Tang, M; Cao, D; Wang, X; Xiang, W; Yi, Y; Ma, L; You, J; Chen, L Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=29589 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=29589&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search LBH 5EF8 6918837 81055018 ZINC22010649 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50474404 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.5b01342 10.7270/Q2T155H3 26443078 Yang, Z; Wang, T; Wang, F; Niu, T; Liu, Z; Chen, X; Long, C; Tang, M; Cao, D; Wang, X; Xiang, W; Yi, Y; Ma, L; You, J; Chen, L Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50483501 FC(F)(F)c1nc(no1)-c1cccc(c1)C(=O)NCC1(CCOCC1)c1nc(cs1)-c1ccccc1 InChI=1S/C25H21F3N4O3S/c26-25(27,28)22-31-20(32-35-22)17-7-4-8-18(13-17)21(33)29-15-24(9-11-34-12-10-24)23-30-19(14-36-23)16-5-2-1-3-6-16/h1-8,13-14H,9-12,15H2,(H,29,33) HORXBWNTEDOVKN-UHFFFAOYSA-N 50446481 CHEMBL3110004::US10011611, TMP269::US10722597, Compound TMP-269 Histone deacetylase 4 Homo sapiens 134 ChEMBL 10.1016/j.ejmech.2016.03.046 10.7270/Q2057HTZ 27060764 Yoo, J; Kim, SJ; Son, D; Seo, H; Baek, SY; Maeng, CY; Lee, C; Kim, IS; Jung, YH; Lee, SM; Park, HJ Sungkyunkwan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446481 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446481&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search NU9 3ZNR 53344908 194944377 CHEMBL3110004 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50483502 ONC(=O)CCCc1csc(\C=C\c2ccccc2)n1 InChI=1S/C15H16N2O2S/c18-14(17-19)8-4-7-13-11-20-15(16-13)10-9-12-5-2-1-3-6-12/h1-3,5-6,9-11,19H,4,7-8H2,(H,17,18)/b10-9+ HJPIJALRLZVGMS-MDZDMXLPSA-N 50156678 CHEMBL3792392 Histone deacetylase 4 Homo sapiens 19700 ChEMBL 10.1016/j.ejmech.2016.03.046 10.7270/Q2057HTZ 27060764 Yoo, J; Kim, SJ; Son, D; Seo, H; Baek, SY; Maeng, CY; Lee, C; Kim, IS; Jung, YH; Lee, SM; Park, HJ Sungkyunkwan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50156678 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50156678&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 102514716 104043787 CHEMBL3792392 ZINC13585890 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50484097 Cc1cnc(nc1)-c1ccc(cc1)[C@@H]1[C@@H](c2ccccc2)[C@@]1(Cl)C(=O)NO InChI=1S/C21H18ClN3O2/c1-13-11-23-19(24-12-13)16-9-7-15(8-10-16)18-17(14-5-3-2-4-6-14)21(18,22)20(26)25-27/h2-12,17-18,27H,1H3,(H,25,26)/t17-,18-,21+/m1/s1 ZOHXVMRBDNGIDM-OPYAIIAOSA-N 50155803 CHEMBL3793455::US9505736, (1S,2S,3S)-1-Chloro-N-hydroxy-2-(4-(5- methylpyrimidin-2-yl)phenyl)-3- phenylcyclopropanecarboxamide Histone deacetylase 4 Homo sapiens 1150 ChEMBL 10.1021/acsmedchemlett.5b00302 10.7270/Q22Z17DJ 26819662 Luckhurst, CA; Breccia, P; Stott, AJ; Aziz, O; Birch, HL; Bürli, RW; Hughes, SJ; Jarvis, RE; Lamers, M; Leonard, PM; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Wishart, G; Yates, D; Dominguez, C BioFocus http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50155803 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50155803&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72948226 104043170 CHEMBL3793455 ZINC36748718 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50484099 Cc1cnc(nc1)-c1ccc(cc1)[C@@H]1[C@@H](c2ccccc2)[C@@]1(C)C(=O)NO InChI=1S/C22H21N3O2/c1-14-12-23-20(24-13-14)17-10-8-16(9-11-17)19-18(15-6-4-3-5-7-15)22(19,2)21(26)25-27/h3-13,18-19,27H,1-2H3,(H,25,26)/t18-,19-,22-/m1/s1 IFWFKBLRTALKJO-WOIUINJBSA-N 50155804 CHEMBL3793569 Histone deacetylase 4 Homo sapiens 730 ChEMBL 10.1021/acsmedchemlett.5b00302 10.7270/Q22Z17DJ 26819662 Luckhurst, CA; Breccia, P; Stott, AJ; Aziz, O; Birch, HL; Bürli, RW; Hughes, SJ; Jarvis, RE; Lamers, M; Leonard, PM; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Wishart, G; Yates, D; Dominguez, C BioFocus http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50155804 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50155804&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 127028836 104043171 CHEMBL3793569 ZINC49908174 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50484101 Cc1cnc(nc1)-c1ccc(cc1)[C@H]1[C@@H]([C@@H]1c1ccccc1)C(=O)NO InChI=1S/C21H19N3O2/c1-13-11-22-20(23-12-13)16-9-7-15(8-10-16)18-17(19(18)21(25)24-26)14-5-3-2-4-6-14/h2-12,17-19,26H,1H3,(H,24,25)/t17-,18-,19-/m1/s1 VEYGHBGGCALTMA-GUDVDZBRSA-N 50155843 CHEMBL3793034::US9765054, Compound 50K Histone deacetylase 4 Homo sapiens 510 ChEMBL 10.1021/acsmedchemlett.5b00302 10.7270/Q22Z17DJ 26819662 Luckhurst, CA; Breccia, P; Stott, AJ; Aziz, O; Birch, HL; Bürli, RW; Hughes, SJ; Jarvis, RE; Lamers, M; Leonard, PM; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Wishart, G; Yates, D; Dominguez, C BioFocus http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50155843 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50155843&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148738 104043210 CHEMBL3793034 ZINC28461075 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50489726 ONC(=O)[C@]1(F)[C@@H]([C@H]1c1ccc(cc1)-c1ncc(Cl)cn1)c1ccccc1 InChI=1S/C20H15ClFN3O2/c21-15-10-23-18(24-11-15)14-8-6-13(7-9-14)17-16(12-4-2-1-3-5-12)20(17,22)19(26)25-27/h1-11,16-17,27H,(H,25,26)/t16-,17-,20+/m1/s1 PXXBZPNRBLVAQD-HLIPFELVSA-N 50161829 CHEMBL3794140 Histone deacetylase 4 Homo sapiens 40 ChEMBL 10.1021/acsmedchemlett.5b00302 10.7270/Q22Z17DJ 26819662 Luckhurst, CA; Breccia, P; Stott, AJ; Aziz, O; Birch, HL; Bürli, RW; Hughes, SJ; Jarvis, RE; Lamers, M; Leonard, PM; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Wishart, G; Yates, D; Dominguez, C BioFocus http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50161829 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50161829&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72948414 341096904 CHEMBL3794140 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50489727 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1ncc(Cl)cn1)c1ccccc1 InChI=1S/C20H16ClN3O2/c21-15-10-22-19(23-11-15)14-8-6-13(7-9-14)17-16(18(17)20(25)24-26)12-4-2-1-3-5-12/h1-11,16-18,26H,(H,24,25)/t16-,17-,18-/m1/s1 JLUNPOGVRYFTEO-KZNAEPCWSA-N 50160873 CHEMBL3794544::US9765054, Compound 50j Histone deacetylase 4 Homo sapiens 430 ChEMBL 10.1021/acsmedchemlett.5b00302 10.7270/Q22Z17DJ 26819662 Luckhurst, CA; Breccia, P; Stott, AJ; Aziz, O; Birch, HL; Bürli, RW; Hughes, SJ; Jarvis, RE; Lamers, M; Leonard, PM; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Wishart, G; Yates, D; Dominguez, C BioFocus http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50160873 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50160873&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148737 340134787 CHEMBL3794544 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50489728 ONC(=O)[C@]1(F)[C@@H]([C@H]1c1ccc(cc1)-c1cnco1)c1ccccc1 InChI=1S/C19H15FN2O3/c20-19(18(23)22-24)16(13-4-2-1-3-5-13)17(19)14-8-6-12(7-9-14)15-10-21-11-25-15/h1-11,16-17,24H,(H,22,23)/t16-,17-,19+/m1/s1 TUZLRTHLFZOEMM-LMMKCTJWSA-N 50161830 CHEMBL3793439 Histone deacetylase 4 Homo sapiens 10 ChEMBL 10.1021/acsmedchemlett.5b00302 10.7270/Q22Z17DJ 26819662 Luckhurst, CA; Breccia, P; Stott, AJ; Aziz, O; Birch, HL; Bürli, RW; Hughes, SJ; Jarvis, RE; Lamers, M; Leonard, PM; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Wishart, G; Yates, D; Dominguez, C BioFocus http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50161830 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50161830&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72948223 341096905 CHEMBL3793439 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50489729 ONC(=O)[C@]1(F)[C@@H]([C@H]1c1ccc(cc1)-c1ncc(Cl)cn1)c1ccccc1 InChI=1S/C20H15ClFN3O2/c21-15-10-23-18(24-11-15)14-8-6-13(7-9-14)17-16(12-4-2-1-3-5-12)20(17,22)19(26)25-27/h1-11,16-17,27H,(H,25,26)/t16-,17-,20+/m1/s1 PXXBZPNRBLVAQD-HLIPFELVSA-N 50161829 CHEMBL3794140 Histone deacetylase 4 Homo sapiens 230 ChEMBL 10.1021/acsmedchemlett.5b00302 10.7270/Q22Z17DJ 26819662 Luckhurst, CA; Breccia, P; Stott, AJ; Aziz, O; Birch, HL; Bürli, RW; Hughes, SJ; Jarvis, RE; Lamers, M; Leonard, PM; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Wishart, G; Yates, D; Dominguez, C BioFocus http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50161829 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50161829&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72948414 341096904 CHEMBL3794140 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50489730 ONC(=O)[C@]1(F)[C@@H]([C@H]1c1ccc(cc1)-c1nccc(n1)C(F)(F)F)c1ccccc1 InChI=1S/C21H15F4N3O2/c22-20(19(29)28-30)16(12-4-2-1-3-5-12)17(20)13-6-8-14(9-7-13)18-26-11-10-15(27-18)21(23,24)25/h1-11,16-17,30H,(H,28,29)/t16-,17-,20+/m1/s1 DDTXYXHMSVMLET-HLIPFELVSA-N 50161831 CHEMBL3793932::US9505736, (1S,2S,3S)-1-Fluoro-N-hydroxy-2-phenyl- 3-(4-(4-(trifluoromethyl)pyrimidin-2- yl)phenyl)cyclopropanecarboxamide Histone deacetylase 4 Homo sapiens 40 ChEMBL 10.1021/acsmedchemlett.5b00302 10.7270/Q22Z17DJ 26819662 Luckhurst, CA; Breccia, P; Stott, AJ; Aziz, O; Birch, HL; Bürli, RW; Hughes, SJ; Jarvis, RE; Lamers, M; Leonard, PM; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Wishart, G; Yates, D; Dominguez, C BioFocus http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50161831 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50161831&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72948224 341096906 CHEMBL3793932 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50489757 Cc1[nH]c2ccccc2c1\C=C\c1ccccc1-c1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C26H22N2O2/c1-18-22(24-8-4-5-9-25(24)27-18)16-15-20-6-2-3-7-23(20)21-13-10-19(11-14-21)12-17-26(29)28-30/h2-17,27,30H,1H3,(H,28,29)/b16-15+,17-12+ PRMXPZIOPNPPCX-JDWGSQHISA-N 50161828 CHEMBL3793310 Histone deacetylase 4 Homo sapiens 17100 ChEMBL 10.1016/j.ejmech.2016.02.001 10.7270/Q2HM5BB0 26890116 Cincinelli, R; Zwick, V; Musso, L; Zuco, V; De Cesare, M; Zunino, F; Simoes-Pires, C; Nurisso, A; Giannini, G; Cuendet, M; Dallavalle, S University of Milan http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50161828 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50161828&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 127030313 104048133 CHEMBL3793310 ZINC13609207 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50489772 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 490 ChEMBL 10.1016/j.ejmech.2016.02.001 10.7270/Q2HM5BB0 26890116 Cincinelli, R; Zwick, V; Musso, L; Zuco, V; De Cesare, M; Zunino, F; Simoes-Pires, C; Nurisso, A; Giannini, G; Cuendet, M; Dallavalle, S University of Milan http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50488851 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1ncc(Cl)cn1)c1ccccc1 InChI=1S/C20H16ClN3O2/c21-15-10-22-19(23-11-15)14-8-6-13(7-9-14)17-16(18(17)20(25)24-26)12-4-2-1-3-5-12/h1-11,16-18,26H,(H,24,25)/t16-,17-,18-/m1/s1 JLUNPOGVRYFTEO-KZNAEPCWSA-N 50160873 CHEMBL3794544::US9765054, Compound 50j Histone deacetylase 4 Homo sapiens 140 ChEMBL 10.1021/acsmedchemlett.5b00302 10.7270/Q22Z17DJ 26819662 Luckhurst, CA; Breccia, P; Stott, AJ; Aziz, O; Birch, HL; Bürli, RW; Hughes, SJ; Jarvis, RE; Lamers, M; Leonard, PM; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Wishart, G; Yates, D; Dominguez, C BioFocus http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50160873 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50160873&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148737 340134787 CHEMBL3794544 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50489026 ONC(=O)[C@]1(F)[C@@H]([C@H]1c1ccc(cc1)-c1ncc(OC(F)F)cn1)c1ccccc1 InChI=1S/C21H16F3N3O3/c22-20(23)30-15-10-25-18(26-11-15)14-8-6-13(7-9-14)17-16(12-4-2-1-3-5-12)21(17,24)19(28)27-29/h1-11,16-17,20,29H,(H,27,28)/t16-,17-,21+/m1/s1 RUTGGTYDBCHEPE-LZJOCLMNSA-N 50160874 CHEMBL3794485::US9505736, (1S,2S,3S)-2-(4-(5- (Difluoromethoxy)pyrimidin-2-yl)phenyl)-1- fluoro-N-hydroxy-3- phenylcyclopropanecarboxamide Histone deacetylase 4 Homo sapiens 30 ChEMBL 10.1021/acsmedchemlett.5b00302 10.7270/Q22Z17DJ 26819662 Luckhurst, CA; Breccia, P; Stott, AJ; Aziz, O; Birch, HL; Bürli, RW; Hughes, SJ; Jarvis, RE; Lamers, M; Leonard, PM; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Wishart, G; Yates, D; Dominguez, C BioFocus http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50160874 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50160874&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72948227 340134788 CHEMBL3794485 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50489027 ONC(=O)[C@]1(F)[C@@H]([C@H]1c1ccc(cc1)-c1ncc(F)cn1)c1ccccc1 InChI=1S/C20H15F2N3O2/c21-15-10-23-18(24-11-15)14-8-6-13(7-9-14)17-16(12-4-2-1-3-5-12)20(17,22)19(26)25-27/h1-11,16-17,27H,(H,25,26)/t16-,17-,20+/m1/s1 MREATSZIGJDNKB-HLIPFELVSA-N 50160879 CHEMBL3793392::US9505736, (1S,2S,3S)-1-Fluoro-2-(4-(5- fluoropyrimidin-2-yl)phenyl)-N-hydroxy-3- phenylcyclopropanecarboxamide Histone deacetylase 4 Homo sapiens 20 ChEMBL 10.1021/acsmedchemlett.5b00302 10.7270/Q22Z17DJ 26819662 Luckhurst, CA; Breccia, P; Stott, AJ; Aziz, O; Birch, HL; Bürli, RW; Hughes, SJ; Jarvis, RE; Lamers, M; Leonard, PM; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Wishart, G; Yates, D; Dominguez, C BioFocus http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50160879 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50160879&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search OTF 5A2S 72722126 340134793 CHEMBL3793392 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50489028 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1nccc(n1)C(F)(F)F)c1ccccc1 InChI=1S/C21H16F3N3O2/c22-21(23,24)15-10-11-25-19(26-15)14-8-6-13(7-9-14)17-16(18(17)20(28)27-29)12-4-2-1-3-5-12/h1-11,16-18,29H,(H,27,28)/t16-,17-,18-/m1/s1 ABWQSANXEMWPFY-KZNAEPCWSA-N 50160875 CHEMBL3794334::US9765054, Compound 50d Histone deacetylase 4 Homo sapiens 80 ChEMBL 10.1021/acsmedchemlett.5b00302 10.7270/Q22Z17DJ 26819662 Luckhurst, CA; Breccia, P; Stott, AJ; Aziz, O; Birch, HL; Bürli, RW; Hughes, SJ; Jarvis, RE; Lamers, M; Leonard, PM; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Wishart, G; Yates, D; Dominguez, C BioFocus http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50160875 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50160875&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148714 340134789 CHEMBL3794334 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50489029 ONC(=O)[C@]1(F)[C@@H]([C@H]1c1ccc(cc1)-c1ncc(OC(F)F)cn1)c1ccccc1 InChI=1S/C21H16F3N3O3/c22-20(23)30-15-10-25-18(26-11-15)14-8-6-13(7-9-14)17-16(12-4-2-1-3-5-12)21(17,24)19(28)27-29/h1-11,16-17,20,29H,(H,27,28)/t16-,17-,21+/m1/s1 RUTGGTYDBCHEPE-LZJOCLMNSA-N 50160874 CHEMBL3794485::US9505736, (1S,2S,3S)-2-(4-(5- (Difluoromethoxy)pyrimidin-2-yl)phenyl)-1- fluoro-N-hydroxy-3- phenylcyclopropanecarboxamide Histone deacetylase 4 Homo sapiens 150 ChEMBL 10.1021/acsmedchemlett.5b00302 10.7270/Q22Z17DJ 26819662 Luckhurst, CA; Breccia, P; Stott, AJ; Aziz, O; Birch, HL; Bürli, RW; Hughes, SJ; Jarvis, RE; Lamers, M; Leonard, PM; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Wishart, G; Yates, D; Dominguez, C BioFocus http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50160874 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50160874&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72948227 340134788 CHEMBL3794485 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50515924 Nc1ccc(cc1NC(=O)[C@H]1C[C@@H]2CC[C@H](C1)O2)-c1ccc(F)cc1 InChI=1S/C20H21FN2O2/c21-15-4-1-12(2-5-15)13-3-8-18(22)19(11-13)23-20(24)14-9-16-6-7-17(10-14)25-16/h1-5,8,11,14,16-17H,6-7,9-10,22H2,(H,23,24)/t14-,16-,17+ SBKJRDAJADZOCH-XGBSXSJOSA-N 50189911 CHEMBL3827611 Histone deacetylase 4 Homo sapiens >33330 ChEMBL 10.1016/j.bmc.2016.06.040 10.7270/Q23B6220 27377864 Wagner, FF; Weïwer, M; Steinbacher, S; Schomburg, A; Reinemer, P; Gale, JP; Campbell, AJ; Fisher, SL; Zhao, WN; Reis, SA; Hennig, KM; Thomas, M; Müller, P; Jefson, MR; Fass, DM; Haggarty, SJ; Zhang, YL; Holson, EB Broad Institute of MIT and Harvard http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50189911 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50189911&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6EZ 5IX0 121499152 104073364 CHEMBL3827611 ZINC34909607 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50515925 Cc1[nH]c2ccccc2c1CCNCc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C21H23N3O2/c1-15-18(19-4-2-3-5-20(19)23-15)12-13-22-14-17-8-6-16(7-9-17)10-11-21(25)24-26/h2-11,22-23,26H,12-14H2,1H3,(H,24,25)/b11-10+ FPOHNWQLNRZRFC-ZHACJKMWSA-N 29589 Faridak::LBH-589::LBH-589B::Panobinostat::US10722597, Compound Panobinostat Histone deacetylase 4 Homo sapiens 373 ChEMBL 10.1016/j.bmc.2016.06.040 10.7270/Q23B6220 27377864 Wagner, FF; Weïwer, M; Steinbacher, S; Schomburg, A; Reinemer, P; Gale, JP; Campbell, AJ; Fisher, SL; Zhao, WN; Reis, SA; Hennig, KM; Thomas, M; Müller, P; Jefson, MR; Fass, DM; Haggarty, SJ; Zhang, YL; Holson, EB Broad Institute of MIT and Harvard http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=29589 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=29589&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search LBH 5EF8 6918837 81055018 ZINC22010649 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50511636 COc1ccc(cc1)-c1nc(N2CCOCC2)c2nc(CN(C)c3ncc(cn3)C(=O)NO)n(C)c2n1 InChI=1S/C24H27N9O4/c1-31(24-25-12-16(13-26-24)23(34)30-35)14-18-27-19-21(32(18)2)28-20(15-4-6-17(36-3)7-5-15)29-22(19)33-8-10-37-11-9-33/h4-7,12-13,35H,8-11,14H2,1-3H3,(H,30,34) XNNZURYUKHKSRF-UHFFFAOYSA-N 50188891 CHEMBL3828518 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acs.jmedchem.6b00579 10.7270/Q2T155K0 27186676 Chen, Y; Wang, X; Xiang, W; He, L; Tang, M; Wang, F; Wang, T; Yang, Z; Yi, Y; Wang, H; Niu, T; Zheng, L; Lei, L; Li, X; Song, H; Chen, L West China Hospital of Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50188891 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50188891&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122648343 346534981 CHEMBL3828518 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50511637 CN(Cc1nc2c(nc(nc2n1C)-c1ccc(N)cc1)N1CCOCC1)c1ncc(cn1)C(=O)NO InChI=1S/C23H26N10O3/c1-31(23-25-11-15(12-26-23)22(34)30-35)13-17-27-18-20(32(17)2)28-19(14-3-5-16(24)6-4-14)29-21(18)33-7-9-36-10-8-33/h3-6,11-12,35H,7-10,13,24H2,1-2H3,(H,30,34) WZIGNCHAFITFNX-UHFFFAOYSA-N 50188637 CHEMBL3827814 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acs.jmedchem.6b00579 10.7270/Q2T155K0 27186676 Chen, Y; Wang, X; Xiang, W; He, L; Tang, M; Wang, F; Wang, T; Yang, Z; Yi, Y; Wang, H; Niu, T; Zheng, L; Lei, L; Li, X; Song, H; Chen, L West China Hospital of Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50188637 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50188637&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122648367 346534970 CHEMBL3827814 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50511638 CN(Cc1nc2c(nc(nc2n1C)-c1cnc(N)nc1)N1CCOCC1)c1ncc(cn1)C(=O)NO InChI=1S/C21H24N12O3/c1-31(21-25-9-13(10-26-21)19(34)30-35)11-14-27-15-17(32(14)2)28-16(12-7-23-20(22)24-8-12)29-18(15)33-3-5-36-6-4-33/h7-10,35H,3-6,11H2,1-2H3,(H,30,34)(H2,22,23,24) GWNBFGJNUNUOOI-UHFFFAOYSA-N 50188959 CHEMBL3827894 Histone deacetylase 4 Homo sapiens 653 ChEMBL 10.1021/acs.jmedchem.6b00579 10.7270/Q2T155K0 27186676 Chen, Y; Wang, X; Xiang, W; He, L; Tang, M; Wang, F; Wang, T; Yang, Z; Yi, Y; Wang, H; Niu, T; Zheng, L; Lei, L; Li, X; Song, H; Chen, L West China Hospital of Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50188959 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50188959&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122648648 104072685 CHEMBL3827894 ZINC13589050 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50511639 COc1ccc(cn1)-c1nc(N2CCOCC2)c2nc(CN(C)c3ncc(cn3)C(=O)NO)n(C)c2n1 InChI=1S/C23H26N10O4/c1-31(23-25-11-15(12-26-23)22(34)30-35)13-16-27-18-20(32(16)2)28-19(14-4-5-17(36-3)24-10-14)29-21(18)33-6-8-37-9-7-33/h4-5,10-12,35H,6-9,13H2,1-3H3,(H,30,34) ZPAHLBXHWVNFMV-UHFFFAOYSA-N 50188897 CHEMBL3827281 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acs.jmedchem.6b00579 10.7270/Q2T155K0 27186676 Chen, Y; Wang, X; Xiang, W; He, L; Tang, M; Wang, F; Wang, T; Yang, Z; Yi, Y; Wang, H; Niu, T; Zheng, L; Lei, L; Li, X; Song, H; Chen, L West China Hospital of Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50188897 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50188897&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122648600 346534987 CHEMBL3827281 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50511640 CN(Cc1nc2c(nc(nc2n1C)-c1ccncc1)N1CCOCC1)c1ncc(cn1)C(=O)NO InChI=1S/C22H24N10O3/c1-30(22-24-11-15(12-25-22)21(33)29-34)13-16-26-17-19(31(16)2)27-18(14-3-5-23-6-4-14)28-20(17)32-7-9-35-10-8-32/h3-6,11-12,34H,7-10,13H2,1-2H3,(H,29,33) ZGYDQVJYONGOFO-UHFFFAOYSA-N 50188899 CHEMBL3827517 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acs.jmedchem.6b00579 10.7270/Q2T155K0 27186676 Chen, Y; Wang, X; Xiang, W; He, L; Tang, M; Wang, F; Wang, T; Yang, Z; Yi, Y; Wang, H; Niu, T; Zheng, L; Lei, L; Li, X; Song, H; Chen, L West China Hospital of Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50188899 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50188899&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122648649 346534989 CHEMBL3827517 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50511641 COc1ccc(cn1)-c1nc(N2CCOCC2)c2sc(CN(C)c3ncc(cn3)C(=O)NO)cc2n1 InChI=1S/C23H24N8O4S/c1-30(23-25-11-15(12-26-23)22(32)29-33)13-16-9-17-19(36-16)21(31-5-7-35-8-6-31)28-20(27-17)14-3-4-18(34-2)24-10-14/h3-4,9-12,33H,5-8,13H2,1-2H3,(H,29,32) JOWXJLIFIIOYMS-UHFFFAOYSA-N 50188961 CHEMBL3622533 Histone deacetylase 4 Homo sapiens 409 ChEMBL 10.1021/acs.jmedchem.6b00579 10.7270/Q2T155K0 27186676 Chen, Y; Wang, X; Xiang, W; He, L; Tang, M; Wang, F; Wang, T; Yang, Z; Yi, Y; Wang, H; Niu, T; Zheng, L; Lei, L; Li, X; Song, H; Chen, L West China Hospital of Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50188961 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50188961&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 54575456 104072687 CHEMBL3622533 ZINC13444145 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50511642 Cc1[nH]c2ccccc2c1CCNCc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C21H23N3O2/c1-15-18(19-4-2-3-5-20(19)23-15)12-13-22-14-17-8-6-16(7-9-17)10-11-21(25)24-26/h2-11,22-23,26H,12-14H2,1H3,(H,24,25)/b11-10+ FPOHNWQLNRZRFC-ZHACJKMWSA-N 29589 Faridak::LBH-589::LBH-589B::Panobinostat::US10722597, Compound Panobinostat Histone deacetylase 4 Homo sapiens 338 ChEMBL 10.1021/acs.jmedchem.6b00579 10.7270/Q2T155K0 27186676 Chen, Y; Wang, X; Xiang, W; He, L; Tang, M; Wang, F; Wang, T; Yang, Z; Yi, Y; Wang, H; Niu, T; Zheng, L; Lei, L; Li, X; Song, H; Chen, L West China Hospital of Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=29589 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=29589&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search LBH 5EF8 6918837 81055018 ZINC22010649 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50516161 ONC(=O)CCCCCC(c1c[nH]c2ccccc12)c1c[nH]c2ccccc12 InChI=1S/C23H25N3O2/c27-23(26-28)13-3-1-2-8-16(19-14-24-21-11-6-4-9-17(19)21)20-15-25-22-12-7-5-10-18(20)22/h4-7,9-12,14-16,24-25,28H,1-3,8,13H2,(H,26,27) ZWBFOQJCRGCPED-UHFFFAOYSA-N 50297444 CHEMBL564876::N-hydroxy-7,7-di(1H-indol-3-yl)heptanamide::ST-2741 Histone deacetylase 4 Homo sapiens 1300.00 ChEMBL 10.1016/j.bmcl.2009.03.101 10.7270/Q2PN95PT 19359173 Giannini, G; Marzi, M; Marzo, MD; Battistuzzi, G; Pezzi, R; Brunetti, T; Cabri, W; Vesci, L; Pisano, C Sigma-Tau Research and Development http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50297444 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50297444&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11993691 104138975 CHEMBL564876 ZINC43010733 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50516162 COc1cccc2c(c[nH]c12)C(CCCCCC(=O)NO)c1c[nH]c2c(OC)cccc12 InChI=1S/C25H29N3O4/c1-31-21-11-6-9-17-19(14-26-24(17)21)16(8-4-3-5-13-23(29)28-30)20-15-27-25-18(20)10-7-12-22(25)32-2/h6-7,9-12,14-16,26-27,30H,3-5,8,13H2,1-2H3,(H,28,29) FSLXJUDEBBIVKO-UHFFFAOYSA-N 50297445 CHEMBL561483::N-hydroxy-7,7-bis(7-methoxy-1H-indol-3-yl)heptanamide Histone deacetylase 4 Homo sapiens 220.00 ChEMBL 10.1016/j.bmcl.2009.03.101 10.7270/Q2PN95PT 19359173 Giannini, G; Marzi, M; Marzo, MD; Battistuzzi, G; Pezzi, R; Brunetti, T; Cabri, W; Vesci, L; Pisano, C Sigma-Tau Research and Development http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50297445 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50297445&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11993694 104138976 CHEMBL561483 ZINC43118302 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50516163 ONC(=O)CCCCCC(c1c[nH]c2ccc(cc12)[N+]([O-])=O)c1c[nH]c2ccc(cc12)[N+]([O-])=O InChI=1S/C23H23N5O6/c29-23(26-30)5-3-1-2-4-16(19-12-24-21-8-6-14(27(31)32)10-17(19)21)20-13-25-22-9-7-15(28(33)34)11-18(20)22/h6-13,16,24-25,30H,1-5H2,(H,26,29) VSVDNXSUROYWOP-UHFFFAOYSA-N 50297446 CHEMBL561604::N-hydroxy-7,7-bis(5-nitro-1H-indol-3-yl)heptanamide::ST-5732 Histone deacetylase 4 Homo sapiens 220.00 ChEMBL 10.1016/j.bmcl.2009.03.101 10.7270/Q2PN95PT 19359173 Giannini, G; Marzi, M; Marzo, MD; Battistuzzi, G; Pezzi, R; Brunetti, T; Cabri, W; Vesci, L; Pisano, C Sigma-Tau Research and Development http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50297446 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50297446&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 45269423 104138977 CHEMBL561604 ZINC43020382 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50516164 ONC(=O)\C=C\c1ccc(cc1)C(c1c[nH]c2ccccc12)c1c[nH]c2ccccc12 InChI=1S/C26H21N3O2/c30-25(29-31)14-11-17-9-12-18(13-10-17)26(21-15-27-23-7-3-1-5-19(21)23)22-16-28-24-8-4-2-6-20(22)24/h1-16,26-28,31H,(H,29,30)/b14-11+ WOXWAGCBPDSRPN-SDNWHVSQSA-N 50297447 3-(4-(di(1H-indol-3-yl)methyl)phenyl)-N-hydroxyacrylamide::CHEMBL564382::ST-2887 Histone deacetylase 4 Homo sapiens 4800.00 ChEMBL 10.1016/j.bmcl.2009.03.101 10.7270/Q2PN95PT 19359173 Giannini, G; Marzi, M; Marzo, MD; Battistuzzi, G; Pezzi, R; Brunetti, T; Cabri, W; Vesci, L; Pisano, C Sigma-Tau Research and Development http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50297447 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50297447&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11993595 104138978 CHEMBL564382 ZINC43014180 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50516165 Nc1ccccc1NC(=O)CCCCCC(c1c[nH]c2ccccc12)c1c[nH]c2ccccc12 InChI=1S/C29H30N4O/c30-25-13-6-9-16-28(25)33-29(34)17-3-1-2-10-20(23-18-31-26-14-7-4-11-21(23)26)24-19-32-27-15-8-5-12-22(24)27/h4-9,11-16,18-20,31-32H,1-3,10,17,30H2,(H,33,34) KJPFZGOXSBMBCC-UHFFFAOYSA-N 50297448 CHEMBL564916::N-(2-aminophenyl)-7,7-di(1H-indol-3-yl)heptanamide::ST-3071 Histone deacetylase 4 Homo sapiens 150000.00 ChEMBL 10.1016/j.bmcl.2009.03.101 10.7270/Q2PN95PT 19359173 Giannini, G; Marzi, M; Marzo, MD; Battistuzzi, G; Pezzi, R; Brunetti, T; Cabri, W; Vesci, L; Pisano, C Sigma-Tau Research and Development http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50297448 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50297448&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 45271073 104138979 CHEMBL564916 ZINC43010294 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50552076 COc1cc2ncnc(Nc3cccc(c3)C#C)c2cc1OCCCCCCC(=O)NO InChI=1S/C24H26N4O4/c1-3-17-9-8-10-18(13-17)27-24-19-14-22(21(31-2)15-20(19)25-16-26-24)32-12-7-5-4-6-11-23(29)28-30/h1,8-10,13-16,30H,4-7,11-12H2,2H3,(H,28,29)(H,25,26,27) PLIVFNIUGLLCEK-UHFFFAOYSA-N 50307768 7-(4-(3-Ethynylphenylamino)-7-methoxyquinazolin-6-yloxy)-N-hydroxyheptanamide::CHEMBL598797::CUDC-101 Histone deacetylase 4 Homo sapiens 13 ChEMBL 10.1021/jm901453q 10.7270/Q2CR5TGQ 20143778 Cai, X; Zhai, HX; Wang, J; Forrester, J; Qu, H; Yin, L; Lai, CJ; Bao, R; Qian, C Curis Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50307768 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50307768&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 24756910 104162129 CHEMBL598797 ZINC43196377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50535337 ONC(=O)C(c1ccc(Cl)cc1)c1ccc(Cl)cc1 InChI=1S/C14H11Cl2NO2/c15-11-5-1-9(2-6-11)13(14(18)17-19)10-3-7-12(16)8-4-10/h1-8,13,19H,(H,17,18) MITRLTIJDHOUFN-UHFFFAOYSA-N 50300452 2,2-bis(4-chlorophenyl)-N-hydroxyacetamide::CHEMBL572805 Histone deacetylase 4 Homo sapiens 960 ChEMBL 10.1016/j.bmcl.2009.08.010 10.7270/Q2NZ87QH 19699639 Tessier, P; Smil, DV; Wahhab, A; Leit, S; Rahil, J; Li, Z; Deziel, R; Besterman, JM MethylGene Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50300452 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50300452&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 45482643 104154813 CHEMBL572805 ZINC45285058 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50535338 ONC(=O)C(c1ccc2OCCc2c1)c1ccc2OCCc2c1 InChI=1S/C18H17NO4/c20-18(19-21)17(13-1-3-15-11(9-13)5-7-22-15)14-2-4-16-12(10-14)6-8-23-16/h1-4,9-10,17,21H,5-8H2,(H,19,20) WEOWFSNVPPFUOU-UHFFFAOYSA-N 50300453 2,2-bis(2,3-dihydrobenzofuran-5-yl)-N-hydroxyacetamide::CHEMBL583967 Histone deacetylase 4 Homo sapiens 210 ChEMBL 10.1016/j.bmcl.2009.08.010 10.7270/Q2NZ87QH 19699639 Tessier, P; Smil, DV; Wahhab, A; Leit, S; Rahil, J; Li, Z; Deziel, R; Besterman, JM MethylGene Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50300453 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50300453&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44626297 104154814 CHEMBL583967 ZINC45318016 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50535339 CS(=O)(=O)Nc1ccc(cc1)C(C(=O)NO)c1ccc(NS(C)(=O)=O)cc1 InChI=1S/C16H19N3O6S2/c1-26(22,23)18-13-7-3-11(4-8-13)15(16(20)17-21)12-5-9-14(10-6-12)19-27(2,24)25/h3-10,15,18-19,21H,1-2H3,(H,17,20) NDCGISZPOIMWEF-UHFFFAOYSA-N 50300454 CHEMBL574378::N-hydroxy-2,2-bis(4-(methylsulfonamido)phenyl)acetamide Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.bmcl.2009.08.010 10.7270/Q2NZ87QH 19699639 Tessier, P; Smil, DV; Wahhab, A; Leit, S; Rahil, J; Li, Z; Deziel, R; Besterman, JM MethylGene Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50300454 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50300454&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 45482635 104154815 CHEMBL574378 ZINC45286163 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50535340 ONC(=O)C(c1cccc(F)c1)c1cccc(F)c1 InChI=1S/C14H11F2NO2/c15-11-5-1-3-9(7-11)13(14(18)17-19)10-4-2-6-12(16)8-10/h1-8,13,19H,(H,17,18) OCJJUBQJPOHGBE-UHFFFAOYSA-N 50300443 2,2-bis(3-fluorophenyl)-N-hydroxyacetamide::CHEMBL574594 Histone deacetylase 4 Homo sapiens 700 ChEMBL 10.1016/j.bmcl.2009.08.010 10.7270/Q2NZ87QH 19699639 Tessier, P; Smil, DV; Wahhab, A; Leit, S; Rahil, J; Li, Z; Deziel, R; Besterman, JM MethylGene Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50300443 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50300443&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 45482630 104154804 CHEMBL574594 ZINC45286806 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50535341 ONC(=O)C(c1ccc(F)cc1)c1ccc(F)cc1 InChI=1S/C14H11F2NO2/c15-11-5-1-9(2-6-11)13(14(18)17-19)10-3-7-12(16)8-4-10/h1-8,13,19H,(H,17,18) HHJNWMNXSDYVHL-UHFFFAOYSA-N 50300444 2,2-bis(4-fluorophenyl)-N-hydroxyacetamide::CHEMBL573190 Histone deacetylase 4 Homo sapiens 1100 ChEMBL 10.1016/j.bmcl.2009.08.010 10.7270/Q2NZ87QH 19699639 Tessier, P; Smil, DV; Wahhab, A; Leit, S; Rahil, J; Li, Z; Deziel, R; Besterman, JM MethylGene Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50300444 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50300444&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 45482672 104154805 CHEMBL573190 ZINC45283761 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50535342 CN1c2ccccc2C(C(=O)NO)c2ccccc12 InChI=1S/C15H14N2O2/c1-17-12-8-4-2-6-10(12)14(15(18)16-19)11-7-3-5-9-13(11)17/h2-9,14,19H,1H3,(H,16,18) QZUGUUMWGJYJFD-UHFFFAOYSA-N 50300445 CHEMBL572545::N-hydroxy-10-methyl-9,10-dihydroacridine-9-carboxamide Histone deacetylase 4 Homo sapiens 1910 ChEMBL 10.1016/j.bmcl.2009.08.010 10.7270/Q2NZ87QH 19699639 Tessier, P; Smil, DV; Wahhab, A; Leit, S; Rahil, J; Li, Z; Deziel, R; Besterman, JM MethylGene Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50300445 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50300445&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 45482667 104154806 CHEMBL572545 ZINC45288616 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50535343 ONC(=O)C1c2ccccc2Oc2ccccc12 InChI=1S/C14H11NO3/c16-14(15-17)13-9-5-1-3-7-11(9)18-12-8-4-2-6-10(12)13/h1-8,13,17H,(H,15,16) ULUVQBMMAOHWSH-UHFFFAOYSA-N 50300446 CHEMBL583490::N-hydroxy-9H-xanthene-9-carboxamide Histone deacetylase 4 Homo sapiens 250 ChEMBL 10.1016/j.bmcl.2009.08.010 10.7270/Q2NZ87QH 19699639 Tessier, P; Smil, DV; Wahhab, A; Leit, S; Rahil, J; Li, Z; Deziel, R; Besterman, JM MethylGene Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50300446 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50300446&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44626296 104154807 CHEMBL583490 ZINC45321222 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50535344 ONC(=O)C1c2ccccc2Cc2ccccc12 InChI=1S/C15H13NO2/c17-15(16-18)14-12-7-3-1-5-10(12)9-11-6-2-4-8-13(11)14/h1-8,14,18H,9H2,(H,16,17) SIYRPEHGIQLXJG-UHFFFAOYSA-N 50300447 CHEMBL575482::N-hydroxy-9,10-dihydroanthracene-9-carboxamide Histone deacetylase 4 Homo sapiens 2320 ChEMBL 10.1016/j.bmcl.2009.08.010 10.7270/Q2NZ87QH 19699639 Tessier, P; Smil, DV; Wahhab, A; Leit, S; Rahil, J; Li, Z; Deziel, R; Besterman, JM MethylGene Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50300447 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50300447&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 45482666 104154808 CHEMBL575482 ZINC45298518 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50535345 CC(C(=O)NO)(c1ccccc1)c1ccccc1 InChI=1S/C15H15NO2/c1-15(14(17)16-18,12-8-4-2-5-9-12)13-10-6-3-7-11-13/h2-11,18H,1H3,(H,16,17) LDAQHFMKFUATRE-UHFFFAOYSA-N 50300448 CHEMBL585365::N-hydroxy-2,2-diphenylpropanamide Histone deacetylase 4 Homo sapiens 4500 ChEMBL 10.1016/j.bmcl.2009.08.010 10.7270/Q2NZ87QH 19699639 Tessier, P; Smil, DV; Wahhab, A; Leit, S; Rahil, J; Li, Z; Deziel, R; Besterman, JM MethylGene Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50300448 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50300448&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 45482660 104154809 CHEMBL585365 ZINC45320948 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50535346 ONC(=O)CC(c1ccccc1)c1ccccc1 InChI=1S/C15H15NO2/c17-15(16-18)11-14(12-7-3-1-4-8-12)13-9-5-2-6-10-13/h1-10,14,18H,11H2,(H,16,17) KJWWMOZTYMOMEU-UHFFFAOYSA-N 50300449 CHEMBL575259::N-hydroxy-3,3-diphenylpropanamide Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.bmcl.2009.08.010 10.7270/Q2NZ87QH 19699639 Tessier, P; Smil, DV; Wahhab, A; Leit, S; Rahil, J; Li, Z; Deziel, R; Besterman, JM MethylGene Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50300449 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50300449&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 13190582 104154810 CHEMBL575259 ZINC41284889 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50535347 ONC(=O)C(Cc1ccccc1)c1ccccc1 InChI=1S/C15H15NO2/c17-15(16-18)14(13-9-5-2-6-10-13)11-12-7-3-1-4-8-12/h1-10,14,18H,11H2,(H,16,17) SZZUTOJFUFBUFD-UHFFFAOYSA-N 50300450 CHEMBL575258::N-hydroxy-2,3-diphenylpropanamide Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.bmcl.2009.08.010 10.7270/Q2NZ87QH 19699639 Tessier, P; Smil, DV; Wahhab, A; Leit, S; Rahil, J; Li, Z; Deziel, R; Besterman, JM MethylGene Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50300450 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50300450&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 45482658 104154811 CHEMBL575258 ZINC45291616 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50535348 CC(C(=O)NO)c1ccccc1 InChI=1S/C9H11NO2/c1-7(9(11)10-12)8-5-3-2-4-6-8/h2-7,12H,1H3,(H,10,11) BRSJAMGWFMNNTO-UHFFFAOYSA-N 50300451 CHEMBL573189::N-hydroxy-2-phenylpropanamide Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.bmcl.2009.08.010 10.7270/Q2NZ87QH 19699639 Tessier, P; Smil, DV; Wahhab, A; Leit, S; Rahil, J; Li, Z; Deziel, R; Besterman, JM MethylGene Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50300451 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50300451&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 9815304 104154812 CHEMBL573189 ZINC45283421 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50535349 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.bmcl.2009.08.010 10.7270/Q2NZ87QH 19699639 Tessier, P; Smil, DV; Wahhab, A; Leit, S; Rahil, J; Li, Z; Deziel, R; Besterman, JM MethylGene Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50535350 Nc1ccccc1NC(=O)c1ccc(CNc2nccc(n2)-c2cccnc2)cc1 InChI=1S/C23H20N6O/c24-19-5-1-2-6-21(19)28-22(30)17-9-7-16(8-10-17)14-27-23-26-13-11-20(29-23)18-4-3-12-25-15-18/h1-13,15H,14,24H2,(H,28,30)(H,26,27,29) HRNLUBSXIHFDHP-UHFFFAOYSA-N 24624 CHEMBL272980::MGCD-0103::MGCD0103::N-(2-aminophenyl)-4-({[4-(pyridin-3-yl)pyrimidin-2-yl]amino}methyl)benzamide::US10227295, Compound MGCD0103::US11377423, MGCD-0103::US9409858, MGCD0103::US9751832, MGCD0103::US9956192, Compound MGCD0103 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.bmcl.2009.08.010 10.7270/Q2NZ87QH 19699639 Tessier, P; Smil, DV; Wahhab, A; Leit, S; Rahil, J; Li, Z; Deziel, R; Besterman, JM MethylGene Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=24624 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=24624&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 9865515 56269575 CHEMBL272980 7008 ZINC13986811 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50535351 OCCN(CCc1c[nH]c2ccccc12)Cc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C22H25N3O3/c26-14-13-25(12-11-19-15-23-21-4-2-1-3-20(19)21)16-18-7-5-17(6-8-18)9-10-22(27)24-28/h1-10,15,23,26,28H,11-14,16H2,(H,24,27)/b10-9+ BWDQBBCUWLSASG-MDZDMXLPSA-N 19428 (2E)-N-hydroxy-3-(4-{[(2-hydroxyethyl)[2-(1H-indol-3-yl)ethyl]amino]methyl}phenyl)prop-2-enamide::(E)-N-hydroxy-3-[4-[[2-hydroxyethyl-[2-(1H-indol-3-yl)ethyl]amino]methyl]phenyl]prop-2-enamide::CHEMBL356066::Dacinostat::LAQ-824::NVP-LAQ824 Histone deacetylase 4 Homo sapiens 500 ChEMBL 10.1016/j.bmcl.2009.08.010 10.7270/Q2NZ87QH 19699639 Tessier, P; Smil, DV; Wahhab, A; Leit, S; Rahil, J; Li, Z; Deziel, R; Besterman, JM MethylGene Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19428 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19428&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6445533 46519450 CHEMBL356066 ZINC01494627 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50535352 ONC(=O)C(c1ccccc1)c1ccccc1 InChI=1S/C14H13NO2/c16-14(15-17)13(11-7-3-1-4-8-11)12-9-5-2-6-10-12/h1-10,13,17H,(H,15,16) OFSBBVCLWMCGNY-UHFFFAOYSA-N 50207561 CHEMBL396097::Class IIa HDAC inhibitor, Compound 6::N-hydroxy-2,2-diphenylacetamide Histone deacetylase 4 Homo sapiens 750 ChEMBL 10.1016/j.bmcl.2009.08.010 10.7270/Q2NZ87QH 19699639 Tessier, P; Smil, DV; Wahhab, A; Leit, S; Rahil, J; Li, Z; Deziel, R; Besterman, JM MethylGene Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50207561 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50207561&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 239512 104084972 CHEMBL396097 ZINC04522248 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50545770 ONC(=O)c1cnc(nc1)N1CCN(CC1)S(=O)(=O)c1ccc2ccccc2c1 InChI=1S/C19H19N5O4S/c25-18(22-26)16-12-20-19(21-13-16)23-7-9-24(10-8-23)29(27,28)17-6-5-14-3-1-2-4-15(14)11-17/h1-6,11-13,26H,7-10H2,(H,22,25) MUTBJZVSRNUIHA-UHFFFAOYSA-N 50304782 CHEMBL609583::N-hydroxy-2-(4-(naphthalen-2-ylsulfonyl)piperazin-1-yl)pyrimidine-5-carboxamide Histone deacetylase 4 Homo sapiens 4.6 ChEMBL 10.1016/j.bmcl.2009.10.118 10.7270/Q2DB81ZS 19906529 Angibaud, P; Van Emelen, K; Decrane, L; van Brandt, S; Ten Holte, P; Pilatte, I; Roux, B; Poncelet, V; Speybrouck, D; Queguiner, L; Gaurrand, S; Marien, A; Floren, W; Janssen, L; Verdonck, M; van Dun, J; van Gompel, J; Gilissen, R; Mackie, C; Du Jardin, M; Peeters, J; Noppe, M; Van Hijfte, L; Freyne, E; Page, M; Janicot, M; Arts, J Ortho-Biotech Oncology Research & Development http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50304782 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50304782&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 10309899 104159143 CHEMBL609583 ZINC03818418 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50545781 OCC(\C=C\c1ccc(F)cc1)N1CCN(CC1)c1ncc(cn1)C(=O)NO InChI=1S/C19H22FN5O3/c20-16-4-1-14(2-5-16)3-6-17(13-26)24-7-9-25(10-8-24)19-21-11-15(12-22-19)18(27)23-28/h1-6,11-12,17,26,28H,7-10,13H2,(H,23,27)/b6-3+ UOEXMKBLKQPTKA-ZZXKWVIFSA-N 50304783 (+)-2-(4-(4-(4-fluorophenyl)-1-hydroxybut-3-en-2-yl)piperazin-1-yl)-N-hydroxypyrimidine-5-carboxamide::(-)-2-(4-(4-(4-fluorophenyl)-1-hydroxybut-3-en-2-yl)piperazin-1-yl)-N-hydroxypyrimidine-5-carboxamide::2-(4-(4-(4-fluorophenyl)-1-hydroxybut-3-en-2-yl)piperazin-1-yl)-N-hydroxypyrimidine-5-carboxamide::CHEMBL594544 Histone deacetylase 4 Homo sapiens 207 ChEMBL 10.1016/j.bmcl.2009.10.118 10.7270/Q2DB81ZS 19906529 Angibaud, P; Van Emelen, K; Decrane, L; van Brandt, S; Ten Holte, P; Pilatte, I; Roux, B; Poncelet, V; Speybrouck, D; Queguiner, L; Gaurrand, S; Marien, A; Floren, W; Janssen, L; Verdonck, M; van Dun, J; van Gompel, J; Gilissen, R; Mackie, C; Du Jardin, M; Peeters, J; Noppe, M; Van Hijfte, L; Freyne, E; Page, M; Janicot, M; Arts, J Ortho-Biotech Oncology Research & Development http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50304783 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50304783&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11682502 104159144 CHEMBL594544 ZINC38238840 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50540861 Cc1ccc(OCCN(Cc2ccc(cc2)C(=O)NO)c2ncc(s2)-c2ccc(C)cc2)cc1 InChI=1S/C27H27N3O3S/c1-19-3-9-22(10-4-19)25-17-28-27(34-25)30(15-16-33-24-13-5-20(2)6-14-24)18-21-7-11-23(12-8-21)26(31)29-32/h3-14,17,32H,15-16,18H2,1-2H3,(H,29,31) ZURLFGLAIMUBQN-UHFFFAOYSA-N 50302945 CHEMBL584273::N-hydroxy-4-(((2-(p-tolyloxy)ethyl)(5-p-tolylthiazol-2-yl)amino)methyl)benzamide Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2009.09.100 10.7270/Q21J99TB 19822426 Su, H; Yu, L; Nebbioso, A; Carafa, V; Chen, Y; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50302945 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50302945&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 45102721 104157306 CHEMBL584273 ZINC45315314 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50540863 Cc1ccc(cc1)-c1cnc(s1)N(CCOc1ccccc1)Cc1ccc(cc1)C(=O)NO InChI=1S/C26H25N3O3S/c1-19-7-11-21(12-8-19)24-17-27-26(33-24)29(15-16-32-23-5-3-2-4-6-23)18-20-9-13-22(14-10-20)25(30)28-31/h2-14,17,31H,15-16,18H2,1H3,(H,28,30) TYUFMBOHNCOHNX-UHFFFAOYSA-N 50302946 CHEMBL586040::N-hydroxy-4-(((2-phenoxyethyl)(5-p-tolylthiazol-2-yl)amino)methyl)benzamide Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2009.09.100 10.7270/Q21J99TB 19822426 Su, H; Yu, L; Nebbioso, A; Carafa, V; Chen, Y; Altucci, L; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50302946 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50302946&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 45102716 104157307 CHEMBL586040 ZINC45324385 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50557069 CC(C=CC(=O)NO)C=C(C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20) ALCVRKZFLFWUAZ-UHFFFAOYSA-N 19130 (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide::CHEMBL99::TSA::Trichostatin A (TSA) Histone deacetylase 4 Homo sapiens 44 ChEMBL 10.1016/j.bmcl.2009.12.054 10.7270/Q2BC3ZNR 20045316 Islam, NM; Kato, T; Nishino, N; Kim, HJ; Ito, A; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19130 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19130&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 91895926 46519165 46024 CHEMBL99 7005 ZINC05579377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50557070 ONC(=O)CCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@@H]2CCCCCCCCC[C@@H](NC1=O)C(=O)N2 InChI=1S/C26H43N5O6/c32-22(30-37)16-10-6-9-13-19-23(33)27-18-12-7-4-2-1-3-5-8-14-20(29-24(18)34)26(36)31-17-11-15-21(31)25(35)28-19/h18-21,37H,1-17H2,(H,27,33)(H,28,35)(H,29,34)(H,30,32)/t18-,19+,20+,21-/m1/s1 QGARLIKKHCLNGY-IVAOSVALSA-N 50309929 6-((1S,7R,10S,13R)-2,8,11,24-Tetraoxo-3,9,12,23-tetraaza-tricyclo[11.9.2.0*3,7*]tetracos-10-yl)-hexanoic acid hydroxyamide::CHEMBL598363 Histone deacetylase 4 Homo sapiens 5.4 ChEMBL 10.1016/j.bmcl.2009.12.054 10.7270/Q2BC3ZNR 20045316 Islam, NM; Kato, T; Nishino, N; Kim, HJ; Ito, A; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50309929 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50309929&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 46216758 104164290 CHEMBL598363 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50557071 ONC(=O)CCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@@H]2CCCCCCCCCC[C@@H](NC1=O)C(=O)N2 InChI=1S/C27H45N5O6/c33-23(31-38)17-11-7-10-14-20-24(34)28-19-13-8-5-3-1-2-4-6-9-15-21(30-25(19)35)27(37)32-18-12-16-22(32)26(36)29-20/h19-22,38H,1-18H2,(H,28,34)(H,29,36)(H,30,35)(H,31,33)/t19-,20+,21+,22-/m1/s1 BVYNKHHGAJSMBT-CLAROIROSA-N 50309930 6-((1S,7R,10S,13R)-2,8,11,25-Tetraoxo-3,9,12,24-tetraaza-tricyclo[11.10.2.0*3,7*]pentacos-10-yl)-hexanoic acid hydroxyamide::CHEMBL592719 Histone deacetylase 4 Homo sapiens 5.5 ChEMBL 10.1016/j.bmcl.2009.12.054 10.7270/Q2BC3ZNR 20045316 Islam, NM; Kato, T; Nishino, N; Kim, HJ; Ito, A; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50309930 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50309930&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 46216759 104164291 CHEMBL592719 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50557072 ONC(=O)CCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@@H]2CCCCCCCCCCC[C@@H](NC1=O)C(=O)N2 InChI=1S/C28H47N5O6/c34-24(32-39)18-12-8-11-15-21-25(35)29-20-14-9-6-4-2-1-3-5-7-10-16-22(31-26(20)36)28(38)33-19-13-17-23(33)27(37)30-21/h20-23,39H,1-19H2,(H,29,35)(H,30,37)(H,31,36)(H,32,34)/t20-,21+,22+,23-/m1/s1 TVNZWPOEHUTSFV-WZYRSQIMSA-N 50309931 6-((1S,7R,10S,13R)-2,8,11,26-Tetraoxo-3,9,12,25-tetraaza-tricyclo[11.11.2.0*3,7*]hexacos-10-yl)-hexanoic acid hydroxyamide::CHEMBL589311 Histone deacetylase 4 Homo sapiens 4.5 ChEMBL 10.1016/j.bmcl.2009.12.054 10.7270/Q2BC3ZNR 20045316 Islam, NM; Kato, T; Nishino, N; Kim, HJ; Ito, A; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50309931 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50309931&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 46216760 104164292 CHEMBL589311 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50557073 ONC(=O)CCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@@H]2CCCCCCCCCCCC[C@@H](NC1=O)C(=O)N2 InChI=1S/C29H49N5O6/c35-25(33-40)19-13-9-12-16-22-26(36)30-21-15-10-7-5-3-1-2-4-6-8-11-17-23(32-27(21)37)29(39)34-20-14-18-24(34)28(38)31-22/h21-24,40H,1-20H2,(H,30,36)(H,31,38)(H,32,37)(H,33,35)/t21-,22+,23+,24-/m1/s1 WJKLHHHHJUCBTH-NAVOZUGXSA-N 50309932 6-((1R,14S,20R,23S)-15,21,24,26-Tetraoxo-16,22,25,27-tetraaza-tricyclo[12.11.2.0*16,20*]heptacos-23-yl)-hexanoic acid hydroxyamide::CHEMBL589918 Histone deacetylase 4 Homo sapiens 5 ChEMBL 10.1016/j.bmcl.2009.12.054 10.7270/Q2BC3ZNR 20045316 Islam, NM; Kato, T; Nishino, N; Kim, HJ; Ito, A; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50309932 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50309932&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 46216772 104164293 CHEMBL589918 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50557074 CCCCC[C@H]1NC(=O)[C@H](CCCCCC(=O)NO)NC(=O)[C@H]2CCCN2C(=O)[C@H](CCCCC)NC1=O InChI=1S/C27H47N5O6/c1-3-5-8-13-19-25(35)30-21(15-9-6-4-2)27(37)32-18-12-16-22(32)26(36)29-20(24(34)28-19)14-10-7-11-17-23(33)31-38/h19-22,38H,3-18H2,1-2H3,(H,28,34)(H,29,36)(H,30,35)(H,31,33)/t19-,20+,21+,22-/m1/s1 IYOLVIFIJXUYFW-CLAROIROSA-N 50309933 6-((5S,8R,11S,13aR)-4,7,10,13-Tetraoxo-5,8-dipentyl-tetradecahydro-3a,6,9,12-tetraaza-cyclopentacyclododecen-11-yl)-hexanoic acid hydroxyamide::CHEMBL589906 Histone deacetylase 4 Homo sapiens 12 ChEMBL 10.1016/j.bmcl.2009.12.054 10.7270/Q2BC3ZNR 20045316 Islam, NM; Kato, T; Nishino, N; Kim, HJ; Ito, A; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50309933 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50309933&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 46230638 104164294 CHEMBL589906 ZINC49746063 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50575300 ONC(=O)CCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC(=O)[C@H](Cc2c[nH]c3ccccc23)NC1=O InChI=1S/C33H40N6O6/c40-29(38-45)16-6-2-5-14-25-30(41)36-26(19-22-20-34-24-13-8-7-12-23(22)24)31(42)37-27(18-21-10-3-1-4-11-21)33(44)39-17-9-15-28(39)32(43)35-25/h1,3-4,7-8,10-13,20,25-28,34,45H,2,5-6,9,14-19H2,(H,35,43)(H,36,41)(H,37,42)(H,38,40)/t25-,26-,27-,28+/m0/s1 OHPVTQHZRUJEEL-LAJGZZDBSA-N 50317649 6-((3S,6S,9S,14aR)-6-((1H-indol-3-yl)methyl)-9-benzyl-1,4,7,10-tetraoxotetradecahydropyrrolo[1,2-a][1,4,7,10]tetraazacyclododecin-3-yl)-N-hydroxyhexanamide::CHEMBL1096985 Histone deacetylase 4 Homo sapiens 9600 ChEMBL 10.1016/j.bmc.2010.03.022 10.7270/Q2BC3ZP6 20381359 Terracciano, S; Di Micco, S; Bifulco, G; Gallinari, P; Riccio, R; Bruno, I Universit£ degli Studi di Salerno http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50317649 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50317649&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 46861822 104152010 CHEMBL1096985 ZINC49783822 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50575304 ONC(=O)CCCCC[C@@H]1NC(=O)[C@H](Cc2c[nH]c3ccccc23)NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2c[nH]c3ccccc23)NC1=O InChI=1S/C35H41N7O6/c43-31(41-48)15-3-1-2-13-27-32(44)40-29(18-22-20-37-26-12-7-5-10-24(22)26)35(47)42-16-8-14-30(42)34(46)39-28(33(45)38-27)17-21-19-36-25-11-6-4-9-23(21)25/h4-7,9-12,19-20,27-30,36-37,48H,1-3,8,13-18H2,(H,38,45)(H,39,46)(H,40,44)(H,41,43)/t27-,28-,29-,30+/m0/s1 DAMGSDKDFKQTGM-GCXHJFECSA-N 50317650 6-((3S,6S,9S,14aR)-3,9-bis((1H-indol-3-yl)methyl)-1,4,7,10-tetraoxotetradecahydropyrrolo[1,2-a][1,4,7,10]tetraazacyclododecin-6-yl)-N-hydroxyhexanamide::CHEMBL1096986 Histone deacetylase 4 Homo sapiens 10650 ChEMBL 10.1016/j.bmc.2010.03.022 10.7270/Q2BC3ZP6 20381359 Terracciano, S; Di Micco, S; Bifulco, G; Gallinari, P; Riccio, R; Bruno, I Universit£ degli Studi di Salerno http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50317650 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50317650&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 46861823 104152011 CHEMBL1096986 ZINC49784883 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50568065 CC(C)(C)c1[nH]c2ccccc2c1[C@H]1CCCN(Cc2ccc(\C=C\C(=O)NO)cc2F)C1 InChI=1S/C27H32FN3O2/c1-27(2,3)26-25(21-8-4-5-9-23(21)29-26)20-7-6-14-31(17-20)16-19-12-10-18(15-22(19)28)11-13-24(32)30-33/h4-5,8-13,15,20,29,33H,6-7,14,16-17H2,1-3H3,(H,30,32)/b13-11+/t20-/m0/s1 ILQPFWGPYWQTHJ-RPAADVPWSA-N 50314642 (E)-3-{4-[(R)-3-(2-tert-Butyl-1H-indol-3-yl)piperidin-1-ylmethyl]-3-fluorophenyl}-N-hydroxyacrylamide::CHEMBL1093033 Histone deacetylase 4 Homo sapiens 28 ChEMBL 10.1021/jm100007m 10.7270/Q20V8CZC 20205394 Cho, YS; Whitehead, L; Li, J; Chen, CH; Jiang, L; Vogtle, M; Francotte, E; Richert, P; Wagner, T; Traebert, M; Lu, Q; Cao, X; Dumotier, B; Fejzo, J; Rajan, S; Wang, P; Yan-Neale, Y; Shao, W; Atadja, P; Shultz, M Novartis Institutes for BioMedical Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50314642 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50314642&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 46197798 104149003 CHEMBL1093033 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50568066 CC(C)(C)c1[nH]c2ccccc2c1[C@@H]1CCCN(Cc2ccc(\C=C\C(=O)NO)cc2F)C1 InChI=1S/C27H32FN3O2/c1-27(2,3)26-25(21-8-4-5-9-23(21)29-26)20-7-6-14-31(17-20)16-19-12-10-18(15-22(19)28)11-13-24(32)30-33/h4-5,8-13,15,20,29,33H,6-7,14,16-17H2,1-3H3,(H,30,32)/b13-11+/t20-/m1/s1 ILQPFWGPYWQTHJ-VSFZPWCASA-N 50314643 (E)-3-{4-[(S)-3-(2-tert-Butyl-1H-indol-3-yl)piperidin-1-ylmethyl]-3-fluorophenyl}-N-hydroxyacrylamide::CHEMBL1093335 Histone deacetylase 4 Homo sapiens 38 ChEMBL 10.1021/jm100007m 10.7270/Q20V8CZC 20205394 Cho, YS; Whitehead, L; Li, J; Chen, CH; Jiang, L; Vogtle, M; Francotte, E; Richert, P; Wagner, T; Traebert, M; Lu, Q; Cao, X; Dumotier, B; Fejzo, J; Rajan, S; Wang, P; Yan-Neale, Y; Shao, W; Atadja, P; Shultz, M Novartis Institutes for BioMedical Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50314643 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50314643&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 46197799 104149004 CHEMBL1093335 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50578957 ONC(=O)CCCCCNC(=O)NC(=O)c1ccccc1 InChI=1S/C14H19N3O4/c18-12(17-21)9-5-2-6-10-15-14(20)16-13(19)11-7-3-1-4-8-11/h1,3-4,7-8,21H,2,5-6,9-10H2,(H,17,18)(H2,15,16,19,20) VQLQZMGNGMOMPU-UHFFFAOYSA-N 50319235 6-(3-Benzoyl-ureido)-hexanoic acid hydroxyamide::CHEMBL1083439 Histone deacetylase 4 Homo sapiens 20 ChEMBL 10.1016/j.bmcl.2010.04.041 10.7270/Q2GT5NCX 20451378 Wang, H; Lim, ZY; Zhou, Y; Ng, M; Lu, T; Lee, K; Sangthongpitag, K; Goh, KC; Wang, X; Wu, X; Khng, HH; Goh, SK; Ong, WC; Bonday, Z; Sun, ET S*BIO Pte Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50319235 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50319235&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11449246 104153596 CHEMBL1083439 ZINC43152345 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50578958 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 16 ChEMBL 10.1016/j.bmcl.2010.04.041 10.7270/Q2GT5NCX 20451378 Wang, H; Lim, ZY; Zhou, Y; Ng, M; Lu, T; Lee, K; Sangthongpitag, K; Goh, KC; Wang, X; Wu, X; Khng, HH; Goh, SK; Ong, WC; Bonday, Z; Sun, ET S*BIO Pte Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50578959 ONC(=O)CCCCCNC(=O)NC(=O)c1ccc(Br)cc1 InChI=1S/C14H18BrN3O4/c15-11-7-5-10(6-8-11)13(20)17-14(21)16-9-3-1-2-4-12(19)18-22/h5-8,22H,1-4,9H2,(H,18,19)(H2,16,17,20,21) RVWKGSCHYRXCNC-UHFFFAOYSA-N 50319209 6-[3-(4-Bromo-benzoyl)-ureido]-hexanoic acid hydroxyamide::CHEMBL1083086 Histone deacetylase 4 Homo sapiens 6 ChEMBL 10.1016/j.bmcl.2010.04.041 10.7270/Q2GT5NCX 20451378 Wang, H; Lim, ZY; Zhou, Y; Ng, M; Lu, T; Lee, K; Sangthongpitag, K; Goh, KC; Wang, X; Wu, X; Khng, HH; Goh, SK; Ong, WC; Bonday, Z; Sun, ET S*BIO Pte Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50319209 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50319209&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 46890583 104153570 CHEMBL1083086 ZINC49034920 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50585664 CCCCCCCC(=O)SCC\C=C\[C@@H]1CC(=O)NCc2nc(cs2)-c2nc(cs2)C(=O)N[C@@H](C(C)C)C(=O)O1 InChI=1S/C28H38N4O5S3/c1-4-5-6-7-8-12-24(34)38-13-10-9-11-19-14-22(33)29-15-23-30-21(17-39-23)27-31-20(16-40-27)26(35)32-25(18(2)3)28(36)37-19/h9,11,16-19,25H,4-8,10,12-15H2,1-3H3,(H,29,33)(H,32,35)/b11-9+/t19-,25+/m1/s1 XWGHGIMKSBEUMD-SLQHSKKLSA-N 50322418 CHEMBL1173195::Octanethioic acid S-[(E)-4-((8S,11S)-8-isopropyl-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraaza-tricyclo[14.2.1.1*2,5*]icosa-1(18),2(20),4,16(19)-tetraen-11-yl)-but-3-enyl]ester Histone deacetylase 4 Homo sapiens 3000 ChEMBL 10.1021/jm100244y 10.7270/Q2WD40R6 20491440 Souto, JA; Vaz, E; Lepore, I; Poppler, AC; Franci, G; Alvarez, R; Altucci, L; de Lera, AR Universidade de Vigo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50322418 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50322418&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44551271 104143947 CHEMBL1173195 C05752 ZINC53242980 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50585665 CCCCCCCC(=O)SCC\C=C\[C@@H]1CC(=O)NCc2nc(cs2)C2=N[C@@](Cc3ccccc3)(CS2)C(=O)N[C@@H](C(C)C)C(=O)O1 InChI=1S/C35H46N4O5S3/c1-4-5-6-7-11-17-30(41)45-18-13-12-16-26-19-28(40)36-21-29-37-27(22-46-29)32-39-35(23-47-32,20-25-14-9-8-10-15-25)34(43)38-31(24(2)3)33(42)44-26/h8-10,12,14-16,22,24,26,31H,4-7,11,13,17-21,23H2,1-3H3,(H,36,40)(H,38,43)/b16-12+/t26-,31+,35+/m1/s1 VRSPHWOZMHPVOQ-BWBAVGLMSA-N 50322419 CHEMBL1171466::Octanethioic acid S-[(E)-4-((5R,8S,11S)-5-benzyl-8-isopropyl-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraaza-tricyclo[14.2.1.1*2,5*]icosa-1(18),2(20),16(19)-trien-11-yl)-but-3-enyl]ester Histone deacetylase 4 Homo sapiens 3000 ChEMBL 10.1021/jm100244y 10.7270/Q2WD40R6 20491440 Souto, JA; Vaz, E; Lepore, I; Poppler, AC; Franci, G; Alvarez, R; Altucci, L; de Lera, AR Universidade de Vigo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50322419 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50322419&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 46838752 104143948 CHEMBL1171466 C05752 ZINC96171959 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50585666 CCCCCCCC(=O)SCC\C=C\[C@@H]1CC(=O)NCc2nc(cs2)C2=N[C@@](CC)(CS2)C(=O)N[C@@H](C(C)C)C(=O)O1 InChI=1S/C30H44N4O5S3/c1-5-7-8-9-10-14-25(36)40-15-12-11-13-21-16-23(35)31-17-24-32-22(18-41-24)27-34-30(6-2,19-42-27)29(38)33-26(20(3)4)28(37)39-21/h11,13,18,20-21,26H,5-10,12,14-17,19H2,1-4H3,(H,31,35)(H,33,38)/b13-11+/t21-,26+,30+/m1/s1 JCEIHOKCTXCFBI-SJQSDZARSA-N 50322420 CHEMBL1171465::Octanethioic acid S-[(E)-4-((5R,8S,11S)-5-ethyl-8-isopropyl-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraaza-tricyclo[14.2.1.1*2,5*]icosa-1(18),2(20),16(19)-trien-11-yl)-but-3-enyl]ester Histone deacetylase 4 Homo sapiens 4900 ChEMBL 10.1021/jm100244y 10.7270/Q2WD40R6 20491440 Souto, JA; Vaz, E; Lepore, I; Poppler, AC; Franci, G; Alvarez, R; Altucci, L; de Lera, AR Universidade de Vigo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50322420 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50322420&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 46838751 104143949 CHEMBL1171465 C05752 ZINC70672917 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50585667 CCCCCCCC(=O)SCC\C=C\[C@@H]1CC(=O)NCc2nc(cs2)C2=N[C@@H](CS2)C(=O)N[C@@H](C(C)C)C(=O)O1 InChI=1S/C28H40N4O5S3/c1-4-5-6-7-8-12-24(34)38-13-10-9-11-19-14-22(33)29-15-23-30-21(17-39-23)27-31-20(16-40-27)26(35)32-25(18(2)3)28(36)37-19/h9,11,17-20,25H,4-8,10,12-16H2,1-3H3,(H,29,33)(H,32,35)/b11-9+/t19-,20+,25+/m1/s1 UKQJPLUKKMJSIY-WVNXAOKXSA-N 50322421 CHEMBL1173194::Octanethioic acid S-[(E)-4-((5R,8S,11S)-8-isopropyl-6,9,13-trioxo-10-oxa-3,17-dithia-7,14,19,20-tetraaza-tricyclo[14.2.1.1*2,5*]icosa-1(18),2(20),16(19)-trien-11-yl)-but-3-enyl]ester Histone deacetylase 4 Homo sapiens 7500 ChEMBL 10.1021/jm100244y 10.7270/Q2WD40R6 20491440 Souto, JA; Vaz, E; Lepore, I; Poppler, AC; Franci, G; Alvarez, R; Altucci, L; de Lera, AR Universidade de Vigo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50322421 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50322421&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 49799582 104143950 CHEMBL1173194 C05752 ZINC56861393 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50585668 CCCCCCCC(=O)SCC\C=C\[C@@H]1CC(=O)NCc2nc(cs2)C2=N[C@@](C)(CS2)C(=O)N[C@@H](C(C)C)C(=O)O1 InChI=1S/C29H42N4O5S3/c1-5-6-7-8-9-13-24(35)39-14-11-10-12-20-15-22(34)30-16-23-31-21(17-40-23)26-33-29(4,18-41-26)28(37)32-25(19(2)3)27(36)38-20/h10,12,17,19-20,25H,5-9,11,13-16,18H2,1-4H3,(H,30,34)(H,32,37)/b12-10+/t20-,25+,29+/m1/s1 AXESYCSCGBQJBL-SZPBEECKSA-N 50322422 CHEMBL1173445::Largazole Histone deacetylase 4 Homo sapiens 3000 ChEMBL 10.1021/jm100244y 10.7270/Q2WD40R6 20491440 Souto, JA; Vaz, E; Lepore, I; Poppler, AC; Franci, G; Alvarez, R; Altucci, L; de Lera, AR Universidade de Vigo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50322422 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50322422&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 24757913 104143951 CHEMBL1173445 C05752 ZINC56861395 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50585669 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 6200 ChEMBL 10.1021/jm100244y 10.7270/Q2WD40R6 20491440 Souto, JA; Vaz, E; Lepore, I; Poppler, AC; Franci, G; Alvarez, R; Altucci, L; de Lera, AR Universidade de Vigo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50603696 CC(C=CC(=O)NO)C=C(C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20) ALCVRKZFLFWUAZ-UHFFFAOYSA-N 19130 (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide::CHEMBL99::TSA::Trichostatin A (TSA) Histone deacetylase 4 Homo sapiens 8 ChEMBL 10.1038/nchembio.275 10.7270/Q2FF3SKD 19966789 Hutt, DM; Herman, D; Rodrigues, AP; Noel, S; Pilewski, JM; Matteson, J; Hoch, B; Kellner, W; Kelly, JW; Schmidt, A; Thomas, PJ; Matsumura, Y; Skach, WR; Gentzsch, M; Riordan, JR; Sorscher, EJ; Okiyoneda, T; Yates, JR; Lukacs, GL; Frizzell, RA; Manning, G; Gottesfeld, JM; Balch, WE The Scripps Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19130 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19130&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 91895926 46519165 46024 CHEMBL99 7005 ZINC05579377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50603697 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 300 ChEMBL 10.1038/nchembio.275 10.7270/Q2FF3SKD 19966789 Hutt, DM; Herman, D; Rodrigues, AP; Noel, S; Pilewski, JM; Matteson, J; Hoch, B; Kellner, W; Kelly, JW; Schmidt, A; Thomas, PJ; Matsumura, Y; Skach, WR; Gentzsch, M; Riordan, JR; Sorscher, EJ; Okiyoneda, T; Yates, JR; Lukacs, GL; Frizzell, RA; Manning, G; Gottesfeld, JM; Balch, WE The Scripps Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50603698 ONC(=O)CCCCCN1C(=O)c2cccc3cccc(C1=O)c23 InChI=1S/C18H18N2O4/c21-15(19-24)10-2-1-3-11-20-17(22)13-8-4-6-12-7-5-9-14(16(12)13)18(20)23/h4-9,24H,1-3,10-11H2,(H,19,21) JTDYUFSDZATMKU-UHFFFAOYSA-N 50328678 6-(1,3-Dioxo-1H,3H-benzo[de]isoquinolin-2-yl)-hexanoic acid hydroxyamide::6-(1,3-dioxo-1H-benzo[de]isoquinolin-2(3H)-yl)-N-hydroxyhexanamide::CHEMBL96051::GNF-Pf-2024::Scriptaid::Scriptaid, 9 Histone deacetylase 4 Homo sapiens 300 ChEMBL 10.1038/nchembio.275 10.7270/Q2FF3SKD 19966789 Hutt, DM; Herman, D; Rodrigues, AP; Noel, S; Pilewski, JM; Matteson, J; Hoch, B; Kellner, W; Kelly, JW; Schmidt, A; Thomas, PJ; Matsumura, Y; Skach, WR; Gentzsch, M; Riordan, JR; Sorscher, EJ; Okiyoneda, T; Yates, JR; Lukacs, GL; Frizzell, RA; Manning, G; Gottesfeld, JM; Balch, WE The Scripps Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50328678 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50328678&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5186 123107793 CHEMBL96051 ZINC03873638 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50603699 Nc1ccccc1NC(=O)c1ccc(CNC(=O)OCc2cccnc2)cc1 InChI=1S/C21H20N4O3/c22-18-5-1-2-6-19(18)25-20(26)17-9-7-15(8-10-17)13-24-21(27)28-14-16-4-3-11-23-12-16/h1-12H,13-14,22H2,(H,24,27)(H,25,26) INVTYAOGFAGBOE-UHFFFAOYSA-N 19410 CHEMBL27759::MS-275::US11377423, MS-275::US11672788, Compound Entinostat::US9265734, MS-275::US9796664, Compound MS-275::benzamide-type inhibitor, 3::pyridin-3-ylmethyl N-({4-[(2-aminophenyl)carbamoyl]phenyl}methyl)carbamate Histone deacetylase 4 Homo sapiens 48700 ChEMBL 10.1038/nchembio.275 10.7270/Q2FF3SKD 19966789 Hutt, DM; Herman, D; Rodrigues, AP; Noel, S; Pilewski, JM; Matteson, J; Hoch, B; Kellner, W; Kelly, JW; Schmidt, A; Thomas, PJ; Matsumura, Y; Skach, WR; Gentzsch, M; Riordan, JR; Sorscher, EJ; Okiyoneda, T; Yates, JR; Lukacs, GL; Frizzell, RA; Manning, G; Gottesfeld, JM; Balch, WE The Scripps Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19410 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19410&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4261 46519433 CHEMBL27759 7007 ZINC01488870 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50621882 CC(C=CC(=O)NO)C=C(C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20) ALCVRKZFLFWUAZ-UHFFFAOYSA-N 19130 (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide::CHEMBL99::TSA::Trichostatin A (TSA) Histone deacetylase 4 Homo sapiens 7690 ChEMBL 10.1016/j.bmcl.2010.12.079 10.7270/Q28K79C8 21256006 Choi, E; Lee, C; Park, JE; Seo, JJ; Cho, M; Kang, JS; Kim, HM; Park, SK; Lee, K; Han, G Yonsei University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19130 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19130&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 91895926 46519165 46024 CHEMBL99 7005 ZINC05579377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50613721 CC(C=CC(=O)NO)C=C(C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20) ALCVRKZFLFWUAZ-UHFFFAOYSA-N 19130 (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide::CHEMBL99::TSA::Trichostatin A (TSA) Histone deacetylase 4 Homo sapiens 12 ChEMBL 10.1021/jm101092u 10.7270/Q28G8KZJ 21073160 Auzzas, L; Larsson, A; Matera, R; Baraldi, A; Deschênes-Simard, B; Giannini, G; Cabri, W; Battistuzzi, G; Gallo, G; Ciacci, A; Vesci, L; Pisano, C TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19130 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19130&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 91895926 46519165 46024 CHEMBL99 7005 ZINC05579377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50613722 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 493 ChEMBL 10.1021/jm101092u 10.7270/Q28G8KZJ 21073160 Auzzas, L; Larsson, A; Matera, R; Baraldi, A; Deschênes-Simard, B; Giannini, G; Cabri, W; Battistuzzi, G; Gallo, G; Ciacci, A; Vesci, L; Pisano, C TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50613723 OCCN(CCc1c[nH]c2ccccc12)Cc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C22H25N3O3/c26-14-13-25(12-11-19-15-23-21-4-2-1-3-20(19)21)16-18-7-5-17(6-8-18)9-10-22(27)24-28/h1-10,15,23,26,28H,11-14,16H2,(H,24,27)/b10-9+ BWDQBBCUWLSASG-MDZDMXLPSA-N 19428 (2E)-N-hydroxy-3-(4-{[(2-hydroxyethyl)[2-(1H-indol-3-yl)ethyl]amino]methyl}phenyl)prop-2-enamide::(E)-N-hydroxy-3-[4-[[2-hydroxyethyl-[2-(1H-indol-3-yl)ethyl]amino]methyl]phenyl]prop-2-enamide::CHEMBL356066::Dacinostat::LAQ-824::NVP-LAQ824 Histone deacetylase 4 Homo sapiens 5.8 ChEMBL 10.1021/jm101092u 10.7270/Q28G8KZJ 21073160 Auzzas, L; Larsson, A; Matera, R; Baraldi, A; Deschênes-Simard, B; Giannini, G; Cabri, W; Battistuzzi, G; Gallo, G; Ciacci, A; Vesci, L; Pisano, C TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19428 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19428&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6445533 46519450 CHEMBL356066 ZINC01494627 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50613724 COc1ccc(COC(CCCCCC(=O)NO)C(=O)Nc2ccccc2)cc1 InChI=1S/C22H28N2O5/c1-28-19-14-12-17(13-15-19)16-29-20(10-6-3-7-11-21(25)24-27)22(26)23-18-8-4-2-5-9-18/h2,4-5,8-9,12-15,20,27H,3,6-7,10-11,16H2,1H3,(H,23,26)(H,24,25) FQAZXPMITHVSOG-UHFFFAOYSA-N 50333091 (R/S)-N8-hydroxy-2-(4-methoxybenzyloxy)-N1-phenyloctanediamide::2-(4-methoxybenzyloxy)-N8-hydroxy-N1-phenyloctanediamide::CHEMBL251011 Histone deacetylase 4 Homo sapiens 648 ChEMBL 10.1021/jm101092u 10.7270/Q28G8KZJ 21073160 Auzzas, L; Larsson, A; Matera, R; Baraldi, A; Deschênes-Simard, B; Giannini, G; Cabri, W; Battistuzzi, G; Gallo, G; Ciacci, A; Vesci, L; Pisano, C TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50333091 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50333091&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 24779722 125083193 CHEMBL251011 ZINC28956683 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50613725 ONC(=O)CCCCCC1OCCCCCOc2ccccc2NC1=O InChI=1S/C19H28N2O5/c22-18(21-24)12-4-1-3-11-17-19(23)20-15-9-5-6-10-16(15)25-13-7-2-8-14-26-17/h5-6,9-10,17,24H,1-4,7-8,11-14H2,(H,20,23)(H,21,22) LOHSCPHJUJZDDV-UHFFFAOYSA-N 50333092 (R/S)-6-(6-Oxo-6,7,9,10,11,12-hexahydro-5H-8,13-dioxa-5-azabenzocycloundecen-7-yl)hexanoic acid hydroxyamide::CHEMBL1631910 Histone deacetylase 4 Homo sapiens 2580 ChEMBL 10.1021/jm101092u 10.7270/Q28G8KZJ 21073160 Auzzas, L; Larsson, A; Matera, R; Baraldi, A; Deschênes-Simard, B; Giannini, G; Cabri, W; Battistuzzi, G; Gallo, G; Ciacci, A; Vesci, L; Pisano, C TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50333092 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50333092&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25066355 125083194 CHEMBL1631910 ZINC66263911 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50613726 ONC(=O)CCCCCC1OCCCCCCOc2ccccc2NC1=O InChI=1S/C20H30N2O5/c23-19(22-25)13-5-3-4-12-18-20(24)21-16-10-6-7-11-17(16)26-14-8-1-2-9-15-27-18/h6-7,10-11,18,25H,1-5,8-9,12-15H2,(H,21,24)(H,22,23) WCTLKUHJSQSAOJ-UHFFFAOYSA-N 50333085 (R/S)-6-(6-Oxo-6,7,10,11,12,13-hexahydro-5H,9H-8,14-dioxa-5-azabenzocyclododecen-7-yl)hexanoic acid hydroxyamide::CHEMBL1631911 Histone deacetylase 4 Homo sapiens 1200 ChEMBL 10.1021/jm101092u 10.7270/Q28G8KZJ 21073160 Auzzas, L; Larsson, A; Matera, R; Baraldi, A; Deschênes-Simard, B; Giannini, G; Cabri, W; Battistuzzi, G; Gallo, G; Ciacci, A; Vesci, L; Pisano, C TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50333085 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50333085&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25066356 125083187 CHEMBL1631911 ZINC66251115 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50613727 ONC(=O)CCCCCC1OCCCCCCCOc2ccccc2NC1=O InChI=1S/C21H32N2O5/c24-20(23-26)14-6-4-5-13-19-21(25)22-17-11-7-8-12-18(17)27-15-9-2-1-3-10-16-28-19/h7-8,11-12,19,26H,1-6,9-10,13-16H2,(H,22,25)(H,23,24) HONLBMJVWSMASP-UHFFFAOYSA-N 50333086 (R/S)-6-(6-Oxo-6,7,9,10,11,12,13,14-octahydro-5H-8,15-dioxa-5-azabenzocyclotridecen-7-yl)hexanoic acid hydroxyamide::CHEMBL1631912 Histone deacetylase 4 Homo sapiens 1250 ChEMBL 10.1021/jm101092u 10.7270/Q28G8KZJ 21073160 Auzzas, L; Larsson, A; Matera, R; Baraldi, A; Deschênes-Simard, B; Giannini, G; Cabri, W; Battistuzzi, G; Gallo, G; Ciacci, A; Vesci, L; Pisano, C TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50333086 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50333086&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25066547 125083188 CHEMBL1631912 ZINC66251117 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50613728 COc1cc2COc3ccccc3NC(=O)C(CCCCCC(=O)NO)OC\C=C/c(c2)c1 InChI=1S/C25H30N2O6/c1-31-20-15-18-8-7-13-32-23(11-3-2-4-12-24(28)27-30)25(29)26-21-9-5-6-10-22(21)33-17-19(14-18)16-20/h5-10,14-16,23,30H,2-4,11-13,17H2,1H3,(H,26,29)(H,27,28)/b8-7- LMOIMHSPFQECJG-FPLPWBNLSA-N 50333087 (R/S)-6-(19-Methoxy-11-oxo-3,13-dioxa-10-azatricyclo[15.3.1.04,9]henicosa-1(21),4(9),5,7,15,17,19-heptaen-12-yl)hexanoic acid hydroxyamide::CHEMBL1631913 Histone deacetylase 4 Homo sapiens 159 ChEMBL 10.1021/jm101092u 10.7270/Q28G8KZJ 21073160 Auzzas, L; Larsson, A; Matera, R; Baraldi, A; Deschênes-Simard, B; Giannini, G; Cabri, W; Battistuzzi, G; Gallo, G; Ciacci, A; Vesci, L; Pisano, C TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50333087 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50333087&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25066548 125083189 CHEMBL1631913 ZINC59151448 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50613729 COc1cc2COc3ccccc3NC(=O)[C@H](CCCCCC(=O)NO)OC\C=C/c(c2)c1 InChI=1S/C25H30N2O6/c1-31-20-15-18-8-7-13-32-23(11-3-2-4-12-24(28)27-30)25(29)26-21-9-5-6-10-22(21)33-17-19(14-18)16-20/h5-10,14-16,23,30H,2-4,11-13,17H2,1H3,(H,26,29)(H,27,28)/b8-7-/t23-/m0/s1 LMOIMHSPFQECJG-YLNCNTMDSA-N 50333088 (S)-6-(19-Methoxy-11-oxo-3,13-dioxa-10-azatricyclo[15.3.1.04,9] henicosa-1(21),4(9),5,7,15,17,19-heptaen-12-yl)hexanoic acid hydroxyamide::CHEMBL1631914 Histone deacetylase 4 Homo sapiens 79 ChEMBL 10.1021/jm101092u 10.7270/Q28G8KZJ 21073160 Auzzas, L; Larsson, A; Matera, R; Baraldi, A; Deschênes-Simard, B; Giannini, G; Cabri, W; Battistuzzi, G; Gallo, G; Ciacci, A; Vesci, L; Pisano, C TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50333088 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50333088&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25227504 125083190 CHEMBL1631914 ZINC59151445 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50613730 COc1cc2COc3ccccc3NC(=O)[C@@H](CCCCCC(=O)NO)OC\C=C/c(c2)c1 InChI=1S/C25H30N2O6/c1-31-20-15-18-8-7-13-32-23(11-3-2-4-12-24(28)27-30)25(29)26-21-9-5-6-10-22(21)33-17-19(14-18)16-20/h5-10,14-16,23,30H,2-4,11-13,17H2,1H3,(H,26,29)(H,27,28)/b8-7-/t23-/m1/s1 LMOIMHSPFQECJG-XBKFQHLESA-N 50333089 (R)-6-(19-Methoxy-11-oxo-3,13-dioxa-10-azatricyclo[15.3.1.04,9] henicosa-1(21),4(9),5,7,15,17,19-heptaen-12-yl)hexanoic acid hydroxyamide::CHEMBL1631915 Histone deacetylase 4 Homo sapiens 284 ChEMBL 10.1021/jm101092u 10.7270/Q28G8KZJ 21073160 Auzzas, L; Larsson, A; Matera, R; Baraldi, A; Deschênes-Simard, B; Giannini, G; Cabri, W; Battistuzzi, G; Gallo, G; Ciacci, A; Vesci, L; Pisano, C TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50333089 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50333089&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25227505 125083191 CHEMBL1631915 ZINC59151448 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50613731 COc1cc2CCCOC(CCCCCC(=O)NO)C(=O)Nc3ccccc3OCc(c2)c1 InChI=1S/C25H32N2O6/c1-31-20-15-18-8-7-13-32-23(11-3-2-4-12-24(28)27-30)25(29)26-21-9-5-6-10-22(21)33-17-19(14-18)16-20/h5-6,9-10,14-16,23,30H,2-4,7-8,11-13,17H2,1H3,(H,26,29)(H,27,28) HIEFOIISQBSAEQ-UHFFFAOYSA-N 50333090 (R/S)-6-(19-Methoxy-11-oxo-3,13-dioxa-10-azatricyclo[15.3.1.04,9]henicosa-1(21),4(9),5,7,17,19-hexaen-12-yl)hexanoic acid hydroxyamide::CHEMBL1631916 Histone deacetylase 4 Homo sapiens 447 ChEMBL 10.1021/jm101092u 10.7270/Q28G8KZJ 21073160 Auzzas, L; Larsson, A; Matera, R; Baraldi, A; Deschênes-Simard, B; Giannini, G; Cabri, W; Battistuzzi, G; Gallo, G; Ciacci, A; Vesci, L; Pisano, C TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50333090 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50333090&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25066549 125083192 CHEMBL1631916 ZINC59151456 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50613732 COc1cc2CCCO[C@@H](CCCCCC(=O)NO)C(=O)Nc3ccccc3OCc(c2)c1 InChI=1S/C25H32N2O6/c1-31-20-15-18-8-7-13-32-23(11-3-2-4-12-24(28)27-30)25(29)26-21-9-5-6-10-22(21)33-17-19(14-18)16-20/h5-6,9-10,14-16,23,30H,2-4,7-8,11-13,17H2,1H3,(H,26,29)(H,27,28)/t23-/m0/s1 HIEFOIISQBSAEQ-QHCPKHFHSA-N 50333093 (S)-6-(19-Methoxy-11-oxo-3,13-dioxa-10-azatricyclo[15.3.1.04,9]henicosa-1(21),4(9),5,7,17,19-hexaen-12-yl)hexanoic acid hydroxyamide::CHEMBL1631917 Histone deacetylase 4 Homo sapiens 118 ChEMBL 10.1021/jm101092u 10.7270/Q28G8KZJ 21073160 Auzzas, L; Larsson, A; Matera, R; Baraldi, A; Deschênes-Simard, B; Giannini, G; Cabri, W; Battistuzzi, G; Gallo, G; Ciacci, A; Vesci, L; Pisano, C TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50333093 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50333093&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25227508 125083195 CHEMBL1631917 ZINC59151451 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50613733 COc1cc2CCCO[C@H](CCCCCC(=O)NO)C(=O)Nc3ccccc3OCc(c2)c1 InChI=1S/C25H32N2O6/c1-31-20-15-18-8-7-13-32-23(11-3-2-4-12-24(28)27-30)25(29)26-21-9-5-6-10-22(21)33-17-19(14-18)16-20/h5-6,9-10,14-16,23,30H,2-4,7-8,11-13,17H2,1H3,(H,26,29)(H,27,28)/t23-/m1/s1 HIEFOIISQBSAEQ-HSZRJFAPSA-N 50333094 (R)-6-(19-Methoxy-11-oxo-3,13-dioxa-10-azatricyclo[15.3.1.04,9]henicosa-1(21),4(9),5,7,17,19-hexaen-12-yl)hexanoic acid hydroxyamide::CHEMBL1631918 Histone deacetylase 4 Homo sapiens 454 ChEMBL 10.1021/jm101092u 10.7270/Q28G8KZJ 21073160 Auzzas, L; Larsson, A; Matera, R; Baraldi, A; Deschênes-Simard, B; Giannini, G; Cabri, W; Battistuzzi, G; Gallo, G; Ciacci, A; Vesci, L; Pisano, C TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50333094 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50333094&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25227513 125083196 CHEMBL1631918 ZINC59151456 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634932 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 210 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634933 CNC(=O)C(CCCCCCC(=O)Nc1ccccc1)N=O InChI=1S/C16H23N3O3/c1-17-16(21)14(19-22)11-7-2-3-8-12-15(20)18-13-9-5-4-6-10-13/h4-6,9-10,14H,2-3,7-8,11-12H2,1H3,(H,17,21)(H,18,20) LEVQYUXQSVPMMA-UHFFFAOYSA-N 50341844 2-(Hydroxyimino)-N1-methyl-N9-phenylnonanediamide::CHEMBL1767029 Histone deacetylase 4 Homo sapiens 65700 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341844 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341844&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932411 131344780 CHEMBL1767029 ZINC71318447 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634934 CNC(=O)C(CCCCCCC(=O)Nc1ccc2ccccc2c1)N=O InChI=1S/C20H25N3O3/c1-21-20(25)18(23-26)10-4-2-3-5-11-19(24)22-17-13-12-15-8-6-7-9-16(15)14-17/h6-9,12-14,18H,2-5,10-11H2,1H3,(H,21,25)(H,22,24) SGEJUQOOLDRWCI-UHFFFAOYSA-N 50341845 2-(Hydroxyimino)-N1-methyl-N9-(naphthalene-2-yl)nonanediamide::CHEMBL1767030 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341845 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341845&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932412 131344781 CHEMBL1767030 ZINC71318392 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634935 CNC(=O)C(CCCCCCC(=O)Nc1cnc2ccccc2c1)N=O InChI=1S/C19H24N4O3/c1-20-19(25)17(23-26)10-4-2-3-5-11-18(24)22-15-12-14-8-6-7-9-16(14)21-13-15/h6-9,12-13,17H,2-5,10-11H2,1H3,(H,20,25)(H,22,24) BKZCDTWYVBUYRW-UHFFFAOYSA-N 50341846 2-(Hydroxyimino)-N1-methyl-N9-(quinolin-3-yl)nonanediamide::CHEMBL1767031 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341846 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341846&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932413 131344782 CHEMBL1767031 ZINC71296799 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634936 CNC(=O)C(CCCCCCC(=O)NC1c2ccccc2-c2ccccc12)N=O InChI=1S/C23H27N3O3/c1-24-23(28)20(26-29)14-4-2-3-5-15-21(27)25-22-18-12-8-6-10-16(18)17-11-7-9-13-19(17)22/h6-13,20,22H,2-5,14-15H2,1H3,(H,24,28)(H,25,27) GCLAISIYNLVKHY-UHFFFAOYSA-N 50341847 CHEMBL1767032::N9-(9H-Fluoren-9-yl)-2-(hydroxyimino)-N1-methylnonanediamide Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341847 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341847&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932414 131344783 CHEMBL1767032 ZINC71329502 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634937 CNC(=O)C(CCCCCCC(=O)Nc1ccc(cc1)N(C)C)N=O InChI=1S/C18H28N4O3/c1-19-18(24)16(21-25)8-6-4-5-7-9-17(23)20-14-10-12-15(13-11-14)22(2)3/h10-13,16H,4-9H2,1-3H3,(H,19,24)(H,20,23) TZBZCBUHLZQZST-UHFFFAOYSA-N 50341848 CHEMBL1767033::N9-(4-(Dimethylamino)phenyl)-2-(hydroxyimino)-N1-methylnonanediamide Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341848 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341848&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932415 131344784 CHEMBL1767033 ZINC71329094 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634938 CNC(=O)C(CCCCCCC(=O)Nc1ccc(cc1)-c1ccccc1)N=O InChI=1S/C22H27N3O3/c1-23-22(27)20(25-28)11-7-2-3-8-12-21(26)24-19-15-13-18(14-16-19)17-9-5-4-6-10-17/h4-6,9-10,13-16,20H,2-3,7-8,11-12H2,1H3,(H,23,27)(H,24,26) DTTAFRPXPCCONE-UHFFFAOYSA-N 50341849 CHEMBL1767034::N9-([1,10-Biphenyl]-4-yl)-2-(hydroxyimino)-N1-methylnonanediamide Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341849 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341849&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932416 131344785 CHEMBL1767034 ZINC71318404 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634939 CNC(=O)C(CCCCCCC(=O)Nc1cccc(Br)c1)N=O InChI=1S/C16H22BrN3O3/c1-18-16(22)14(20-23)9-4-2-3-5-10-15(21)19-13-8-6-7-12(17)11-13/h6-8,11,14H,2-5,9-10H2,1H3,(H,18,22)(H,19,21) KWVURXQEMVUPQP-UHFFFAOYSA-N 50341850 CHEMBL1767035::N9-(3-Bromophenyl)-2-(hydroxyimino)-N1-methylnonanediamide Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341850 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341850&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932417 131344786 CHEMBL1767035 ZINC71316222 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634940 CNC(=O)C(CCCCCCC(=O)Nc1cccc(c1)-c1ccccc1)N=O InChI=1S/C22H27N3O3/c1-23-22(27)20(25-28)14-7-2-3-8-15-21(26)24-19-13-9-12-18(16-19)17-10-5-4-6-11-17/h4-6,9-13,16,20H,2-3,7-8,14-15H2,1H3,(H,23,27)(H,24,26) GZLCDSKYHTVXEH-UHFFFAOYSA-N 50341851 CHEMBL1767036::N9-([1,1'-Biphenyl]-3-yl)-2-(hydroxyimino)-N1-methylnonanediamide Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341851 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341851&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932418 131344787 CHEMBL1767036 ZINC71318457 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634941 CNC(=O)C(CCCCCCC(=O)Nc1cccc(c1)-c1ccc(cc1)C(O)=O)N=O InChI=1S/C23H27N3O5/c1-24-22(28)20(26-31)9-4-2-3-5-10-21(27)25-19-8-6-7-18(15-19)16-11-13-17(14-12-16)23(29)30/h6-8,11-15,20H,2-5,9-10H2,1H3,(H,24,28)(H,25,27)(H,29,30) FXMFVAHFHJMAQP-UHFFFAOYSA-N 50341852 3'-(8-(Hydroxyimino)-9-(methylamino)-9-oxononanamido)-[1,1'-biphenyl]-4-carboxylic Acid::CHEMBL1767037 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341852 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341852&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932419 131344788 CHEMBL1767037 ZINC71318403 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634942 CNC(=O)C(CCCCCCC(=O)Nc1cccc(c1)-c1cccnc1)N=O InChI=1S/C21H26N4O3/c1-22-21(27)19(25-28)11-4-2-3-5-12-20(26)24-18-10-6-8-16(14-18)17-9-7-13-23-15-17/h6-10,13-15,19H,2-5,11-12H2,1H3,(H,22,27)(H,24,26) VYGXZAJSYVNMJG-UHFFFAOYSA-N 50341853 2-(Hydroxyimino)-N1-methyl-N9-(3-(pyridine-3-yl)phenyl)nonanediamide::CHEMBL1767038 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341853 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341853&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932420 131344789 CHEMBL1767038 ZINC71329803 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634943 CNC(=O)C(CCCCCCC(=O)Nc1cccc(c1)-c1ccc(Cl)nc1)N=O InChI=1S/C21H25ClN4O3/c1-23-21(28)18(26-29)9-4-2-3-5-10-20(27)25-17-8-6-7-15(13-17)16-11-12-19(22)24-14-16/h6-8,11-14,18H,2-5,9-10H2,1H3,(H,23,28)(H,25,27) QTHIZXQOFLSDLG-UHFFFAOYSA-N 50341854 CHEMBL1767039::N9-(3-(6-Chloropyridin-3-yl)phenyl)-2-(hydroxyimino)-N1-methylnonanediamide Histone deacetylase 4 Homo sapiens 58900 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341854 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341854&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932421 131344790 CHEMBL1767039 ZINC71296703 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634944 CNC(=O)C(CCCCCCC(=O)Nc1cccc(c1)-c1cncc2cc(Cl)ccc12)N=O InChI=1S/C25H27ClN4O3/c1-27-25(32)23(30-33)9-4-2-3-5-10-24(31)29-20-8-6-7-17(14-20)22-16-28-15-18-13-19(26)11-12-21(18)22/h6-8,11-16,23H,2-5,9-10H2,1H3,(H,27,32)(H,29,31) GQNYPVFSTOGQGD-UHFFFAOYSA-N 50341855 CHEMBL1767040::N9-(3-(7-Chloroisoquinolin-4-yl)phenyl)-2-)hydroxyimino)-N1-methylnonanediamide Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341855 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341855&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932422 131344791 CHEMBL1767040 ZINC71329812 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634945 CNC(=O)C(CCCCCCNC(=O)c1cc(on1)-c1cccc(NC(=O)OC(C)(C)C)c1)N=O InChI=1S/C24H33N5O6/c1-24(2,3)34-23(32)27-17-11-9-10-16(14-17)20-15-19(29-35-20)22(31)26-13-8-6-5-7-12-18(28-33)21(30)25-4/h9-11,14-15,18H,5-8,12-13H2,1-4H3,(H,25,30)(H,26,31)(H,27,32) LZPYYMDMJZQOPI-UHFFFAOYSA-N 50341837 CHEMBL1767041::tert-Butyl 3-(3-(7-(Hydroxyimino)-8-(methylamino)-8-oxooctylcarbamoyl)isoxazol-5-yl)phenylcarbamate Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341837 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341837&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932404 131344773 CHEMBL1767041 ZINC71317592 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634946 CNC(=O)C(CCCCCCNC(=O)c1cc(on1)-c1ccc(NC(=O)OC(C)(C)C)cc1)N=O InChI=1S/C24H33N5O6/c1-24(2,3)34-23(32)27-17-12-10-16(11-13-17)20-15-19(29-35-20)22(31)26-14-8-6-5-7-9-18(28-33)21(30)25-4/h10-13,15,18H,5-9,14H2,1-4H3,(H,25,30)(H,26,31)(H,27,32) ZHSZISXSXFCTGV-UHFFFAOYSA-N 50341838 CHEMBL1767042::tert-Butyl 4-(3-(7-Hydroxyimino-8-(methylamino)-8-oxooctylcarbamoyl)isoxazol-5-yl)phenylcarbamate Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341838 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341838&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932405 131344774 CHEMBL1767042 ZINC71316239 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634947 CNC(=O)C(CCCCCCNC(=O)c1cc(on1)-c1cccc(N)c1)N=O InChI=1S/C19H25N5O4/c1-21-18(25)15(23-27)9-4-2-3-5-10-22-19(26)16-12-17(28-24-16)13-7-6-8-14(20)11-13/h6-8,11-12,15H,2-5,9-10,20H2,1H3,(H,21,25)(H,22,26) HFTBQKCVLFDPKD-UHFFFAOYSA-N 50341839 5-(3-Aminophenyl)-N-(7-(hydroxyimino)-8-(methylamino)-8-oxooctyl)isoxazole-3-carboxamide::CHEMBL1767043 Histone deacetylase 4 Homo sapiens 38900 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341839 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341839&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932406 131344775 CHEMBL1767043 ZINC71318818 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634948 CNC(=O)C(CCCCCCNC(=O)c1cc(on1)-c1ccc(N)cc1)N=O InChI=1S/C19H25N5O4/c1-21-18(25)15(23-27)6-4-2-3-5-11-22-19(26)16-12-17(28-24-16)13-7-9-14(20)10-8-13/h7-10,12,15H,2-6,11,20H2,1H3,(H,21,25)(H,22,26) LUOBQTLGSXROBD-UHFFFAOYSA-N 50341840 5-(4-Aminophenyl)-N-(7-(hydroxyimino)-8-(methylamino)-8-oxooctyl)isoxazole-3-carboxamide::CHEMBL1767044 Histone deacetylase 4 Homo sapiens 48800 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341840 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341840&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932407 131344776 CHEMBL1767044 ZINC71317238 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634949 CNC(=O)C(CCCCC[C@H](N(Cc1ccc(OC)cc1)C(=O)OC(C)(C)C)C(=O)Nc1ccccc1)N=O InChI=1S/C29H40N4O6/c1-29(2,3)39-28(36)33(20-21-16-18-23(38-5)19-17-21)25(27(35)31-22-12-8-6-9-13-22)15-11-7-10-14-24(32-37)26(34)30-4/h6,8-9,12-13,16-19,24-25H,7,10-11,14-15,20H2,1-5H3,(H,30,34)(H,31,35)/t24?,25-/m0/s1 GVOVWTCGJXODRR-BBMPLOMVSA-N 50341841 (S)-tert-Butyl(8-(Hydroxyimino)-9-(methylamino)-1,9-dioxo-1-(phenylamino)nonan-2-yl)(4-methoxybenzyl)carbamate::CHEMBL1767045 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341841 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341841&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932408 131344777 CHEMBL1767045 ZINC71318090 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634950 CNC(=O)C(CCCCC[C@H](NCc1ccc(OC)cc1)C(=O)Nc1ccccc1)N=O InChI=1S/C24H32N4O4/c1-25-23(29)22(28-31)12-8-4-7-11-21(24(30)27-19-9-5-3-6-10-19)26-17-18-13-15-20(32-2)16-14-18/h3,5-6,9-10,13-16,21-22,26H,4,7-8,11-12,17H2,1-2H3,(H,25,29)(H,27,30)/t21-,22?/m0/s1 KVSXZHGSBZYVCZ-HMTLIYDFSA-N 50341842 (S)-2-(Hydroxyimino)-8-((4-methoxybenzyl)amino)-N1methyl-N9-phenylnonanediamide::CHEMBL1767046 Histone deacetylase 4 Homo sapiens 59200 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341842 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341842&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932409 131344778 CHEMBL1767046 ZINC71316223 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50634951 CNC(=O)C(CCCCC[C@H](N(Cc1ccccc1)Cc1ccccc1)C(=O)Nc1ccccc1)N=O InChI=1S/C30H36N4O3/c1-31-29(35)27(33-37)20-12-5-13-21-28(30(36)32-26-18-10-4-11-19-26)34(22-24-14-6-2-7-15-24)23-25-16-8-3-9-17-25/h2-4,6-11,14-19,27-28H,5,12-13,20-23H2,1H3,(H,31,35)(H,32,36)/t27?,28-/m0/s1 WAZRMVAFNMGPBD-CPRJBALCSA-N 50341843 (S)-2-(Dibenzylamino)-8-(hydroxyimino)-N9-methyl-N1-phenylnonanediamide::CHEMBL1767047 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/jm101373a 10.7270/Q2CR5TNZ 21417297 Botta, CB; Cabri, W; Cini, E; De Cesare, L; Fattorusso, C; Giannini, G; Persico, M; Petrella, A; Rondinelli, F; Rodriquez, M; Russo, A; Taddei, M Universita` degli Studi di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341843 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341843&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932410 131344779 CHEMBL1767047 ZINC71317596 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50657595 CC(C)CCc1c(O)c(CCC(=O)NO)ccc1OCCCCCCC(=O)NO InChI=1S/C21H34N2O6/c1-15(2)8-11-17-18(29-14-6-4-3-5-7-19(24)22-27)12-9-16(21(17)26)10-13-20(25)23-28/h9,12,15,26-28H,3-8,10-11,13-14H2,1-2H3,(H,22,24)(H,23,25) UQMPTGLAYDPERB-UHFFFAOYSA-N 50351943 CHEMBL1822042 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2011.06.002 10.7270/Q2ZS2WWD 21712146 Huang, WJ; Chen, CC; Chao, SW; Yu, CC; Yang, CY; Guh, JH; Lin, YC; Kuo, CI; Yang, P; Chang, CI Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50351943 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50351943&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 54576530 136358629 CHEMBL1822042 ZINC72179371 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50657596 CC(C)CCc1c(O)c(CCC(=O)NO)ccc1OCCCCCCCC(=O)NO InChI=1S/C22H36N2O6/c1-16(2)9-12-18-19(13-10-17(22(18)27)11-14-21(26)24-29)30-15-7-5-3-4-6-8-20(25)23-28/h10,13,16,27-29H,3-9,11-12,14-15H2,1-2H3,(H,23,25)(H,24,26) CHQKSRGYKLCECS-UHFFFAOYSA-N 50351944 CHEMBL1822043 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2011.06.002 10.7270/Q2ZS2WWD 21712146 Huang, WJ; Chen, CC; Chao, SW; Yu, CC; Yang, CY; Guh, JH; Lin, YC; Kuo, CI; Yang, P; Chang, CI Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50351944 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50351944&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 54576529 136358630 CHEMBL1822043 ZINC72179372 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50662853 C\C=C1/NC(=O)[C@@H](CS)NC(=O)[C@H](CC(=O)C[C@H](OC(=O)[C@@H](NC1=O)C(C)C)\C=C\CCS)C(C)C InChI=1S/C25H39N3O6S2/c1-6-19-23(31)28-21(15(4)5)25(33)34-17(9-7-8-10-35)11-16(29)12-18(14(2)3)22(30)27-20(13-36)24(32)26-19/h6-7,9,14-15,17-18,20-21,35-36H,8,10-13H2,1-5H3,(H,26,32)(H,27,30)(H,28,31)/b9-7+,19-6-/t17-,18-,20-,21+/m1/s1 UPCFDQLGZODPFB-BXJZLCHMSA-N 50354086 FK-228::Istodax::ROMIDEPSIN Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1021/np200324x 10.7270/Q2MW2HJ9 21793558 Wang, C; Henkes, LM; Doughty, LB; He, M; Wang, D; Meyer-Almes, FJ; Cheng, YQ University of Wisconsin-Milwaukee http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50354086 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50354086&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 49863499 136360772 ZINC58575686 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50662854 C\C=C1\NC(=O)[C@@H](CS)NC(=O)[C@H](NC(=O)C[C@H](OC(=O)[C@@H](NC1=O)C(C)C)\C=C\CCS)C(C)C InChI=1S/C24H38N4O6S2/c1-6-16-21(30)28-20(14(4)5)24(33)34-15(9-7-8-10-35)11-18(29)27-19(13(2)3)23(32)26-17(12-36)22(31)25-16/h6-7,9,13-15,17,19-20,35-36H,8,10-12H2,1-5H3,(H,25,31)(H,26,32)(H,27,29)(H,28,30)/b9-7+,16-6+/t15-,17-,19-,20+/m1/s1 MEJLVLMAJJRLCR-LSUWEBKGSA-N 50354087 CHEMBL1836143 Histone deacetylase 4 Homo sapiens 470 ChEMBL 10.1021/np200324x 10.7270/Q2MW2HJ9 21793558 Wang, C; Henkes, LM; Doughty, LB; He, M; Wang, D; Meyer-Almes, FJ; Cheng, YQ University of Wisconsin-Milwaukee http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50354087 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50354087&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56673171 136360773 CHEMBL1836143 ZINC03944185 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50662855 CC[C@H](C)[C@H]1NC(=O)[C@H]2CSSCC\C=C\[C@H](CC(=O)N[C@H](CCSC)C(=O)N2)OC(=O)C[C@@H]1O InChI=1S/C23H37N3O6S3/c1-4-14(2)21-18(27)12-20(29)32-15-7-5-6-9-34-35-13-17(23(31)26-21)25-22(30)16(8-10-33-3)24-19(28)11-15/h5,7,14-18,21,27H,4,6,8-13H2,1-3H3,(H,24,28)(H,25,30)(H,26,31)/b7-5+/t14-,15+,16+,17+,18-,21+/m0/s1 VJXBYUITQBTTQM-DSRNDQRRSA-N 50354088 CHEMBL1836142 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1021/np200324x 10.7270/Q2MW2HJ9 21793558 Wang, C; Henkes, LM; Doughty, LB; He, M; Wang, D; Meyer-Almes, FJ; Cheng, YQ University of Wisconsin-Milwaukee http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50354088 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50354088&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56602459 136360774 CHEMBL1836142 ZINC72125220 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50662856 CC[C@H](C)[C@H]1NC(=O)[C@@H](CS)NC(=O)[C@@H](CCSC)NC(=O)C[C@H](OC(=O)C[C@@H]1O)\C=C\CCS InChI=1S/C23H39N3O6S3/c1-4-14(2)21-18(27)12-20(29)32-15(7-5-6-9-33)11-19(28)24-16(8-10-35-3)22(30)25-17(13-34)23(31)26-21/h5,7,14-18,21,27,33-34H,4,6,8-13H2,1-3H3,(H,24,28)(H,25,30)(H,26,31)/b7-5+/t14-,15+,16+,17+,18-,21+/m0/s1 QPHJHMOKVYIJGF-DSRNDQRRSA-N 50354089 CHEMBL1836144 Histone deacetylase 4 Homo sapiens 42000 ChEMBL 10.1021/np200324x 10.7270/Q2MW2HJ9 21793558 Wang, C; Henkes, LM; Doughty, LB; He, M; Wang, D; Meyer-Almes, FJ; Cheng, YQ University of Wisconsin-Milwaukee http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50354089 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50354089&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56602461 136360775 CHEMBL1836144 ZINC72123158 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50662857 CCCC[C@H]1NC(=O)C[C@@H]2OC(=O)C[C@H](O)[C@H](NC(=O)[C@@H](CSSCC\C=C\2)NC1=O)[C@@H](C)CC InChI=1S/C24H39N3O6S2/c1-4-6-10-17-23(31)26-18-14-35-34-11-8-7-9-16(12-20(29)25-17)33-21(30)13-19(28)22(15(3)5-2)27-24(18)32/h7,9,15-19,22,28H,4-6,8,10-14H2,1-3H3,(H,25,29)(H,26,31)(H,27,32)/b9-7+/t15-,16+,17+,18+,19-,22+/m0/s1 MUNWAZFRKGVMPQ-RIRJJDMNSA-N 50354084 CHEMBL1836145 Histone deacetylase 4 Homo sapiens 22000 ChEMBL 10.1021/np200324x 10.7270/Q2MW2HJ9 21793558 Wang, C; Henkes, LM; Doughty, LB; He, M; Wang, D; Meyer-Almes, FJ; Cheng, YQ University of Wisconsin-Milwaukee http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50354084 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50354084&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56676500 136360770 CHEMBL1836145 ZINC72122972 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50662858 CCCC[C@H]1NC(=O)C[C@H](OC(=O)C[C@H](O)[C@H](NC(=O)[C@@H](CS)NC1=O)[C@@H](C)CC)\C=C\CCS InChI=1S/C24H41N3O6S2/c1-4-6-10-17-23(31)26-18(14-35)24(32)27-22(15(3)5-2)19(28)13-21(30)33-16(9-7-8-11-34)12-20(29)25-17/h7,9,15-19,22,28,34-35H,4-6,8,10-14H2,1-3H3,(H,25,29)(H,26,31)(H,27,32)/b9-7+/t15-,16+,17+,18+,19-,22+/m0/s1 SOUWDYWQNTVVMP-RIRJJDMNSA-N 50354085 CHEMBL1836042 Histone deacetylase 4 Homo sapiens 18000 ChEMBL 10.1021/np200324x 10.7270/Q2MW2HJ9 21793558 Wang, C; Henkes, LM; Doughty, LB; He, M; Wang, D; Meyer-Almes, FJ; Cheng, YQ University of Wisconsin-Milwaukee http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50354085 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50354085&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56682413 136360771 CHEMBL1836042 ZINC72123426 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50657597 CC(C)CCc1c(OCCCCCCC(=O)NO)ccc2ccc(=O)oc12 InChI=1S/C21H29NO5/c1-15(2)8-11-17-18(12-9-16-10-13-20(24)27-21(16)17)26-14-6-4-3-5-7-19(23)22-25/h9-10,12-13,15,25H,3-8,11,14H2,1-2H3,(H,22,23) KEVRYVQWWIUOTN-UHFFFAOYSA-N 50351945 CHEMBL1822046 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2011.06.002 10.7270/Q2ZS2WWD 21712146 Huang, WJ; Chen, CC; Chao, SW; Yu, CC; Yang, CY; Guh, JH; Lin, YC; Kuo, CI; Yang, P; Chang, CI Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50351945 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50351945&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 54576744 136358631 CHEMBL1822046 ZINC72179477 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50657598 CC(C)CCc1c(OCCCCCCC(=O)NO)ccc2CCC(=O)Oc12 InChI=1S/C21H31NO5/c1-15(2)8-11-17-18(12-9-16-10-13-20(24)27-21(16)17)26-14-6-4-3-5-7-19(23)22-25/h9,12,15,25H,3-8,10-11,13-14H2,1-2H3,(H,22,23) LNONTANPNYDPKB-UHFFFAOYSA-N 50351946 CHEMBL1822050 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2011.06.002 10.7270/Q2ZS2WWD 21712146 Huang, WJ; Chen, CC; Chao, SW; Yu, CC; Yang, CY; Guh, JH; Lin, YC; Kuo, CI; Yang, P; Chang, CI Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50351946 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50351946&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 54770442 136358632 CHEMBL1822050 ZINC72180845 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50657599 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2011.06.002 10.7270/Q2ZS2WWD 21712146 Huang, WJ; Chen, CC; Chao, SW; Yu, CC; Yang, CY; Guh, JH; Lin, YC; Kuo, CI; Yang, P; Chang, CI Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50664343 FC(F)(F)C(=O)c1ccc(s1)C(=O)N1CCn2c(C1)ncc2-c1ccccc1 InChI=1S/C19H14F3N3O2S/c20-19(21,22)17(26)14-6-7-15(28-14)18(27)24-8-9-25-13(10-23-16(25)11-24)12-4-2-1-3-5-12/h1-7,10H,8-9,11H2 AZTSYZUNKYTXOA-UHFFFAOYSA-N 25164 2,2,2-trifluoro-1-[5-({3-phenyl-5H,6H,7H,8H-imidazo[1,2-a]pyrazin-7-yl}carbonyl)thiophen-2-yl]ethan-1-one::CHEMBL496094::thiophene derivative, 3j Histone deacetylase 4 Homo sapiens 367 ChEMBL 10.1016/j.bmcl.2011.07.100 10.7270/Q2KS6RZR 21875805 Ilies, M; Dowling, DP; Lombardi, PM; Christianson, DW Drexel University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25164 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25164&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023802 56374305 CHEMBL496094 ZINC29069775 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649203 CN(C(C)=O)c1ccc(cc1)C(=O)CSc1nc(C)cc(=O)[nH]1 InChI=1S/C16H17N3O3S/c1-10-8-15(22)18-16(17-10)23-9-14(21)12-4-6-13(7-5-12)19(3)11(2)20/h4-8H,9H2,1-3H3,(H,17,18,22) AQXNOPHVPVYVTH-UHFFFAOYSA-N 50348372 CHEMBL1800251 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348372 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348372&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56666361 136355058 CHEMBL1800251 ZINC72109037 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649204 Cc1cc(=O)[nH]c(SCC(=O)c2ccc(NC(=O)c3ccccc3)cc2)n1 InChI=1S/C20H17N3O3S/c1-13-11-18(25)23-20(21-13)27-12-17(24)14-7-9-16(10-8-14)22-19(26)15-5-3-2-4-6-15/h2-11H,12H2,1H3,(H,22,26)(H,21,23,25) ZKCAAGFLDZQGRH-UHFFFAOYSA-N 50348373 CHEMBL1800373 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348373 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348373&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56662847 136355059 CHEMBL1800373 ZINC72109868 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649205 COc1ccc(cc1)C(=O)CSc1nc(C)cc(=O)[nH]1 InChI=1S/C14H14N2O3S/c1-9-7-13(18)16-14(15-9)20-8-12(17)10-3-5-11(19-2)6-4-10/h3-7H,8H2,1-2H3,(H,15,16,18) PYEQFDZBEVPXJY-UHFFFAOYSA-N 50348374 CHEMBL1307946 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348374 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348374&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 722456 136355060 CHEMBL1307946 ZINC08632101 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649206 Cc1cc(=O)[nH]c(SCC(=O)c2ccc(cc2)C(C)(C)C)n1 InChI=1S/C17H20N2O2S/c1-11-9-15(21)19-16(18-11)22-10-14(20)12-5-7-13(8-6-12)17(2,3)4/h5-9H,10H2,1-4H3,(H,18,19,21) QMAHTCRPGFEJOU-UHFFFAOYSA-N 50348375 CHEMBL1800374 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348375 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348375&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 2439049 136355061 CHEMBL1800374 ZINC09143521 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649207 Cc1cc(=O)[nH]c(SCC(=O)c2ccc(Cl)cc2)n1 InChI=1S/C13H11ClN2O2S/c1-8-6-12(18)16-13(15-8)19-7-11(17)9-2-4-10(14)5-3-9/h2-6H,7H2,1H3,(H,15,16,18) NGNBFAHURVSCGG-UHFFFAOYSA-N 50348376 CHEMBL1800375 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348376 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348376&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 696767 136355062 CHEMBL1800375 ZINC17750270 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649208 Cc1cc(=O)[nH]c(SCC(=O)c2ccc(O)cc2)n1 InChI=1S/C13H12N2O3S/c1-8-6-12(18)15-13(14-8)19-7-11(17)9-2-4-10(16)5-3-9/h2-6,16H,7H2,1H3,(H,14,15,18) AZEYVCAPARHUDD-UHFFFAOYSA-N 50348377 CHEMBL1800376 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348377 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348377&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 43802426 136355063 CHEMBL1800376 ZINC37354313 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649209 Cc1cc(=O)[nH]c(SCC(=O)c2ccc(O)c(O)c2)n1 InChI=1S/C13H12N2O4S/c1-7-4-12(19)15-13(14-7)20-6-11(18)8-2-3-9(16)10(17)5-8/h2-5,16-17H,6H2,1H3,(H,14,15,19) GYSSMOSVLZXNJL-UHFFFAOYSA-N 55151 1-(3,4-Dihydroxy-phenyl)-2-(4-hydroxy-6-methyl-pyrimidin-2-ylsulfanyl)-ethanone::2-[2-(3,4-dihydroxyphenyl)-2-oxoethyl]sulfanyl-6-methyl-1H-pyrimidin-4-one::2-[2-[3,4-bis(oxidanyl)phenyl]-2-oxidanylidene-ethyl]sulfanyl-6-methyl-1H-pyrimidin-4-one::2-[[2-(3,4-dihydroxyphenyl)-2-keto-ethyl]thio]-6-methyl-1H-pyrimidin-4-one::2-[[2-(3,4-dihydroxyphenyl)-2-oxoethyl]thio]-6-methyl-1H-pyrimidin-4-one::CHEMBL209453::MLS001212148::SMR000518041::cid_687937 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=55151 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=55151&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 687937 252635154 CHEMBL209453 ZINC18163844 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649210 Cc1cc(=O)[nH]c(SCC(=O)c2ccc3OCCOc3c2)n1 InChI=1S/C15H14N2O4S/c1-9-6-14(19)17-15(16-9)22-8-11(18)10-2-3-12-13(7-10)21-5-4-20-12/h2-3,6-7H,4-5,8H2,1H3,(H,16,17,19) YOCPSWNLBPSEPL-UHFFFAOYSA-N 50348378 CHEMBL1800377 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348378 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348378&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56679897 136355064 CHEMBL1800377 ZINC72108993 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649211 Cc1cc(=O)[nH]c(SCC(=O)c2ccc3CC(=O)Nc3c2)n1 InChI=1S/C15H13N3O3S/c1-8-4-13(20)18-15(16-8)22-7-12(19)10-3-2-9-6-14(21)17-11(9)5-10/h2-5H,6-7H2,1H3,(H,17,21)(H,16,18,20) ZNBAASZQROSFAR-UHFFFAOYSA-N 50348379 CHEMBL1800378 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348379 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348379&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56676563 136355065 CHEMBL1800378 ZINC72109714 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649212 Cc1cc(=O)[nH]c(SCC(=O)c2cccs2)n1 InChI=1S/C11H10N2O2S2/c1-7-5-10(15)13-11(12-7)17-6-8(14)9-3-2-4-16-9/h2-5H,6H2,1H3,(H,12,13,15) BUJNNVDRDXQSPZ-UHFFFAOYSA-N 50348380 CHEMBL1800379 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348380 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348380&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1114049 136355066 CHEMBL1800379 ZINC18084678 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649213 COC(=O)CSc1nc(C)cc(=O)[nH]1 InChI=1S/C8H10N2O3S/c1-5-3-6(11)10-8(9-5)14-4-7(12)13-2/h3H,4H2,1-2H3,(H,9,10,11) NDOORHZZKWHUSR-UHFFFAOYSA-N 50348381 CHEMBL1800380 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348381 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348381&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 593355 136355067 CHEMBL1800380 ZINC13739146 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649214 CC(=O)CSc1nc(C)cc(=O)[nH]1 InChI=1S/C8H10N2O2S/c1-5-3-7(12)10-8(9-5)13-4-6(2)11/h3H,4H2,1-2H3,(H,9,10,12) SVUUYQJCKFMOIW-UHFFFAOYSA-N 50348382 CHEMBL1800381 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348382 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348382&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 2084143 136355068 CHEMBL1800381 ZINC02622230 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649215 Cc1cc(=O)[nH]c(SCC(=O)C(C)(C)C)n1 InChI=1S/C11H16N2O2S/c1-7-5-9(15)13-10(12-7)16-6-8(14)11(2,3)4/h5H,6H2,1-4H3,(H,12,13,15) ILJHWOPYMZRUJN-UHFFFAOYSA-N 50348383 CHEMBL1800382 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348383 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348383&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 2730153 136355069 CHEMBL1800382 ZINC13468269 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649216 CCOC(=O)CC(=O)CSc1nc(C)cc(=O)[nH]1 InChI=1S/C11H14N2O4S/c1-3-17-10(16)5-8(14)6-18-11-12-7(2)4-9(15)13-11/h4H,3,5-6H2,1-2H3,(H,12,13,15) LDHVRTTYVRCAAV-UHFFFAOYSA-N 50348384 CHEMBL1800383 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348384 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348384&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56676564 136355070 CHEMBL1800383 ZINC68815599 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649217 Cc1cc(=O)[nH]c(SCC(=O)NCCCCc2ccccc2)n1 InChI=1S/C17H21N3O2S/c1-13-11-15(21)20-17(19-13)23-12-16(22)18-10-6-5-9-14-7-3-2-4-8-14/h2-4,7-8,11H,5-6,9-10,12H2,1H3,(H,18,22)(H,19,20,21) VGIVLGHUCVQJCA-UHFFFAOYSA-N 50348385 CHEMBL1800384 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348385 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348385&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56679898 136355071 CHEMBL1800384 ZINC72110855 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649218 Cc1cc(=O)[nH]c(SCC(=O)NCCc2ccccc2)n1 InChI=1S/C15H17N3O2S/c1-11-9-13(19)18-15(17-11)21-10-14(20)16-8-7-12-5-3-2-4-6-12/h2-6,9H,7-8,10H2,1H3,(H,16,20)(H,17,18,19) VEYSSDYQEFIFDX-UHFFFAOYSA-N 96613 2-[(4-keto-6-methyl-1H-pyrimidin-2-yl)thio]-N-phenethyl-acetamide::2-[(4-methyl-6-oxo-1,6-dihydro-2-pyrimidinyl)thio]-N-(2-phenylethyl)acetamide::2-[(6-methyl-4-oxidanylidene-1H-pyrimidin-2-yl)sulfanyl]-N-(2-phenylethyl)ethanamide::2-[(6-methyl-4-oxo-1H-pyrimidin-2-yl)sulfanyl]-N-(2-phenylethyl)acetamide::2-[(6-methyl-4-oxo-1H-pyrimidin-2-yl)thio]-N-(2-phenylethyl)acetamide::CHEMBL1722433::MLS000531589::SMR000136527::cid_892234 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=96613 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=96613&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 892234 164037857 CHEMBL1722433 ZINC18093765 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649219 Cc1cc(=O)[nH]c(SCC(=O)NCCCCCCc2ccccc2)n1 InChI=1S/C19H25N3O2S/c1-15-13-17(23)22-19(21-15)25-14-18(24)20-12-8-3-2-5-9-16-10-6-4-7-11-16/h4,6-7,10-11,13H,2-3,5,8-9,12,14H2,1H3,(H,20,24)(H,21,22,23) YAGMJQSXXVLPGT-UHFFFAOYSA-N 50348387 CHEMBL1800385 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348387 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348387&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56666338 136355073 CHEMBL1800385 ZINC72110856 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649433 CC(=O)Nc1ccc(cc1)C(=O)CSc1nc(C)cc(=O)[nH]1 InChI=1S/C15H15N3O3S/c1-9-7-14(21)18-15(16-9)22-8-13(20)11-3-5-12(6-4-11)17-10(2)19/h3-7H,8H2,1-2H3,(H,17,19)(H,16,18,21) NZVOKXQPGIDGBV-UHFFFAOYSA-N 50348388 CHEMBL1800241 Histone deacetylase 4 Homo sapiens 32500 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348388 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348388&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 784998 136355074 CHEMBL1800241 ZINC18155397 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649434 CC(=O)Nc1ccc(cc1)C(=O)CSc1nccc(C)n1 InChI=1S/C15H15N3O2S/c1-10-7-8-16-15(17-10)21-9-14(20)12-3-5-13(6-4-12)18-11(2)19/h3-8H,9H2,1-2H3,(H,18,19) CIRYLVAQJQBNQO-UHFFFAOYSA-N 50348389 CHEMBL1800242 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348389 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348389&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56659403 136355075 CHEMBL1800242 ZINC72109334 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649435 COc1cc(C)nc(SCC(=O)c2ccc(NC(C)=O)cc2)n1 InChI=1S/C16H17N3O3S/c1-10-8-15(22-3)19-16(17-10)23-9-14(21)12-4-6-13(7-5-12)18-11(2)20/h4-8H,9H2,1-3H3,(H,18,20) XIMLQEFHZGPEAB-UHFFFAOYSA-N 50348390 CHEMBL1800243 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348390 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348390&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56673234 136355076 CHEMBL1800243 ZINC72108167 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649436 CC(=O)Nc1ccc(cc1)C(=O)CSc1nc(C)cc(C)n1 InChI=1S/C16H17N3O2S/c1-10-8-11(2)18-16(17-10)22-9-15(21)13-4-6-14(7-5-13)19-12(3)20/h4-8H,9H2,1-3H3,(H,19,20) IEFMPTCWLPFBLK-UHFFFAOYSA-N 50348391 CHEMBL1800244 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348391 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348391&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1108280 136355077 CHEMBL1800244 ZINC00841137 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649437 CC(=O)Nc1ccc(cc1)C(=O)CSc1cccc(O)c1 InChI=1S/C16H15NO3S/c1-11(18)17-13-7-5-12(6-8-13)16(20)10-21-15-4-2-3-14(19)9-15/h2-9,19H,10H2,1H3,(H,17,18) ZKJBOQRBWXMBRK-UHFFFAOYSA-N 50348392 CHEMBL1800245 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348392 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348392&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56666337 136355078 CHEMBL1800245 ZINC72107588 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649438 CC(=O)Nc1ccc(cc1)C(=O)COc1nc(C)cc(=O)[nH]1 InChI=1S/C15H15N3O4/c1-9-7-14(21)18-15(16-9)22-8-13(20)11-3-5-12(6-4-11)17-10(2)19/h3-7H,8H2,1-2H3,(H,17,19)(H,16,18,21) IYHJPCSJWTYWLB-UHFFFAOYSA-N 50348393 CHEMBL1800246 Histone deacetylase 4 Homo sapiens 54200 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348393 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348393&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56679894 136355079 CHEMBL1800246 ZINC72109194 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649439 CC(=O)Nc1ccc(cc1)C(=O)COc1cc(C)cc(=O)[nH]1 InChI=1S/C16H16N2O4/c1-10-7-15(21)18-16(8-10)22-9-14(20)12-3-5-13(6-4-12)17-11(2)19/h3-8H,9H2,1-2H3,(H,17,19)(H,18,21) SNILZMZTNVWFRS-UHFFFAOYSA-N 50348394 CHEMBL1800247 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348394 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348394&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56673261 136355080 CHEMBL1800247 ZINC72109699 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649440 CC(=O)Nc1ccc(CSc2nc(C)cc(=O)[nH]2)cc1 InChI=1S/C14H15N3O2S/c1-9-7-13(19)17-14(15-9)20-8-11-3-5-12(6-4-11)16-10(2)18/h3-7H,8H2,1-2H3,(H,16,18)(H,15,17,19) ADGPHPSNLKLQDU-UHFFFAOYSA-N 50348395 CHEMBL1800248 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348395 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348395&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56662874 136355081 CHEMBL1800248 ZINC72109036 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649441 CC(=O)Nc1ccc(cc1)C(O)CSc1nc(C)cc(=O)[nH]1 InChI=1S/C15H17N3O3S/c1-9-7-14(21)18-15(16-9)22-8-13(20)11-3-5-12(6-4-11)17-10(2)19/h3-7,13,20H,8H2,1-2H3,(H,17,19)(H,16,18,21) ONYHRCLBDDLZNZ-UHFFFAOYSA-N 50348396 CHEMBL1800249 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348396 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348396&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56662875 136355082 CHEMBL1800249 ZINC72107278 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50649442 Cc1cc(=O)[nH]c(SCC(=O)c2ccccc2)n1 InChI=1S/C13H12N2O2S/c1-9-7-12(17)15-13(14-9)18-8-11(16)10-5-3-2-4-6-10/h2-7H,8H2,1H3,(H,14,15,17) LDUQCWSKGSQRBH-UHFFFAOYSA-N 50348397 CHEMBL1800250 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2011.05.098 10.7270/Q20P10CT 21696956 Kemp, MM; Wang, Q; Fuller, JH; West, N; Martinez, NM; Morse, EM; Weiwer, M; Schreiber, SL; Bradner, JE; Koehler, AN Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348397 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348397&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 334111 136355083 CHEMBL1800250 ZINC09446020 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50661021 ONC(=O)\C=C\c1ccc2n(CCN3CCCCC3)c(CCc3ccccc3)nc2c1 InChI=1S/C25H30N4O2/c30-25(27-31)14-11-21-9-12-23-22(19-21)26-24(13-10-20-7-3-1-4-8-20)29(23)18-17-28-15-5-2-6-16-28/h1,3-4,7-9,11-12,14,19,31H,2,5-6,10,13,15-18H2,(H,27,30)/b14-11+ XZWCFUZJOAZGAI-SDNWHVSQSA-N 50248522 CHEMBL489332::N-hydroxy-3-(2-phenethyl-1-(2-(piperidin-1-yl)ethyl)-1H-benzo[d]imidazol-5-yl)acrylamide::US10201527, Compound 67::US10736881, Compound 67::US8551988, 67 Histone deacetylase 4 Homo sapiens 8.7 ChEMBL 10.1021/jm2003552 10.7270/Q29S1RD6 21634430 Wang, H; Yu, N; Chen, D; Lee, KC; Lye, PL; Chang, JW; Deng, W; Ng, MC; Lu, T; Khoo, ML; Poulsen, A; Sangthongpitag, K; Wu, X; Hu, C; Goh, KC; Wang, X; Fang, L; Goh, KL; Khng, HH; Goh, SK; Yeo, P; Liu, X; Bonday, Z; Wood, JM; Dymock, BW; Kantharaj, E; Sun, ET S*BIO Pte Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50248522 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50248522&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6918846 104103167 CHEMBL489332 ZINC13981299 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50661022 Cl.Cl.CCCCc1nc2cc(\C=C\C(=O)NO)ccc2n1CCN(CC)CC InChI=1S/C20H30N4O2/c1-4-7-8-19-21-17-15-16(10-12-20(25)22-26)9-11-18(17)24(19)14-13-23(5-2)6-3/h9-12,15,26H,4-8,13-14H2,1-3H3,(H,22,25)/b12-10+ JHDKZFFAIZKUCU-ZRDIBKRKSA-N 50353227 CHEMBL3215861 Histone deacetylase 4 Homo sapiens 19.0 ChEMBL 10.1021/jm2003552 10.7270/Q29S1RD6 21634430 Wang, H; Yu, N; Chen, D; Lee, KC; Lye, PL; Chang, JW; Deng, W; Ng, MC; Lu, T; Khoo, ML; Poulsen, A; Sangthongpitag, K; Wu, X; Hu, C; Goh, KC; Wang, X; Fang, L; Goh, KL; Khng, HH; Goh, SK; Yeo, P; Liu, X; Bonday, Z; Wood, JM; Dymock, BW; Kantharaj, E; Sun, ET S*BIO Pte Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50353227 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50353227&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90664458 136359913 CHEMBL3215861 ZINC43152558 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50661023 CCCCc1nc2cc(\C=C\C(=O)NO)ccc2n1CCNC(C)C InChI=1S/C19H28N4O2/c1-4-5-6-18-21-16-13-15(8-10-19(24)22-25)7-9-17(16)23(18)12-11-20-14(2)3/h7-10,13-14,20,25H,4-6,11-12H2,1-3H3,(H,22,24)/b10-8+ OCDKGOFASZWZBG-CSKARUKUSA-N 50353228 CHEMBL1830396 Histone deacetylase 4 Homo sapiens 11 ChEMBL 10.1021/jm2003552 10.7270/Q29S1RD6 21634430 Wang, H; Yu, N; Chen, D; Lee, KC; Lye, PL; Chang, JW; Deng, W; Ng, MC; Lu, T; Khoo, ML; Poulsen, A; Sangthongpitag, K; Wu, X; Hu, C; Goh, KC; Wang, X; Fang, L; Goh, KL; Khng, HH; Goh, SK; Yeo, P; Liu, X; Bonday, Z; Wood, JM; Dymock, BW; Kantharaj, E; Sun, ET S*BIO Pte Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50353228 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50353228&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 16068495 136359914 CHEMBL1830396 ZINC34987244 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50661024 CN(C)CC(C)(C)Cn1c(CC(C)(C)C)nc2cc(\C=C\C(=O)NO)ccc12 InChI=1S/C22H34N4O2/c1-21(2,3)13-19-23-17-12-16(9-11-20(27)24-28)8-10-18(17)26(19)15-22(4,5)14-25(6)7/h8-12,28H,13-15H2,1-7H3,(H,24,27)/b11-9+ FDURBWFXDKGGLQ-PKNBQFBNSA-N 50353229 CHEMBL1830397 Histone deacetylase 4 Homo sapiens 7.9 ChEMBL 10.1021/jm2003552 10.7270/Q29S1RD6 21634430 Wang, H; Yu, N; Chen, D; Lee, KC; Lye, PL; Chang, JW; Deng, W; Ng, MC; Lu, T; Khoo, ML; Poulsen, A; Sangthongpitag, K; Wu, X; Hu, C; Goh, KC; Wang, X; Fang, L; Goh, KL; Khng, HH; Goh, SK; Yeo, P; Liu, X; Bonday, Z; Wood, JM; Dymock, BW; Kantharaj, E; Sun, ET S*BIO Pte Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50353229 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50353229&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 16068056 136359915 CHEMBL1830397 ZINC34986773 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50661025 CCCCCCc1nc2cc(\C=C\C(=O)NO)ccc2n1CCNCC InChI=1S/C20H30N4O2/c1-3-5-6-7-8-19-22-17-15-16(10-12-20(25)23-26)9-11-18(17)24(19)14-13-21-4-2/h9-12,15,21,26H,3-8,13-14H2,1-2H3,(H,23,25)/b12-10+ QEULZLVHLYBHJN-ZRDIBKRKSA-N 50353230 CHEMBL1830420 Histone deacetylase 4 Homo sapiens 6.2 ChEMBL 10.1021/jm2003552 10.7270/Q29S1RD6 21634430 Wang, H; Yu, N; Chen, D; Lee, KC; Lye, PL; Chang, JW; Deng, W; Ng, MC; Lu, T; Khoo, ML; Poulsen, A; Sangthongpitag, K; Wu, X; Hu, C; Goh, KC; Wang, X; Fang, L; Goh, KL; Khng, HH; Goh, SK; Yeo, P; Liu, X; Bonday, Z; Wood, JM; Dymock, BW; Kantharaj, E; Sun, ET S*BIO Pte Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50353230 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50353230&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 16068595 136359916 CHEMBL1830420 ZINC34987351 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50661026 CCCCCCc1nc2cc(\C=C\C(=O)NO)ccc2n1CCNC(C)C InChI=1S/C21H32N4O2/c1-4-5-6-7-8-20-23-18-15-17(10-12-21(26)24-27)9-11-19(18)25(20)14-13-22-16(2)3/h9-12,15-16,22,27H,4-8,13-14H2,1-3H3,(H,24,26)/b12-10+ IFKSLVQLRLKBBZ-ZRDIBKRKSA-N 50353231 CHEMBL1830422 Histone deacetylase 4 Homo sapiens 6.6 ChEMBL 10.1021/jm2003552 10.7270/Q29S1RD6 21634430 Wang, H; Yu, N; Chen, D; Lee, KC; Lye, PL; Chang, JW; Deng, W; Ng, MC; Lu, T; Khoo, ML; Poulsen, A; Sangthongpitag, K; Wu, X; Hu, C; Goh, KC; Wang, X; Fang, L; Goh, KL; Khng, HH; Goh, SK; Yeo, P; Liu, X; Bonday, Z; Wood, JM; Dymock, BW; Kantharaj, E; Sun, ET S*BIO Pte Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50353231 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50353231&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 16068594 136359917 CHEMBL1830422 ZINC34987350 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50661027 CCCCCCc1nc2cc(\C=C\C(=O)NO)ccc2n1CCN(C)C InChI=1S/C20H30N4O2/c1-4-5-6-7-8-19-21-17-15-16(10-12-20(25)22-26)9-11-18(17)24(19)14-13-23(2)3/h9-12,15,26H,4-8,13-14H2,1-3H3,(H,22,25)/b12-10+ PUFPSZILMLJFEU-ZRDIBKRKSA-N 50353232 CHEMBL1830424 Histone deacetylase 4 Homo sapiens 5.3 ChEMBL 10.1021/jm2003552 10.7270/Q29S1RD6 21634430 Wang, H; Yu, N; Chen, D; Lee, KC; Lye, PL; Chang, JW; Deng, W; Ng, MC; Lu, T; Khoo, ML; Poulsen, A; Sangthongpitag, K; Wu, X; Hu, C; Goh, KC; Wang, X; Fang, L; Goh, KL; Khng, HH; Goh, SK; Yeo, P; Liu, X; Bonday, Z; Wood, JM; Dymock, BW; Kantharaj, E; Sun, ET S*BIO Pte Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50353232 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50353232&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 15983982 136359918 CHEMBL1830424 ZINC34849693 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50661028 CCNCCn1c(CC\C=C/CC)nc2cc(\C=C\C(=O)NO)ccc12 InChI=1S/C20H28N4O2/c1-3-5-6-7-8-19-22-17-15-16(10-12-20(25)23-26)9-11-18(17)24(19)14-13-21-4-2/h5-6,9-12,15,21,26H,3-4,7-8,13-14H2,1-2H3,(H,23,25)/b6-5-,12-10+ YKOJCIKYDZHWDT-UDMPHVCXSA-N 50353233 CHEMBL1830536 Histone deacetylase 4 Homo sapiens 2.4 ChEMBL 10.1021/jm2003552 10.7270/Q29S1RD6 21634430 Wang, H; Yu, N; Chen, D; Lee, KC; Lye, PL; Chang, JW; Deng, W; Ng, MC; Lu, T; Khoo, ML; Poulsen, A; Sangthongpitag, K; Wu, X; Hu, C; Goh, KC; Wang, X; Fang, L; Goh, KL; Khng, HH; Goh, SK; Yeo, P; Liu, X; Bonday, Z; Wood, JM; Dymock, BW; Kantharaj, E; Sun, ET S*BIO Pte Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50353233 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50353233&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 53363518 136359919 CHEMBL1830536 ZINC72120618 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50661029 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 20 ChEMBL 10.1021/jm2003552 10.7270/Q29S1RD6 21634430 Wang, H; Yu, N; Chen, D; Lee, KC; Lye, PL; Chang, JW; Deng, W; Ng, MC; Lu, T; Khoo, ML; Poulsen, A; Sangthongpitag, K; Wu, X; Hu, C; Goh, KC; Wang, X; Fang, L; Goh, KL; Khng, HH; Goh, SK; Yeo, P; Liu, X; Bonday, Z; Wood, JM; Dymock, BW; Kantharaj, E; Sun, ET S*BIO Pte Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50661030 Cc1[nH]c2ccccc2c1CCNCc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C21H23N3O2/c1-15-18(19-4-2-3-5-20(19)23-15)12-13-22-14-17-8-6-16(7-9-17)10-11-21(25)24-26/h2-11,22-23,26H,12-14H2,1H3,(H,24,25)/b11-10+ FPOHNWQLNRZRFC-ZHACJKMWSA-N 29589 Faridak::LBH-589::LBH-589B::Panobinostat::US10722597, Compound Panobinostat Histone deacetylase 4 Homo sapiens 0.600000 ChEMBL 10.1021/jm2003552 10.7270/Q29S1RD6 21634430 Wang, H; Yu, N; Chen, D; Lee, KC; Lye, PL; Chang, JW; Deng, W; Ng, MC; Lu, T; Khoo, ML; Poulsen, A; Sangthongpitag, K; Wu, X; Hu, C; Goh, KC; Wang, X; Fang, L; Goh, KL; Khng, HH; Goh, SK; Yeo, P; Liu, X; Bonday, Z; Wood, JM; Dymock, BW; Kantharaj, E; Sun, ET S*BIO Pte Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=29589 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=29589&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search LBH 5EF8 6918837 81055018 ZINC22010649 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50661031 ONC(=O)\C=C\c1cccc(c1)S(=O)(=O)Nc1ccccc1 InChI=1S/C15H14N2O4S/c18-15(16-19)10-9-12-5-4-8-14(11-12)22(20,21)17-13-6-2-1-3-7-13/h1-11,17,19H,(H,16,18)/b10-9+ NCNRHFGMJRPRSK-MDZDMXLPSA-N 25150 (2E)-N-hydroxy-3-[3-(phenylsulfamoyl)phenyl]prop-2-enamide::Belinosta::Belinostat::PXD-101::PXD101 Histone deacetylase 4 Homo sapiens 15 ChEMBL 10.1021/jm2003552 10.7270/Q29S1RD6 21634430 Wang, H; Yu, N; Chen, D; Lee, KC; Lye, PL; Chang, JW; Deng, W; Ng, MC; Lu, T; Khoo, ML; Poulsen, A; Sangthongpitag, K; Wu, X; Hu, C; Goh, KC; Wang, X; Fang, L; Goh, KL; Khng, HH; Goh, SK; Yeo, P; Liu, X; Bonday, Z; Wood, JM; Dymock, BW; Kantharaj, E; Sun, ET S*BIO Pte Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25150 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25150&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5OG 5EEN 6918638 56374291 61076 ZINC03818726 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50661228 ONC(=O)\C=C\c1ccc2n(CCN3CCCC3)c(CCc3ccccc3)nc2c1 InChI=1S/C24H28N4O2/c29-24(26-30)13-10-20-8-11-22-21(18-20)25-23(12-9-19-6-2-1-3-7-19)28(22)17-16-27-14-4-5-15-27/h1-3,6-8,10-11,13,18,30H,4-5,9,12,14-17H2,(H,26,29)/b13-10+ RCDIZKAYZBEALO-JLHYYAGUSA-N 50248476 CHEMBL491316::N-hydroxy-3-(2-phenethyl-1-(2-(pyrrolidin-1-yl)ethyl)-1H-benzo[d]imidazol-5-yl)acrylamide::N-hydroxy-3-[2-phenethyl-1-(2-pyrrolidin-1-ylethyl)-1H-benzimidazol-5-yl]acrylamide::SB-639::US10201527, Compound 72::US10736881, Compound 72::US8551988, 72 Histone deacetylase 4 Homo sapiens 8.5 ChEMBL 10.1021/jm2003552 10.7270/Q29S1RD6 21634430 Wang, H; Yu, N; Chen, D; Lee, KC; Lye, PL; Chang, JW; Deng, W; Ng, MC; Lu, T; Khoo, ML; Poulsen, A; Sangthongpitag, K; Wu, X; Hu, C; Goh, KC; Wang, X; Fang, L; Goh, KL; Khng, HH; Goh, SK; Yeo, P; Liu, X; Bonday, Z; Wood, JM; Dymock, BW; Kantharaj, E; Sun, ET S*BIO Pte Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50248476 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50248476&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6918877 104103127 CHEMBL491316 ZINC38192628 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50661229 CN(C)CC(C)(C)Cn1c(CCc2ccccc2)nc2cc(\C=C\C(=O)NO)ccc12 InChI=1S/C25H32N4O2/c1-25(2,17-28(3)4)18-29-22-13-10-20(12-15-24(30)27-31)16-21(22)26-23(29)14-11-19-8-6-5-7-9-19/h5-10,12-13,15-16,31H,11,14,17-18H2,1-4H3,(H,27,30)/b15-12+ FOLVOXAEHBGIDM-NTCAYCPXSA-N 50248570 3-(1-(3-(dimethylamino)-2,2-dimethylpropyl)-2-phenethyl-1H-benzo[d]imidazol-5-yl)-N-hydroxyacrylamide::CHEMBL460963::US10201527, Compound 17::US10736881, Compound 17::US8551988, 17 Histone deacetylase 4 Homo sapiens 10 ChEMBL 10.1021/jm2003552 10.7270/Q29S1RD6 21634430 Wang, H; Yu, N; Chen, D; Lee, KC; Lye, PL; Chang, JW; Deng, W; Ng, MC; Lu, T; Khoo, ML; Poulsen, A; Sangthongpitag, K; Wu, X; Hu, C; Goh, KC; Wang, X; Fang, L; Goh, KL; Khng, HH; Goh, SK; Yeo, P; Liu, X; Bonday, Z; Wood, JM; Dymock, BW; Kantharaj, E; Sun, ET S*BIO Pte Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50248570 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50248570&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44564642 104103208 CHEMBL460963 ZINC13981303 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50661238 CCCCCc1nc2cc(\C=C\C(=O)NO)ccc2n1CCNC(C)C InChI=1S/C20H30N4O2/c1-4-5-6-7-19-22-17-14-16(9-11-20(25)23-26)8-10-18(17)24(19)13-12-21-15(2)3/h8-11,14-15,21,26H,4-7,12-13H2,1-3H3,(H,23,25)/b11-9+ HRKITJYWVNASHR-PKNBQFBNSA-N 50353234 CHEMBL1830537 Histone deacetylase 4 Homo sapiens 3.6 ChEMBL 10.1021/jm2003552 10.7270/Q29S1RD6 21634430 Wang, H; Yu, N; Chen, D; Lee, KC; Lye, PL; Chang, JW; Deng, W; Ng, MC; Lu, T; Khoo, ML; Poulsen, A; Sangthongpitag, K; Wu, X; Hu, C; Goh, KC; Wang, X; Fang, L; Goh, KL; Khng, HH; Goh, SK; Yeo, P; Liu, X; Bonday, Z; Wood, JM; Dymock, BW; Kantharaj, E; Sun, ET S*BIO Pte Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50353234 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50353234&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 16068912 136359920 CHEMBL1830537 ZINC34987681 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50711432 ONC(=O)C=Cc1ccc2OC3(CCN(Cc4ccccc4)CC3)CC(=O)c2c1 InChI=1S/C23H24N2O4/c26-20-15-23(10-12-25(13-11-23)16-18-4-2-1-3-5-18)29-21-8-6-17(14-19(20)21)7-9-22(27)24-28/h1-9,14,28H,10-13,15-16H2,(H,24,27) PTSASYUIHCGRFT-UHFFFAOYSA-N 50361444 CHEMBL1938433 Histone deacetylase 4 Homo sapiens 127 ChEMBL 10.1021/jm200146u 10.7270/Q21V5FD6 21417419 Varasi, M; Thaler, F; Abate, A; Bigogno, C; Boggio, R; Carenzi, G; Cataudella, T; Dal Zuffo, R; Fulco, MC; Rozio, MG; Mai, A; Dondio, G; Minucci, S; Mercurio, C DAC SRL http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361444 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361444&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44253226 136965506 CHEMBL1938433 ZINC43208345 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50700497 ONC(=O)CCCCCCNC(=O)c1cc(on1)-c1ccc(NC(=O)c2cc(CN=[N+]=[N-])cc(c2)N=[N+]=[N-])cc1 InChI=1S/C25H26N10O5/c26-34-29-15-16-11-18(13-20(12-16)31-35-27)24(37)30-19-8-6-17(7-9-19)22-14-21(33-40-22)25(38)28-10-4-2-1-3-5-23(36)32-39/h6-9,11-14,39H,1-5,10,15H2,(H,28,38)(H,30,37)(H,32,36) CRPIWCWIMAOUCX-UHFFFAOYSA-N 50356634 CHEMBL1914702 Histone deacetylase 4 Homo sapiens 432 ChEMBL 10.1021/jm2001025 10.7270/Q2RX9CG0 21548582 Neelarapu, R; Holzle, DL; Velaparthi, S; Bai, H; Brunsteiner, M; Blond, SY; Petukhov, PA University of Illinois at Chicago http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50356634 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50356634&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 53361475 136960658 CHEMBL1914702 ZINC73161078 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50700498 ONC(=O)CCCCCCC(=O)Nc1cnn(Cc2cc(CN=[N+]=[N-])cc(c2)N=[N+]=[N-])c1 InChI=1S/C19H24N10O3/c20-27-22-10-14-7-15(9-16(8-14)25-28-21)12-29-13-17(11-23-29)24-18(30)5-3-1-2-4-6-19(31)26-32/h7-9,11,13,32H,1-6,10,12H2,(H,24,30)(H,26,31) IGNPXOQRVRXSKJ-UHFFFAOYSA-N 50356635 CHEMBL1914708 Histone deacetylase 4 Homo sapiens 379 ChEMBL 10.1021/jm2001025 10.7270/Q2RX9CG0 21548582 Neelarapu, R; Holzle, DL; Velaparthi, S; Bai, H; Brunsteiner, M; Blond, SY; Petukhov, PA University of Illinois at Chicago http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50356635 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50356635&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 53361474 136960659 CHEMBL1914708 ZINC73169434 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50700499 CC(C=CC(=O)NO)C=C(C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20) ALCVRKZFLFWUAZ-UHFFFAOYSA-N 19130 (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide::CHEMBL99::TSA::Trichostatin A (TSA) Histone deacetylase 4 Homo sapiens 122 ChEMBL 10.1021/jm2001025 10.7270/Q2RX9CG0 21548582 Neelarapu, R; Holzle, DL; Velaparthi, S; Bai, H; Brunsteiner, M; Blond, SY; Petukhov, PA University of Illinois at Chicago http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19130 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19130&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 91895926 46519165 46024 CHEMBL99 7005 ZINC05579377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815294 C[C@@H]1NC(=O)[C@H](CCCCCC(=O)NO)NC(=O)[C@H]2CCCN2C(=O)[C@H](C)NC1=O InChI=1S/C19H31N5O6/c1-11-16(26)21-12(2)19(29)24-10-6-8-14(24)18(28)22-13(17(27)20-11)7-4-3-5-9-15(25)23-30/h11-14,30H,3-10H2,1-2H3,(H,20,27)(H,21,26)(H,22,28)(H,23,25)/t11-,12-,13-,14+/m0/s1 ICSUPTZKVJGDQG-XDQVBPFNSA-N 50134799 6-((5S,8S,11S,13aR)-5,8-Dimethyl-4,7,10,13-tetraoxo-tetradecahydro-3a,6,9,12-tetraaza-cyclopentacyclododecen-11-yl)-hexanoic acid hydroxyamide::CHEMBL145110 Histone deacetylase 4 Homo sapiens 2.7 ChEMBL 10.1021/jm034167p 10.7270/Q28C9X0G 14584932 Mai, A; Massa, S; Pezzi, R; Rotili, D; Loidl, P; Brosch, G Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50134799 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50134799&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44363182 104025303 CHEMBL145110 ZINC27548922 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815302 C[C@@H]1NC(=O)[C@H](CCCCCC(=O)C2CO2)NC(=O)[C@H]2CCCN2C(=O)[C@H](C)NC1=O InChI=1S/C21H32N4O6/c1-12-18(27)23-13(2)21(30)25-10-6-8-15(25)20(29)24-14(19(28)22-12)7-4-3-5-9-16(26)17-11-31-17/h12-15,17H,3-11H2,1-2H3,(H,22,28)(H,23,27)(H,24,29)/t12-,13-,14-,15+,17?/m0/s1 WJKBTCSWQYZOOK-NNZQMTATSA-N 50134803 5,8-Dimethyl-11-(6-oxiranyl-6-oxo-hexyl)-decahydro-3a,6,9,12-tetraaza-cyclopentacyclododecene-4,7,10,13-tetraone::CHEMBL144205 Histone deacetylase 4 Homo sapiens 0.3 ChEMBL 10.1021/jm034167p 10.7270/Q28C9X0G 14584932 Mai, A; Massa, S; Pezzi, R; Rotili, D; Loidl, P; Brosch, G Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50134803 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50134803&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44363187 104025307 CHEMBL144205 ZINC27551344 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815315 C\C=C1/NC(=O)[C@@H](CS)NC(=O)[C@H](CC(=O)C[C@H](OC(=O)[C@@H](NC1=O)C(C)C)\C=C\CCS)C(C)C InChI=1S/C25H39N3O6S2/c1-6-19-23(31)28-21(15(4)5)25(33)34-17(9-7-8-10-35)11-16(29)12-18(14(2)3)22(30)27-20(13-36)24(32)26-19/h6-7,9,14-15,17-18,20-21,35-36H,8,10-13H2,1-5H3,(H,26,32)(H,27,30)(H,28,31)/b9-7+,19-6-/t17-,18-,20-,21+/m1/s1 UPCFDQLGZODPFB-BXJZLCHMSA-N 50354086 FK-228::Istodax::ROMIDEPSIN Histone deacetylase 4 Homo sapiens 510 ChEMBL 10.1021/jm034167p 10.7270/Q28C9X0G 14584932 Mai, A; Massa, S; Pezzi, R; Rotili, D; Loidl, P; Brosch, G Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50354086 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50354086&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 49863499 136360772 ZINC58575686 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815572 COc1ccc(cc1)S(=O)(=O)Nc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C16H16N2O5S/c1-23-14-7-9-15(10-8-14)24(21,22)18-13-5-2-12(3-6-13)4-11-16(19)17-20/h2-11,18,20H,1H3,(H,17,19)/b11-4+ OGJOCFPURGELIS-NYYWCZLTSA-N 50105678 (E)-N-Hydroxy-3-[4-(4-methoxy-benzenesulfonylamino)-phenyl]-acrylamide::CHEMBL95553::N-Hydroxy-3-[4-(4-methoxy-benzenesulfonylamino)-phenyl]-acrylamide::N-hydroxy-3-(4-(4-methoxyphenylsulfonamido)phenyl)acrylamide::US8796330, 113 Histone deacetylase 4 Homo sapiens 5000 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105678 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105678&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 10247137 104001377 CHEMBL95553 ZINC13493379 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815575 ONC(=O)CCc1ccc(NS(=O)(=O)c2ccccc2)cc1 InChI=1S/C15H16N2O4S/c18-15(16-19)11-8-12-6-9-13(10-7-12)17-22(20,21)14-4-2-1-3-5-14/h1-7,9-10,17,19H,8,11H2,(H,16,18) UDTWOBDYINGQOW-UHFFFAOYSA-N 50105684 3-(4-Benzenesulfonylamino-phenyl)-N-hydroxy-propionamide::CHEMBL98346::N-hydroxy-3-(4-(phenylsulfonamido)phenyl)propanamide::US8796330, 38 Histone deacetylase 4 Homo sapiens 5000 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105684 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105684&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4144 104001383 CHEMBL98346 ZINC03873248 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815582 ONC(=O)CCCc1ccc(NS(=O)(=O)c2ccccc2)cc1 InChI=1S/C16H18N2O4S/c19-16(17-20)8-4-5-13-9-11-14(12-10-13)18-23(21,22)15-6-2-1-3-7-15/h1-3,6-7,9-12,18,20H,4-5,8H2,(H,17,19) KJRQLODJJCERFP-UHFFFAOYSA-N 50105694 4-(4-Benzenesulfonylamino-phenyl)-N-hydroxy-butyramide::CHEMBL97860::N-hydroxy-4-(4-(phenylsulfonamido)phenyl)butanamide::US8796330, 42 Histone deacetylase 4 Homo sapiens >25000 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105694 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105694&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 18618646 104001393 CHEMBL97860 ZINC26718736 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815595 ONC(=O)Cc1ccc(NS(=O)(=O)c2ccccc2)cc1 InChI=1S/C14H14N2O4S/c17-14(15-18)10-11-6-8-12(9-7-11)16-21(19,20)13-4-2-1-3-5-13/h1-9,16,18H,10H2,(H,15,17) CCHZXNSNTYSTMZ-UHFFFAOYSA-N 50105690 2-(4-Benzenesulfonylamino-phenyl)-N-hydroxy-acetamide::CHEMBL319248::N-hydroxy-2-(4-(phenylsulfonamido)phenyl)acetamide Histone deacetylase 4 Homo sapiens >25000 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105690 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105690&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44328682 104001389 CHEMBL319248 ZINC26726729 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815600 C\C=C1/NC(=O)[C@@H](CS)NC(=O)[C@H](NC(=O)C[C@H](OC(=O)[C@@H](NC1=O)C(C)C)\C=C\CCS)C(C)C InChI=1S/C24H38N4O6S2/c1-6-16-21(30)28-20(14(4)5)24(33)34-15(9-7-8-10-35)11-18(29)27-19(13(2)3)23(32)26-17(12-36)22(31)25-16/h6-7,9,13-15,17,19-20,35-36H,8,10-12H2,1-5H3,(H,25,31)(H,26,32)(H,27,29)(H,28,30)/b9-7+,16-6-/t15-,17-,19-,20+/m1/s1 MEJLVLMAJJRLCR-GCCNXGTGSA-N 50135746 (3S,14S,15S)-6-Ethylidene-12-((R)-isopropyl)-3-isopropyl-16-(4-mercapto-but-1-enyl)-9-mercaptomethyl-1-oxa-4,7,10,13-tetraaza-cyclohexadecane-2,5,8,11,14-pentaone::CHEMBL146250 Histone deacetylase 4 Homo sapiens 25 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50135746 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50135746&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 9828788 104026105 CHEMBL146250 ZINC53224610 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815602 COc1ccc(NC(=O)Nc2ccc(\C=C\C(=O)NO)cc2)cc1OC InChI=1S/C18H19N3O5/c1-25-15-9-8-14(11-16(15)26-2)20-18(23)19-13-6-3-12(4-7-13)5-10-17(22)21-24/h3-11,24H,1-2H3,(H,21,22)(H2,19,20,23)/b10-5+ YYJQTOKVRNZEPY-BJMVGYQFSA-N 50123973 3-{4-[3-(3,4-Dimethoxy-phenyl)-ureido]-phenyl}-N-hydroxy-acrylamide::CHEMBL148769::US8796330, 147 Histone deacetylase 4 Homo sapiens >25000 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50123973 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50123973&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11068279 104016340 CHEMBL148769 ZINC13493387 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815629 C\C(=C/c1ccc(NS(=O)(=O)c2ccccc2)cc1)C(=O)NO InChI=1S/C16H16N2O4S/c1-12(16(19)17-20)11-13-7-9-14(10-8-13)18-23(21,22)15-5-3-2-4-6-15/h2-11,18,20H,1H3,(H,17,19)/b12-11+ RCHSCTGFXSOIJV-VAWYXSNFSA-N 50105695 (E)-3-(4-Benzenesulfonylamino-phenyl)-N-hydroxy-2-methyl-acrylamide::3-(4-Benzenesulfonylamino-phenyl)-N-hydroxy-2-methyl-acrylamide::CHEMBL100035::N-hydroxy-2-methyl-3-(4-(phenylsulfonamido)phenyl)acrylamide::US8796330, 91 Histone deacetylase 4 Homo sapiens >25000 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105695 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105695&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5353768 104001394 CHEMBL100035 ZINC26736167 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815636 C\C=C1/NC(=O)[C@@H](CS)NC(=O)[C@H](CC(=O)C[C@H](OC(=O)[C@@H](NC1=O)C(C)C)\C=C\CCS)C(C)C InChI=1S/C25H39N3O6S2/c1-6-19-23(31)28-21(15(4)5)25(33)34-17(9-7-8-10-35)11-16(29)12-18(14(2)3)22(30)27-20(13-36)24(32)26-19/h6-7,9,14-15,17-18,20-21,35-36H,8,10-13H2,1-5H3,(H,26,32)(H,27,30)(H,28,31)/b9-7+,19-6-/t17-,18-,20-,21+/m1/s1 UPCFDQLGZODPFB-BXJZLCHMSA-N 50354086 FK-228::Istodax::ROMIDEPSIN Histone deacetylase 4 Homo sapiens 510 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50354086 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50354086&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 49863499 136360772 ZINC58575686 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815642 CC(C=CC(=O)NO)C=C(C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20) ALCVRKZFLFWUAZ-UHFFFAOYSA-N 19130 (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide::CHEMBL99::TSA::Trichostatin A (TSA) Histone deacetylase 4 Homo sapiens 1000 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19130 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19130&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 91895926 46519165 46024 CHEMBL99 7005 ZINC05579377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815654 COc1ccc(cc1OC)S(=O)(=O)Nc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C17H18N2O6S/c1-24-15-9-8-14(11-16(15)25-2)26(22,23)19-13-6-3-12(4-7-13)5-10-17(20)18-21/h3-11,19,21H,1-2H3,(H,18,20)/b10-5+ MWBVVOSAOJSWLG-BJMVGYQFSA-N 50105689 (E)-3-[4-(3,4-Dimethoxy-benzenesulfonylamino)-phenyl]-N-hydroxy-acrylamide::3-(4-(3,4-dimethoxyphenylsulfonamido)phenyl)-N-hydroxyacrylamide::3-[4-(3,4-Dimethoxy-benzenesulfonylamino)-phenyl]-N-hydroxy-acrylamide::CHEMBL98669::US8796330, 90 Histone deacetylase 4 Homo sapiens 1000 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105689 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105689&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5353770 104001388 CHEMBL98669 ZINC01489488 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815663 CC(C)C(Cc1ccc(NS(=O)(=O)c2ccccc2)cc1)C(=O)NO InChI=1S/C18H22N2O4S/c1-13(2)17(18(21)19-22)12-14-8-10-15(11-9-14)20-25(23,24)16-6-4-3-5-7-16/h3-11,13,17,20,22H,12H2,1-2H3,(H,19,21) YADVGYPHHXJWNW-UHFFFAOYSA-N 50105676 2-(4-Benzenesulfonylamino-benzyl)-N-hydroxy-3-methyl-butyramide::CHEMBL97632::US8796330, 81 Histone deacetylase 4 Homo sapiens >25000 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105676 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105676&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 22986766 104001375 CHEMBL97632 ZINC26723002 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815673 Cc1ccc(NS(=O)(=O)c2ccc(\C=C\C(=O)NO)cc2)cc1 InChI=1S/C16H16N2O4S/c1-12-2-7-14(8-3-12)18-23(21,22)15-9-4-13(5-10-15)6-11-16(19)17-20/h2-11,18,20H,1H3,(H,17,19)/b11-6+ DQBCBVSLJCVWJK-IZZDOVSWSA-N 50123974 CHEMBL149534::N-Hydroxy-3-(4-p-tolylsulfamoyl-phenyl)-acrylamide::US8796330, 161 Histone deacetylase 4 Homo sapiens 1000 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50123974 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50123974&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 10914552 104016341 CHEMBL149534 ZINC13493384 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815675 ONC(=O)\C=C\c1ccc(NS(=O)(=O)c2ccc(cc2)-c2ccccc2)cc1 InChI=1S/C21H18N2O4S/c24-21(22-25)15-8-16-6-11-19(12-7-16)23-28(26,27)20-13-9-18(10-14-20)17-4-2-1-3-5-17/h1-15,23,25H,(H,22,24)/b15-8+ CITNMKKLNPYCDV-OVCLIPMQSA-N 50123975 3-[4-(biphenyl-4-sulfonylamino)-phenyl]-N-hydroxy-acrylamide::CHEMBL145891::US8796330, 120 Histone deacetylase 4 Homo sapiens 1000 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50123975 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50123975&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5353765 104016342 CHEMBL145891 ZINC03873249 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815692 CC(C=CC(=O)NO)C=C(C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20) ALCVRKZFLFWUAZ-UHFFFAOYSA-N 19130 (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide::CHEMBL99::TSA::Trichostatin A (TSA) Histone deacetylase 4 Homo sapiens 1000 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19130 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19130&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 91895926 46519165 46024 CHEMBL99 7005 ZINC05579377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50822658 CCC(C)[C@@H]1NC(=O)[C@@H](Cc2ccc(OC)cc2)NC(=O)[C@H](CCCCCC(=O)C(F)(F)F)NC(=O)[C@H]2CCCN2C1=O InChI=1S/C30H41F3N4O6/c1-4-18(2)25-29(42)37-16-8-10-23(37)28(41)34-21(9-6-5-7-11-24(38)30(31,32)33)26(39)35-22(27(40)36-25)17-19-12-14-20(43-3)15-13-19/h12-15,18,21-23,25H,4-11,16-17H2,1-3H3,(H,34,41)(H,35,39)(H,36,40)/t18?,21-,22+,23+,25-/m0/s1 JWEUAXYYHBPUQY-QXIQIYTISA-N 50153766 (5S,8R,11S,13aR)-5-sec-Butyl-8-(4-methoxy-benzyl)-11-(7,7,7-trifluoro-6-oxo-heptyl)-decahydro-3a,6,9,12-tetraaza-cyclopentacyclododecene-4,7,10,13-tetraone::CHEMBL188007 Histone deacetylase 4 Homo sapiens 610 ChEMBL 10.1016/j.bmcl.2004.08.016 10.7270/Q2222VJ6 15454224 Jose, B; Oniki, Y; Kato, T; Nishino, N; Sumida, Y; Yoshida, M CREST Research Project http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153766 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153766&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44395329 104041517 CHEMBL188007 ZINC28393120 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50822659 CCC(C)[C@@H]1NC(=O)[C@@H](Cc2ccc(OC)cc2)NC(=O)[C@H](CCCCSCC(=O)C(F)(F)F)NC(=O)[C@H]2CCCN2C1=O InChI=1S/C30H41F3N4O6S/c1-4-18(2)25-29(42)37-14-7-9-23(37)28(41)34-21(8-5-6-15-44-17-24(38)30(31,32)33)26(39)35-22(27(40)36-25)16-19-10-12-20(43-3)13-11-19/h10-13,18,21-23,25H,4-9,14-17H2,1-3H3,(H,34,41)(H,35,39)(H,36,40)/t18?,21-,22+,23+,25-/m0/s1 ZCQUKODSCJWNBV-QXIQIYTISA-N 50153767 (5S,8R,11S,13aR)-5-sec-Butyl-8-(4-methoxy-benzyl)-11-[4-(3,3,3-trifluoro-2-oxo-propylsulfanyl)-butyl]-decahydro-3a,6,9,12-tetraaza-cyclopentacyclododecene-4,7,10,13-tetraone::CHEMBL363750 Histone deacetylase 4 Homo sapiens 190 ChEMBL 10.1016/j.bmcl.2004.08.016 10.7270/Q2222VJ6 15454224 Jose, B; Oniki, Y; Kato, T; Nishino, N; Sumida, Y; Yoshida, M CREST Research Project http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153767 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153767&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 10326820 104041518 CHEMBL363750 ZINC28393745 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50822669 CC(C=CC(=O)NO)C=C(C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20) ALCVRKZFLFWUAZ-UHFFFAOYSA-N 19130 (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide::CHEMBL99::TSA::Trichostatin A (TSA) Histone deacetylase 4 Homo sapiens 20 ChEMBL 10.1016/j.bmcl.2004.08.016 10.7270/Q2222VJ6 15454224 Jose, B; Oniki, Y; Kato, T; Nishino, N; Sumida, Y; Yoshida, M CREST Research Project http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19130 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19130&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 91895926 46519165 46024 CHEMBL99 7005 ZINC05579377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815715 ONC(=O)\C=C\c1ccc(NS(=O)(=O)c2ccccc2)cc1 InChI=1S/C15H14N2O4S/c18-15(16-19)11-8-12-6-9-13(10-7-12)17-22(20,21)14-4-2-1-3-5-14/h1-11,17,19H,(H,16,18)/b11-8+ XPHVJIKSPLGZRT-DHZHZOJOSA-N 50105691 (E)-3-(4-Benzenesulfonylamino-phenyl)-N-hydroxy-acrylamide::3-(4-Benzenesulfonylamino-phenyl)-N-hydroxy-acrylamide::CHEMBL317814::N-hydroxy-3-(4-(phenylsulfonamido)phenyl)acrylamide::US8796330, 36 Histone deacetylase 4 Homo sapiens 5000 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105691 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105691&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5353767 104001390 CHEMBL317814 ZINC03873252 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815745 CN(c1ccc(\C=C\C(=O)NO)cc1)S(=O)(=O)c1ccccc1 InChI=1S/C16H16N2O4S/c1-18(23(21,22)15-5-3-2-4-6-15)14-10-7-13(8-11-14)9-12-16(19)17-20/h2-12,20H,1H3,(H,17,19)/b12-9+ IAMCGWXEUBEXCF-FMIVXFBMSA-N 50105685 (E)-3-[4-(Benzenesulfonyl-methyl-amino)-phenyl]-N-hydroxy-acrylamide::3-[4-(Benzenesulfonyl-methyl-amino)-phenyl]-N-hydroxy-acrylamide::CHEMBL97387::N-hydroxy-3-(4-(N-methylphenylsulfonamido)phenyl)acrylamide::US8796330, 170 Histone deacetylase 4 Homo sapiens >25000 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105685 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105685&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5353769 104001384 CHEMBL97387 ZINC03873568 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815755 ONC(=O)c1ccc(NS(=O)(=O)c2ccccc2)cc1 InChI=1S/C13H12N2O4S/c16-13(14-17)10-6-8-11(9-7-10)15-20(18,19)12-4-2-1-3-5-12/h1-9,15,17H,(H,14,16) ZSIKBIFOAPITGF-UHFFFAOYSA-N 50105682 4-Benzenesulfonylamino-N-hydroxy-benzamide::CHEMBL98345::N-hydroxy-4-(phenylsulfonamido)benzamide Histone deacetylase 4 Homo sapiens 5000 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105682 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105682&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44328873 104001381 CHEMBL98345 ZINC26721899 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815776 CC(Cc1ccc(NS(=O)(=O)c2ccccc2)cc1)C(=O)NO InChI=1S/C16H18N2O4S/c1-12(16(19)17-20)11-13-7-9-14(10-8-13)18-23(21,22)15-5-3-2-4-6-15/h2-10,12,18,20H,11H2,1H3,(H,17,19) RKDXFSHFQNWESJ-UHFFFAOYSA-N 50105680 3-(4-Benzenesulfonylamino-phenyl)-N-hydroxy-2-methyl-propionamide::CHEMBL97108::N-hydroxy-2-methyl-3-(4-(phenylsulfonamido)phenyl)propanamide::US8796330, 92 Histone deacetylase 4 Homo sapiens >25000 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105680 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105680&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 22986790 104001379 CHEMBL97108 ZINC26722539 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815799 COc1ccc(NS(=O)(=O)c2ccc(\C=C\C(=O)NO)cc2)cc1OC InChI=1S/C17H18N2O6S/c1-24-15-9-6-13(11-16(15)25-2)19-26(22,23)14-7-3-12(4-8-14)5-10-17(20)18-21/h3-11,19,21H,1-2H3,(H,18,20)/b10-5+ IMQKXTRDVUWCMO-BJMVGYQFSA-N 50123958 3-[4-(3,4-Dimethoxy-phenylsulfamoyl)-phenyl]-N-hydroxy-acrylamide::CHEMBL147506::US8796330, 98 Histone deacetylase 4 Homo sapiens 1000 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50123958 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50123958&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11036226 104016325 CHEMBL147506 ZINC13493385 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815804 Cc1ccc(cc1)S(=O)(=O)Nc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C16H16N2O4S/c1-12-2-9-15(10-3-12)23(21,22)18-14-7-4-13(5-8-14)6-11-16(19)17-20/h2-11,18,20H,1H3,(H,17,19)/b11-6+ PAOPWNUFHBHBRD-IZZDOVSWSA-N 50105677 (E)-N-Hydroxy-3-[4-(toluene-4-sulfonylamino)-phenyl]-acrylamide::CHEMBL317570::N-Hydroxy-3-[4-(toluene-4-sulfonylamino)-phenyl]-acrylamide::N-hydroxy-3-(4-(4-methylphenylsulfonamido)phenyl)acrylamide::US8796330, 108 Histone deacetylase 4 Homo sapiens 10000 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105677 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105677&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11724319 104001376 CHEMBL317570 ZINC13493377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50815805 ONC(=O)\C=C\c1ccc(cc1)S(=O)(=O)Nc1ccc(cc1)-c1ccccc1 InChI=1S/C21H18N2O4S/c24-21(22-25)15-8-16-6-13-20(14-7-16)28(26,27)23-19-11-9-18(10-12-19)17-4-2-1-3-5-17/h1-15,23,25H,(H,22,24)/b15-8+ TWAKWKHDTZWUMO-OVCLIPMQSA-N 50123967 3-[4-(Biphenyl-4-ylsulfamoyl)-phenyl]-N-hydroxy-acrylamide::CHEMBL434466::US8796330, 162 Histone deacetylase 4 Homo sapiens 1000 ChEMBL 10.1021/jm0303094 10.7270/Q2MP5413 14613312 Miller, TA; Witter, DJ; Belvedere, S Aton Pharma, Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50123967 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50123967&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 10271952 104016334 CHEMBL434466 ZINC13493386 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50841252 COc1ccc2[nH]c(C)c(CC(=O)N[C@@H](CCCCCC(=O)NO)C(=O)NCCc3c([nH]c4ccccc34)-c3ccccc3)c2c1 InChI=1S/C36H41N5O5/c1-23-28(29-21-25(46-2)17-18-31(29)38-23)22-34(43)39-32(15-7-4-8-16-33(42)41-45)36(44)37-20-19-27-26-13-9-10-14-30(26)40-35(27)24-11-5-3-6-12-24/h3,5-6,9-14,17-18,21,32,38,40,45H,4,7-8,15-16,19-20,22H2,1-2H3,(H,37,44)(H,39,43)(H,41,42)/t32-/m0/s1 VBWCMILVHANAGG-YTTGMZPUSA-N 50195108 (S)-N8-hydroxy-2-(2-(5-methoxy-2-methyl-1H-indol-3-yl)acetamido)-N1-(2-(2-phenyl-1H-indol-3-yl)ethyl)octanediamide::CHEMBL216641 Histone deacetylase 4 Homo sapiens 260 ChEMBL 10.1016/j.bmcl.2006.09.002 10.7270/Q2RN38PD 16987657 Jones, P; Altamura, S; Chakravarty, PK; Cecchetti, O; De Francesco, R; Gallinari, P; Ingenito, R; Meinke, PT; Petrocchi, A; Rowley, M; Scarpelli, R; Serafini, S; Steinkuhler, C IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50195108 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50195108&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11664499 104077249 CHEMBL216641 ZINC36338671 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50872137 CC[C@H](C)[C@@H]1NC(=O)[C@H](Cc2cn(OC)c3ccccc23)NC(=O)[C@H](CCCCCC(=O)CC)NC(=O)[C@H]2CCCCN2C1=O InChI=1S/C34H49N5O6/c1-5-22(3)30-34(44)38-19-13-12-18-29(38)33(43)35-26(16-9-7-8-14-24(40)6-2)31(41)36-27(32(42)37-30)20-23-21-39(45-4)28-17-11-10-15-25(23)28/h10-11,15,17,21-22,26-27,29-30H,5-9,12-14,16,18-20H2,1-4H3,(H,35,43)(H,36,41)(H,37,42)/t22-,26-,27-,29+,30-/m0/s1 JWOGUUIOCYMBPV-GMFLJSBRSA-N 50238632 (6S,9S,12S,14aR)-6-((S)-sec-Butyl)-9-(1-methoxy-1H-indol-3-ylmethyl)-12-(6-oxo-octyl)-decahydro-4a,7,10,13-tetraaza-benzocyclododecene-5,8,11,14-tetraone::CHEMBL430060::ChEMBL_275631 Histone deacetylase 4 Homo sapiens 1 ChEMBL 10.1073/pnas.0706487104 10.7270/Q2C82B5X 17956988 Lahm, A; Paolini, C; Pallaoro, M; Nardi, MC; Jones, P; Neddermann, P; Sambucini, S; Bottomley, MJ; Lo Surdo, P; Carfi, A; Koch, U; De Francesco, R; Steinkuhler, C; Gallinari, P Istituto di Ricerche di Biologia Molecolare http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50238632 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50238632&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6918328 104056492 CHEMBL430060 ZINC17654900 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50872140 OCCN(CCc1c[nH]c2ccccc12)Cc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C22H25N3O3/c26-14-13-25(12-11-19-15-23-21-4-2-1-3-20(19)21)16-18-7-5-17(6-8-18)9-10-22(27)24-28/h1-10,15,23,26,28H,11-14,16H2,(H,24,27)/b10-9+ BWDQBBCUWLSASG-MDZDMXLPSA-N 19428 (2E)-N-hydroxy-3-(4-{[(2-hydroxyethyl)[2-(1H-indol-3-yl)ethyl]amino]methyl}phenyl)prop-2-enamide::(E)-N-hydroxy-3-[4-[[2-hydroxyethyl-[2-(1H-indol-3-yl)ethyl]amino]methyl]phenyl]prop-2-enamide::CHEMBL356066::Dacinostat::LAQ-824::NVP-LAQ824 Histone deacetylase 4 Homo sapiens 1.2 ChEMBL 10.1073/pnas.0706487104 10.7270/Q2C82B5X 17956988 Lahm, A; Paolini, C; Pallaoro, M; Nardi, MC; Jones, P; Neddermann, P; Sambucini, S; Bottomley, MJ; Lo Surdo, P; Carfi, A; Koch, U; De Francesco, R; Steinkuhler, C; Gallinari, P Istituto di Ricerche di Biologia Molecolare http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19428 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19428&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6445533 46519450 CHEMBL356066 ZINC01494627 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50872141 Nc1ccccc1NC(=O)c1ccc(CNC(=O)OCc2cccnc2)cc1 InChI=1S/C21H20N4O3/c22-18-5-1-2-6-19(18)25-20(26)17-9-7-15(8-10-17)13-24-21(27)28-14-16-4-3-11-23-12-16/h1-12H,13-14,22H2,(H,24,27)(H,25,26) INVTYAOGFAGBOE-UHFFFAOYSA-N 19410 CHEMBL27759::MS-275::US11377423, MS-275::US11672788, Compound Entinostat::US9265734, MS-275::US9796664, Compound MS-275::benzamide-type inhibitor, 3::pyridin-3-ylmethyl N-({4-[(2-aminophenyl)carbamoyl]phenyl}methyl)carbamate Histone deacetylase 4 Homo sapiens 510 ChEMBL 10.1073/pnas.0706487104 10.7270/Q2C82B5X 17956988 Lahm, A; Paolini, C; Pallaoro, M; Nardi, MC; Jones, P; Neddermann, P; Sambucini, S; Bottomley, MJ; Lo Surdo, P; Carfi, A; Koch, U; De Francesco, R; Steinkuhler, C; Gallinari, P Istituto di Ricerche di Biologia Molecolare http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19410 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19410&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4261 46519433 CHEMBL27759 7007 ZINC01488870 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50872142 Nc1ccccc1NC(=O)c1ccc(CNC(=O)OCc2cccnc2)cc1 InChI=1S/C21H20N4O3/c22-18-5-1-2-6-19(18)25-20(26)17-9-7-15(8-10-17)13-24-21(27)28-14-16-4-3-11-23-12-16/h1-12H,13-14,22H2,(H,24,27)(H,25,26) INVTYAOGFAGBOE-UHFFFAOYSA-N 19410 CHEMBL27759::MS-275::US11377423, MS-275::US11672788, Compound Entinostat::US9265734, MS-275::US9796664, Compound MS-275::benzamide-type inhibitor, 3::pyridin-3-ylmethyl N-({4-[(2-aminophenyl)carbamoyl]phenyl}methyl)carbamate Histone deacetylase 4 Homo sapiens 3017 ChEMBL 10.1073/pnas.0706487104 10.7270/Q2C82B5X 17956988 Lahm, A; Paolini, C; Pallaoro, M; Nardi, MC; Jones, P; Neddermann, P; Sambucini, S; Bottomley, MJ; Lo Surdo, P; Carfi, A; Koch, U; De Francesco, R; Steinkuhler, C; Gallinari, P Istituto di Ricerche di Biologia Molecolare http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19410 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19410&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4261 46519433 CHEMBL27759 7007 ZINC01488870 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50872143 OCCN(CCc1c[nH]c2ccccc12)Cc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C22H25N3O3/c26-14-13-25(12-11-19-15-23-21-4-2-1-3-20(19)21)16-18-7-5-17(6-8-18)9-10-22(27)24-28/h1-10,15,23,26,28H,11-14,16H2,(H,24,27)/b10-9+ BWDQBBCUWLSASG-MDZDMXLPSA-N 19428 (2E)-N-hydroxy-3-(4-{[(2-hydroxyethyl)[2-(1H-indol-3-yl)ethyl]amino]methyl}phenyl)prop-2-enamide::(E)-N-hydroxy-3-[4-[[2-hydroxyethyl-[2-(1H-indol-3-yl)ethyl]amino]methyl]phenyl]prop-2-enamide::CHEMBL356066::Dacinostat::LAQ-824::NVP-LAQ824 Histone deacetylase 4 Homo sapiens 4 ChEMBL 10.1073/pnas.0706487104 10.7270/Q2C82B5X 17956988 Lahm, A; Paolini, C; Pallaoro, M; Nardi, MC; Jones, P; Neddermann, P; Sambucini, S; Bottomley, MJ; Lo Surdo, P; Carfi, A; Koch, U; De Francesco, R; Steinkuhler, C; Gallinari, P Istituto di Ricerche di Biologia Molecolare http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19428 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19428&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6445533 46519450 CHEMBL356066 ZINC01494627 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50872144 CC[C@H](C)[C@@H]1NC(=O)[C@H](Cc2cn(OC)c3ccccc23)NC(=O)[C@H](CCCCCC(=O)CC)NC(=O)[C@H]2CCCCN2C1=O InChI=1S/C34H49N5O6/c1-5-22(3)30-34(44)38-19-13-12-18-29(38)33(43)35-26(16-9-7-8-14-24(40)6-2)31(41)36-27(32(42)37-30)20-23-21-39(45-4)28-17-11-10-15-25(23)28/h10-11,15,17,21-22,26-27,29-30H,5-9,12-14,16,18-20H2,1-4H3,(H,35,43)(H,36,41)(H,37,42)/t22-,26-,27-,29+,30-/m0/s1 JWOGUUIOCYMBPV-GMFLJSBRSA-N 50238632 (6S,9S,12S,14aR)-6-((S)-sec-Butyl)-9-(1-methoxy-1H-indol-3-ylmethyl)-12-(6-oxo-octyl)-decahydro-4a,7,10,13-tetraaza-benzocyclododecene-5,8,11,14-tetraone::CHEMBL430060::ChEMBL_275631 Histone deacetylase 4 Homo sapiens 2.4 ChEMBL 10.1073/pnas.0706487104 10.7270/Q2C82B5X 17956988 Lahm, A; Paolini, C; Pallaoro, M; Nardi, MC; Jones, P; Neddermann, P; Sambucini, S; Bottomley, MJ; Lo Surdo, P; Carfi, A; Koch, U; De Francesco, R; Steinkuhler, C; Gallinari, P Istituto di Ricerche di Biologia Molecolare http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50238632 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50238632&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6918328 104056492 CHEMBL430060 ZINC17654900 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50872145 OCCN(CCc1c[nH]c2ccccc12)Cc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C22H25N3O3/c26-14-13-25(12-11-19-15-23-21-4-2-1-3-20(19)21)16-18-7-5-17(6-8-18)9-10-22(27)24-28/h1-10,15,23,26,28H,11-14,16H2,(H,24,27)/b10-9+ BWDQBBCUWLSASG-MDZDMXLPSA-N 19428 (2E)-N-hydroxy-3-(4-{[(2-hydroxyethyl)[2-(1H-indol-3-yl)ethyl]amino]methyl}phenyl)prop-2-enamide::(E)-N-hydroxy-3-[4-[[2-hydroxyethyl-[2-(1H-indol-3-yl)ethyl]amino]methyl]phenyl]prop-2-enamide::CHEMBL356066::Dacinostat::LAQ-824::NVP-LAQ824 Histone deacetylase 4 Homo sapiens 1 ChEMBL 10.1073/pnas.0706487104 10.7270/Q2C82B5X 17956988 Lahm, A; Paolini, C; Pallaoro, M; Nardi, MC; Jones, P; Neddermann, P; Sambucini, S; Bottomley, MJ; Lo Surdo, P; Carfi, A; Koch, U; De Francesco, R; Steinkuhler, C; Gallinari, P Istituto di Ricerche di Biologia Molecolare http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19428 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19428&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6445533 46519450 CHEMBL356066 ZINC01494627 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50872146 CC[C@H](C)[C@@H]1NC(=O)[C@H](Cc2cn(OC)c3ccccc23)NC(=O)[C@H](CCCCCC(=O)CC)NC(=O)[C@H]2CCCCN2C1=O InChI=1S/C34H49N5O6/c1-5-22(3)30-34(44)38-19-13-12-18-29(38)33(43)35-26(16-9-7-8-14-24(40)6-2)31(41)36-27(32(42)37-30)20-23-21-39(45-4)28-17-11-10-15-25(23)28/h10-11,15,17,21-22,26-27,29-30H,5-9,12-14,16,18-20H2,1-4H3,(H,35,43)(H,36,41)(H,37,42)/t22-,26-,27-,29+,30-/m0/s1 JWOGUUIOCYMBPV-GMFLJSBRSA-N 50238632 (6S,9S,12S,14aR)-6-((S)-sec-Butyl)-9-(1-methoxy-1H-indol-3-ylmethyl)-12-(6-oxo-octyl)-decahydro-4a,7,10,13-tetraaza-benzocyclododecene-5,8,11,14-tetraone::CHEMBL430060::ChEMBL_275631 Histone deacetylase 4 Homo sapiens 1.2 ChEMBL 10.1073/pnas.0706487104 10.7270/Q2C82B5X 17956988 Lahm, A; Paolini, C; Pallaoro, M; Nardi, MC; Jones, P; Neddermann, P; Sambucini, S; Bottomley, MJ; Lo Surdo, P; Carfi, A; Koch, U; De Francesco, R; Steinkuhler, C; Gallinari, P Istituto di Ricerche di Biologia Molecolare http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50238632 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50238632&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6918328 104056492 CHEMBL430060 ZINC17654900 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50872147 OCCN(CCc1c[nH]c2ccccc12)Cc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C22H25N3O3/c26-14-13-25(12-11-19-15-23-21-4-2-1-3-20(19)21)16-18-7-5-17(6-8-18)9-10-22(27)24-28/h1-10,15,23,26,28H,11-14,16H2,(H,24,27)/b10-9+ BWDQBBCUWLSASG-MDZDMXLPSA-N 19428 (2E)-N-hydroxy-3-(4-{[(2-hydroxyethyl)[2-(1H-indol-3-yl)ethyl]amino]methyl}phenyl)prop-2-enamide::(E)-N-hydroxy-3-[4-[[2-hydroxyethyl-[2-(1H-indol-3-yl)ethyl]amino]methyl]phenyl]prop-2-enamide::CHEMBL356066::Dacinostat::LAQ-824::NVP-LAQ824 Histone deacetylase 4 Homo sapiens 3 ChEMBL 10.1073/pnas.0706487104 10.7270/Q2C82B5X 17956988 Lahm, A; Paolini, C; Pallaoro, M; Nardi, MC; Jones, P; Neddermann, P; Sambucini, S; Bottomley, MJ; Lo Surdo, P; Carfi, A; Koch, U; De Francesco, R; Steinkuhler, C; Gallinari, P Istituto di Ricerche di Biologia Molecolare http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19428 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19428&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6445533 46519450 CHEMBL356066 ZINC01494627 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50872148 OCCN(CCc1c[nH]c2ccccc12)Cc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C22H25N3O3/c26-14-13-25(12-11-19-15-23-21-4-2-1-3-20(19)21)16-18-7-5-17(6-8-18)9-10-22(27)24-28/h1-10,15,23,26,28H,11-14,16H2,(H,24,27)/b10-9+ BWDQBBCUWLSASG-MDZDMXLPSA-N 19428 (2E)-N-hydroxy-3-(4-{[(2-hydroxyethyl)[2-(1H-indol-3-yl)ethyl]amino]methyl}phenyl)prop-2-enamide::(E)-N-hydroxy-3-[4-[[2-hydroxyethyl-[2-(1H-indol-3-yl)ethyl]amino]methyl]phenyl]prop-2-enamide::CHEMBL356066::Dacinostat::LAQ-824::NVP-LAQ824 Histone deacetylase 4 Homo sapiens 2.5 ChEMBL 10.1073/pnas.0706487104 10.7270/Q2C82B5X 17956988 Lahm, A; Paolini, C; Pallaoro, M; Nardi, MC; Jones, P; Neddermann, P; Sambucini, S; Bottomley, MJ; Lo Surdo, P; Carfi, A; Koch, U; De Francesco, R; Steinkuhler, C; Gallinari, P Istituto di Ricerche di Biologia Molecolare http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19428 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19428&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6445533 46519450 CHEMBL356066 ZINC01494627 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50872149 CC[C@@H](C)[C@H](NC(=O)[C@@H](N)Cc1cn(OC)c2ccccc12)C(=O)N1CCCC[C@@H]1C(=O)N[C@@H](CCCCCC(=O)CC)C(O)=O InChI=1S/C34H51N5O7/c1-5-22(3)30(37-31(41)26(35)20-23-21-39(46-4)28-17-11-10-15-25(23)28)33(43)38-19-13-12-18-29(38)32(42)36-27(34(44)45)16-9-7-8-14-24(40)6-2/h10-11,15,17,21-22,26-27,29-30H,5-9,12-14,16,18-20,35H2,1-4H3,(H,36,42)(H,37,41)(H,44,45)/t22-,26+,27+,29-,30+/m1/s1 WGYDJUMLABBZSI-VWIQTCEGSA-N 50377931 CHEMBL1791402 Histone deacetylase 4 Homo sapiens 152 ChEMBL 10.1073/pnas.0706487104 10.7270/Q2C82B5X 17956988 Lahm, A; Paolini, C; Pallaoro, M; Nardi, MC; Jones, P; Neddermann, P; Sambucini, S; Bottomley, MJ; Lo Surdo, P; Carfi, A; Koch, U; De Francesco, R; Steinkuhler, C; Gallinari, P Istituto di Ricerche di Biologia Molecolare http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50377931 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50377931&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56664649 160857014 CHEMBL1791402 ZINC44352103 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50872150 CC[C@@H](C)[C@H](NC(=O)[C@@H](N)Cc1cn(OC)c2ccccc12)C(=O)N1CCCC[C@@H]1C(=O)N[C@@H](CCCCCC(=O)CC)C(O)=O InChI=1S/C34H51N5O7/c1-5-22(3)30(37-31(41)26(35)20-23-21-39(46-4)28-17-11-10-15-25(23)28)33(43)38-19-13-12-18-29(38)32(42)36-27(34(44)45)16-9-7-8-14-24(40)6-2/h10-11,15,17,21-22,26-27,29-30H,5-9,12-14,16,18-20,35H2,1-4H3,(H,36,42)(H,37,41)(H,44,45)/t22-,26+,27+,29-,30+/m1/s1 WGYDJUMLABBZSI-VWIQTCEGSA-N 50377931 CHEMBL1791402 Histone deacetylase 4 Homo sapiens 88 ChEMBL 10.1073/pnas.0706487104 10.7270/Q2C82B5X 17956988 Lahm, A; Paolini, C; Pallaoro, M; Nardi, MC; Jones, P; Neddermann, P; Sambucini, S; Bottomley, MJ; Lo Surdo, P; Carfi, A; Koch, U; De Francesco, R; Steinkuhler, C; Gallinari, P Istituto di Ricerche di Biologia Molecolare http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50377931 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50377931&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56664649 160857014 CHEMBL1791402 ZINC44352103 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50856849 CC(=O)Nc1ccc(cc1)C(=O)Nc1cc(ccc1N)-c1cccs1 InChI=1S/C19H17N3O2S/c1-12(23)21-15-7-4-13(5-8-15)19(24)22-17-11-14(6-9-16(17)20)18-3-2-10-25-18/h2-11H,20H2,1H3,(H,21,23)(H,22,24) ABZSPJVXTTUFAA-UHFFFAOYSA-N 19423 HDAC inhibitor, Compound 1::N-[2-amino-5-(thiophen-2-yl)phenyl]-4-acetamidobenzamide::N-[2-amino-5-(thiophen-2-yl)phenyl]-4-acetamidobenzamide (60)::SHI-1:2::benzamide-type inhibitor, 19 Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.1021/jm7011408 10.7270/Q2M32WMT 18247554 Paris, M; Porcelloni, M; Binaschi, M; Fattori, D Menarini Ricerche http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19423 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19423&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 20Y 4LY1 6918878 46519445 ZINC14970815 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50867777 Nc1ccccc1NC(=O)c1ccc(CSc2nc(cc(=O)[nH]2)-c2ccccc2)cc1 InChI=1S/C24H20N4O2S/c25-19-8-4-5-9-20(19)26-23(30)18-12-10-16(11-13-18)15-31-24-27-21(14-22(29)28-24)17-6-2-1-3-7-17/h1-14H,15,25H2,(H,26,30)(H,27,28,29) DDFXLJZLWDEHBH-UHFFFAOYSA-N 50376851 CHEMBL259127 Histone deacetylase 4 Homo sapiens 125000 ChEMBL 10.1016/j.bmcl.2008.03.055 10.7270/Q2930V17 18381238 Mai, A; Perrone, A; Nebbioso, A; Rotili, D; Valente, S; Tardugno, M; Massa, S; De Bellis, F; Altucci, L Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50376851 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50376851&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25010205 160855934 CHEMBL259127 ZINC29052796 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50867779 Nc1ccccc1NC(=O)c1ccc(CNC(=O)OCc2cccnc2)cc1 InChI=1S/C21H20N4O3/c22-18-5-1-2-6-19(18)25-20(26)17-9-7-15(8-10-17)13-24-21(27)28-14-16-4-3-11-23-12-16/h1-12H,13-14,22H2,(H,24,27)(H,25,26) INVTYAOGFAGBOE-UHFFFAOYSA-N 19410 CHEMBL27759::MS-275::US11377423, MS-275::US11672788, Compound Entinostat::US9265734, MS-275::US9796664, Compound MS-275::benzamide-type inhibitor, 3::pyridin-3-ylmethyl N-({4-[(2-aminophenyl)carbamoyl]phenyl}methyl)carbamate Histone deacetylase 4 Homo sapiens 142000 ChEMBL 10.1016/j.bmcl.2008.03.055 10.7270/Q2930V17 18381238 Mai, A; Perrone, A; Nebbioso, A; Rotili, D; Valente, S; Tardugno, M; Massa, S; De Bellis, F; Altucci, L Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19410 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19410&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4261 46519433 CHEMBL27759 7007 ZINC01488870 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50860834 Nc1ccc(cc1NC(=O)c1ccccc1)-c1cccs1 InChI=1S/C17H14N2OS/c18-14-9-8-13(16-7-4-10-21-16)11-15(14)19-17(20)12-5-2-1-3-6-12/h1-11H,18H2,(H,19,20) UVIOPWAIOGENCM-UHFFFAOYSA-N 50374007 CHEMBL271949 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2007.12.031 10.7270/Q2765G5S 18182289 Methot, JL; Chakravarty, PK; Chenard, M; Close, J; Cruz, JC; Dahlberg, WK; Fleming, J; Hamblett, CL; Hamill, JE; Harrington, P; Harsch, A; Heidebrecht, R; Hughes, B; Jung, J; Kenific, CM; Kral, AM; Meinke, PT; Middleton, RE; Ozerova, N; Sloman, DL; Stanton, MG; Szewczak, AA; Tyagarajan, S; Witter, DJ; Secrist, JP; Miller, TA Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50374007 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50374007&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44454144 160853108 CHEMBL271949 ZINC29126955 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50860835 Nc1ccc(cc1NC(=O)c1cccnc1)-c1cccs1 InChI=1S/C16H13N3OS/c17-13-6-5-11(15-4-2-8-21-15)9-14(13)19-16(20)12-3-1-7-18-10-12/h1-10H,17H2,(H,19,20) VHWNADCYYRKHOX-UHFFFAOYSA-N 50232034 CHEMBL256440::N-(2-amino-5-(thiophen-2-yl)phenyl)nicotinamide Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2007.12.031 10.7270/Q2765G5S 18182289 Methot, JL; Chakravarty, PK; Chenard, M; Close, J; Cruz, JC; Dahlberg, WK; Fleming, J; Hamblett, CL; Hamill, JE; Harrington, P; Harsch, A; Heidebrecht, R; Hughes, B; Jung, J; Kenific, CM; Kral, AM; Meinke, PT; Middleton, RE; Ozerova, N; Sloman, DL; Stanton, MG; Szewczak, AA; Tyagarajan, S; Witter, DJ; Secrist, JP; Miller, TA Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50232034 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50232034&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44454416 104055387 CHEMBL256440 ZINC29127438 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50869055 CC(C=CC(=O)NO)C=C(C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20) ALCVRKZFLFWUAZ-UHFFFAOYSA-N 19130 (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide::CHEMBL99::TSA::Trichostatin A (TSA) Histone deacetylase 4 Homo sapiens 62.9 ChEMBL 10.1016/j.bmcl.2008.03.053 10.7270/Q20G3M1G 18397826 Nakao, Y; Narazaki, G; Hoshino, T; Maeda, S; Yoshida, M; Maejima, H; Yamashita, JK Waseda University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19130 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19130&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 91895926 46519165 46024 CHEMBL99 7005 ZINC05579377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50869056 CC(C)[C@H]1NC(=O)[C@@H](C)[C@@H](CC=CCCC(O)=O)NC(=O)[C@@H](Cc2ccccc2)NC(=O)[C@@H](C)NC1=O InChI=1S/C27H38N4O6/c1-16(2)23-27(37)28-18(4)25(35)30-21(15-19-11-7-5-8-12-19)26(36)29-20(17(3)24(34)31-23)13-9-6-10-14-22(32)33/h5-9,11-12,16-18,20-21,23H,10,13-15H2,1-4H3,(H,28,37)(H,29,36)(H,30,35)(H,31,34)(H,32,33)/t17-,18+,20+,21+,23+/m0/s1 DMXROUYLQHFRCS-VIDCAOJFSA-N 50372469 AZUMAMIDE E Histone deacetylase 4 Homo sapiens 2280 ChEMBL 10.1016/j.bmcl.2008.03.053 10.7270/Q20G3M1G 18397826 Nakao, Y; Narazaki, G; Hoshino, T; Maeda, S; Yoshida, M; Maejima, H; Yamashita, JK Waseda University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50372469 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50372469&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 16095101 160851570 ZINC13974757 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50869057 CC(C)[C@H]1NC(=O)[C@@H](C)[C@@H](CC=CCCC(O)=O)NC(=O)[C@@H](Cc2ccc(O)cc2)NC(=O)[C@@H](C)NC1=O InChI=1S/C27H38N4O7/c1-15(2)23-27(38)28-17(4)25(36)30-21(14-18-10-12-19(32)13-11-18)26(37)29-20(16(3)24(35)31-23)8-6-5-7-9-22(33)34/h5-6,10-13,15-17,20-21,23,32H,7-9,14H2,1-4H3,(H,28,38)(H,29,37)(H,30,36)(H,31,35)(H,33,34)/t16-,17+,20+,21+,23+/m0/s1 QKNOLJBQLJGNKI-CGNYWNNHSA-N 50377384 AZUMAMIDE C Histone deacetylase 4 Homo sapiens 3160 ChEMBL 10.1016/j.bmcl.2008.03.053 10.7270/Q20G3M1G 18397826 Nakao, Y; Narazaki, G; Hoshino, T; Maeda, S; Yoshida, M; Maejima, H; Yamashita, JK Waseda University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50377384 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50377384&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 16095114 160856467 ZINC14858639 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50869058 CC(C)[C@H]1NC(=O)[C@@H](C)[C@@H](CC=CCCC(N)=O)NC(=O)[C@@H](Cc2ccc(O)cc2)NC(=O)[C@@H](C)NC1=O InChI=1S/C27H39N5O6/c1-15(2)23-27(38)29-17(4)25(36)31-21(14-18-10-12-19(33)13-11-18)26(37)30-20(16(3)24(35)32-23)8-6-5-7-9-22(28)34/h5-6,10-13,15-17,20-21,23,33H,7-9,14H2,1-4H3,(H2,28,34)(H,29,38)(H,30,37)(H,31,36)(H,32,35)/t16-,17+,20+,21+,23+/m0/s1 RFGAANHNJBCQAS-CGNYWNNHSA-N 50377383 AZUMAMIDE B Histone deacetylase 4 Homo sapiens 3660 ChEMBL 10.1016/j.bmcl.2008.03.053 10.7270/Q20G3M1G 18397826 Nakao, Y; Narazaki, G; Hoshino, T; Maeda, S; Yoshida, M; Maejima, H; Yamashita, JK Waseda University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50377383 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50377383&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 16095112 160856466 ZINC14858635 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50869064 C[C@H]1NC(=O)[C@@H](C)[C@@H](CC=CCCC(N)=O)NC(=O)[C@@H](Cc2ccccc2)NC(=O)[C@@H](C)NC1=O InChI=1S/C25H35N5O5/c1-15-19(12-8-5-9-13-21(26)31)29-25(35)20(14-18-10-6-4-7-11-18)30-24(34)17(3)28-23(33)16(2)27-22(15)32/h4-8,10-11,15-17,19-20H,9,12-14H2,1-3H3,(H2,26,31)(H,27,32)(H,28,33)(H,29,35)(H,30,34)/t15-,16+,17+,19+,20+/m0/s1 CTSOUSRCWCZQCB-AZNNDXHDSA-N 50377382 AZUMAMIDE D Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2008.03.053 10.7270/Q20G3M1G 18397826 Nakao, Y; Narazaki, G; Hoshino, T; Maeda, S; Yoshida, M; Maejima, H; Yamashita, JK Waseda University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50377382 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50377382&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 16095113 160856465 ZINC14858643 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50869067 CC(C)[C@H]1NC(=O)[C@@H](C)[C@@H](CC=CCCC(N)=O)NC(=O)[C@@H](Cc2ccccc2)NC(=O)[C@@H](C)NC1=O InChI=1S/C27H39N5O5/c1-16(2)23-27(37)29-18(4)25(35)31-21(15-19-11-7-5-8-12-19)26(36)30-20(17(3)24(34)32-23)13-9-6-10-14-22(28)33/h5-9,11-12,16-18,20-21,23H,10,13-15H2,1-4H3,(H2,28,33)(H,29,37)(H,30,36)(H,31,35)(H,32,34)/t17-,18+,20+,21+,23+/m0/s1 VADNNPZELPREQB-VIDCAOJFSA-N 50377385 AZUMAMIDE A Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2008.03.053 10.7270/Q20G3M1G 18397826 Nakao, Y; Narazaki, G; Hoshino, T; Maeda, S; Yoshida, M; Maejima, H; Yamashita, JK Waseda University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50377385 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50377385&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 16095102 160856468 ZINC13974761 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50860865 CC(=O)Nc1ccc(cc1)C(=O)Nc1cc(ccc1N)-c1cccs1 InChI=1S/C19H17N3O2S/c1-12(23)21-15-7-4-13(5-8-15)19(24)22-17-11-14(6-9-16(17)20)18-3-2-10-25-18/h2-11H,20H2,1H3,(H,21,23)(H,22,24) ABZSPJVXTTUFAA-UHFFFAOYSA-N 19423 HDAC inhibitor, Compound 1::N-[2-amino-5-(thiophen-2-yl)phenyl]-4-acetamidobenzamide::N-[2-amino-5-(thiophen-2-yl)phenyl]-4-acetamidobenzamide (60)::SHI-1:2::benzamide-type inhibitor, 19 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.bmcl.2007.12.031 10.7270/Q2765G5S 18182289 Methot, JL; Chakravarty, PK; Chenard, M; Close, J; Cruz, JC; Dahlberg, WK; Fleming, J; Hamblett, CL; Hamill, JE; Harrington, P; Harsch, A; Heidebrecht, R; Hughes, B; Jung, J; Kenific, CM; Kral, AM; Meinke, PT; Middleton, RE; Ozerova, N; Sloman, DL; Stanton, MG; Szewczak, AA; Tyagarajan, S; Witter, DJ; Secrist, JP; Miller, TA Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19423 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19423&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 20Y 4LY1 6918878 46519445 ZINC14970815 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50860910 C[C@H]1CN(CCN1C(=O)OCc1ccccc1)c1ccc(cn1)C(=O)Nc1cc(ccc1N)-c1ccccc1 InChI=1S/C31H31N5O3/c1-22-20-35(16-17-36(22)31(38)39-21-23-8-4-2-5-9-23)29-15-13-26(19-33-29)30(37)34-28-18-25(12-14-27(28)32)24-10-6-3-7-11-24/h2-15,18-19,22H,16-17,20-21,32H2,1H3,(H,34,37)/t22-/m0/s1 KESMZCYRWONIJD-QFIPXVFZSA-N 50374011 CHEMBL437029 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2007.12.031 10.7270/Q2765G5S 18182289 Methot, JL; Chakravarty, PK; Chenard, M; Close, J; Cruz, JC; Dahlberg, WK; Fleming, J; Hamblett, CL; Hamill, JE; Harrington, P; Harsch, A; Heidebrecht, R; Hughes, B; Jung, J; Kenific, CM; Kral, AM; Meinke, PT; Middleton, RE; Ozerova, N; Sloman, DL; Stanton, MG; Szewczak, AA; Tyagarajan, S; Witter, DJ; Secrist, JP; Miller, TA Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50374011 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50374011&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 16663079 160853112 CHEMBL437029 ZINC29126912 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50860915 Nc1ccccc1NC(=O)c1cccnc1 InChI=1S/C12H11N3O/c13-10-5-1-2-6-11(10)15-12(16)9-4-3-7-14-8-9/h1-8H,13H2,(H,15,16) CEZRXCCXPZWXNX-UHFFFAOYSA-N 50220259 CHEMBL236678::N-(2-aminophenyl)nicotinamide Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2007.12.031 10.7270/Q2765G5S 18182289 Methot, JL; Chakravarty, PK; Chenard, M; Close, J; Cruz, JC; Dahlberg, WK; Fleming, J; Hamblett, CL; Hamill, JE; Harrington, P; Harsch, A; Heidebrecht, R; Hughes, B; Jung, J; Kenific, CM; Kral, AM; Meinke, PT; Middleton, RE; Ozerova, N; Sloman, DL; Stanton, MG; Szewczak, AA; Tyagarajan, S; Witter, DJ; Secrist, JP; Miller, TA Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50220259 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50220259&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1133083 104093300 CHEMBL236678 ZINC00873967 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50860920 Nc1ccc(cc1NC(=O)c1ccccc1)-c1ccccc1 InChI=1S/C19H16N2O/c20-17-12-11-16(14-7-3-1-4-8-14)13-18(17)21-19(22)15-9-5-2-6-10-15/h1-13H,20H2,(H,21,22) ZWLFHHHQRUYIBT-UHFFFAOYSA-N 50232053 CHEMBL271741::N-(4-amino-biphenyl-3-yl)-benzamide::N-(4-aminobiphenyl-3-yl)benzamide Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2007.12.031 10.7270/Q2765G5S 18182289 Methot, JL; Chakravarty, PK; Chenard, M; Close, J; Cruz, JC; Dahlberg, WK; Fleming, J; Hamblett, CL; Hamill, JE; Harrington, P; Harsch, A; Heidebrecht, R; Hughes, B; Jung, J; Kenific, CM; Kral, AM; Meinke, PT; Middleton, RE; Ozerova, N; Sloman, DL; Stanton, MG; Szewczak, AA; Tyagarajan, S; Witter, DJ; Secrist, JP; Miller, TA Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50232053 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50232053&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search LLX 3MAX 44454143 104055390 CHEMBL271741 ZINC29126954 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50860921 Nc1ccccc1NC(=O)c1ccccc1 InChI=1S/C13H12N2O/c14-11-8-4-5-9-12(11)15-13(16)10-6-2-1-3-7-10/h1-9H,14H2,(H,15,16) RFDVMOUXHKTCDO-UHFFFAOYSA-N 50232046 CHEMBL405072::N-(2-aminophenyl)benzamide Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2007.12.031 10.7270/Q2765G5S 18182289 Methot, JL; Chakravarty, PK; Chenard, M; Close, J; Cruz, JC; Dahlberg, WK; Fleming, J; Hamblett, CL; Hamill, JE; Harrington, P; Harsch, A; Heidebrecht, R; Hughes, B; Jung, J; Kenific, CM; Kral, AM; Meinke, PT; Middleton, RE; Ozerova, N; Sloman, DL; Stanton, MG; Szewczak, AA; Tyagarajan, S; Witter, DJ; Secrist, JP; Miller, TA Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50232046 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50232046&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 759408 104055389 CHEMBL405072 ZINC00225957 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50860922 Nc1ccc(cc1NC(=O)c1cccnc1)-c1ccccc1 InChI=1S/C18H15N3O/c19-16-9-8-14(13-5-2-1-3-6-13)11-17(16)21-18(22)15-7-4-10-20-12-15/h1-12H,19H2,(H,21,22) RAJXTGVDLBIWMD-UHFFFAOYSA-N 50232035 CHEMBL255805::N-(4-amino-biphenyl-3-yl)-nicotinamide::N-(4-aminobiphenyl-3-yl)nicotinamide Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2007.12.031 10.7270/Q2765G5S 18182289 Methot, JL; Chakravarty, PK; Chenard, M; Close, J; Cruz, JC; Dahlberg, WK; Fleming, J; Hamblett, CL; Hamill, JE; Harrington, P; Harsch, A; Heidebrecht, R; Hughes, B; Jung, J; Kenific, CM; Kral, AM; Meinke, PT; Middleton, RE; Ozerova, N; Sloman, DL; Stanton, MG; Szewczak, AA; Tyagarajan, S; Witter, DJ; Secrist, JP; Miller, TA Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50232035 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50232035&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44454415 104055388 CHEMBL255805 ZINC29127437 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50860935 Oc1ccc(cc1NC(=O)c1ccccc1)-c1ccccc1 InChI=1S/C19H15NO2/c21-18-12-11-16(14-7-3-1-4-8-14)13-17(18)20-19(22)15-9-5-2-6-10-15/h1-13,21H,(H,20,22) INXWGOLWSBWSOQ-UHFFFAOYSA-N 50232005 CHEMBL269935::N-(4-hydroxy-biphenyl-3-yl)-benzamide::N-(4-hydroxybiphenyl-3-yl)benzamide Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2007.12.031 10.7270/Q2765G5S 18182289 Methot, JL; Chakravarty, PK; Chenard, M; Close, J; Cruz, JC; Dahlberg, WK; Fleming, J; Hamblett, CL; Hamill, JE; Harrington, P; Harsch, A; Heidebrecht, R; Hughes, B; Jung, J; Kenific, CM; Kral, AM; Meinke, PT; Middleton, RE; Ozerova, N; Sloman, DL; Stanton, MG; Szewczak, AA; Tyagarajan, S; Witter, DJ; Secrist, JP; Miller, TA Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50232005 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50232005&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44454650 104055386 CHEMBL269935 ZINC29127807 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50879076 COc1ccc2[nH]c(C)c(CC(=O)N[C@@H](CCCCCC(C)=O)c3nc(c[nH]3)-c3ccccc3)c2c1 InChI=1S/C29H34N4O3/c1-19(34)10-6-4-9-13-26(29-30-18-27(33-29)21-11-7-5-8-12-21)32-28(35)17-23-20(2)31-25-15-14-22(36-3)16-24(23)25/h5,7-8,11-12,14-16,18,26,31H,4,6,9-10,13,17H2,1-3H3,(H,30,33)(H,32,35)/t26-/m0/s1 DBOGSXSBFWKDRX-SANMLTNESA-N 25146 2-(5-methoxy-2-methyl-1H-indol-3-yl)-N-[(1S)-7-oxo-1-(5-phenyl-1H-imidazol-2-yl)octyl]acetamide::4-phenylimidazole, 17::CHEMBL407959 Histone deacetylase 4 Homo sapiens >1 ChEMBL 10.1016/j.bmcl.2008.09.003 10.7270/Q24T6K81 18809328 Pescatore, G; Kinzel, O; Attenni, B; Cecchetti, O; Fiore, F; Fonsi, M; Rowley, M; Schultz-Fademrecht, C; Serafini, S; Steinkuhler, C; Jones, P IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25146 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25146&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 24853793 56374287 CHEMBL407959 ZINC29054657 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50879077 CN1CCC(CC1)C(=O)N[C@@H](CCCCCC(C)=O)c1nc(c[nH]1)-c1ccc2ccccc2c1 InChI=1S/C28H36N4O2/c1-20(33)8-4-3-5-11-25(31-28(34)22-14-16-32(2)17-15-22)27-29-19-26(30-27)24-13-12-21-9-6-7-10-23(21)18-24/h6-7,9-10,12-13,18-19,22,25H,3-5,8,11,14-17H2,1-2H3,(H,29,30)(H,31,34)/t25-/m0/s1 PFMPKMYQXOCJMI-VWLOTQADSA-N 50258539 (S)-1-methyl-N-(1-(5-(naphthalen-2-yl)-1H-imidazol-2-yl)-7-oxooctyl)piperidine-4-carboxamide::CHEMBL468513 Histone deacetylase 4 Homo sapiens >1 ChEMBL 10.1016/j.bmcl.2008.09.003 10.7270/Q24T6K81 18809328 Pescatore, G; Kinzel, O; Attenni, B; Cecchetti, O; Fiore, F; Fonsi, M; Rowley, M; Schultz-Fademrecht, C; Serafini, S; Steinkuhler, C; Jones, P IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50258539 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50258539&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 16049824 104109187 CHEMBL468513 ZINC34947211 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50879078 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >1 ChEMBL 10.1016/j.bmcl.2008.09.003 10.7270/Q24T6K81 18809328 Pescatore, G; Kinzel, O; Attenni, B; Cecchetti, O; Fiore, F; Fonsi, M; Rowley, M; Schultz-Fademrecht, C; Serafini, S; Steinkuhler, C; Jones, P IRBM/Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50921451 CCCC(O)=O InChI=1S/C4H8O2/c1-2-3-4(5)6/h2-3H2,1H3,(H,5,6) FERIUCNNQQJTOY-UHFFFAOYSA-N 26109 Butyrate::butanoic acid::butanoic acid, 4 Histone deacetylase 4 Homo sapiens >2000000 ChEMBL 10.1021/ml1001954 10.7270/Q2TH8NQJ 21874153 Fass, DM; Shah, R; Ghosh, B; Hennig, K; Norton, S; Zhao, WN; Reis, SA; Klein, PS; Mazitschek, R; Maglathlin, RL; Lewis, TA; Haggarty, SJ Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=26109 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=26109&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search BUA 3UMQ,6KSL,6KSM,6KSI,5VNW,3VPD,3I3F,6UQV,3DLT,7SL9,5GRO,4UHF,6LPY,7CIP,4MZL,1ZRM,5AOB,1UGP,2HA7,2CZ0,7W8N,2J4C,2CZ1,1P0I,4QSF,3WWC,1UK7 264 56464546 50329 DB03568 1059 C00246 ZINC00895132 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50921460 CCCC(=O)NO InChI=1S/C4H9NO2/c1-2-3-4(6)5-7/h7H,2-3H2,1H3,(H,5,6) CCBCHURBDSNSTJ-UHFFFAOYSA-N 50336883 Butyrylhydroxamic acid::CHEMBL1672332 Histone deacetylase 4 Homo sapiens >2000000 ChEMBL 10.1021/ml1001954 10.7270/Q2TH8NQJ 21874153 Fass, DM; Shah, R; Ghosh, B; Hennig, K; Norton, S; Zhao, WN; Reis, SA; Klein, PS; Mazitschek, R; Maglathlin, RL; Lewis, TA; Haggarty, SJ Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50336883 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50336883&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 419176 125086985 CHEMBL1672332 ZINC04809144 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50921469 [O-]C(=O)CCCc1ccccc1 InChI=1S/C10H12O2/c11-10(12)8-4-7-9-5-2-1-3-6-9/h1-3,5-6H,4,7-8H2,(H,11,12)/p-1 OBKXEAXTFZPCHS-UHFFFAOYSA-M 36184 4-phenylbutanoate Histone deacetylase 4 Homo sapiens >2000000 ChEMBL 10.1021/ml1001954 10.7270/Q2TH8NQJ 21874153 Fass, DM; Shah, R; Ghosh, B; Hennig, K; Norton, S; Zhao, WN; Reis, SA; Klein, PS; Mazitschek, R; Maglathlin, RL; Lewis, TA; Haggarty, SJ Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=36184 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=36184&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 22053264 103147831 75317 DB06819 ZINC00056568 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50921478 ONC(=O)CCCc1ccccc1 InChI=1S/C10H13NO2/c12-10(11-13)8-4-7-9-5-2-1-3-6-9/h1-3,5-6,13H,4,7-8H2,(H,11,12) UPHXPXYRKPCXHK-UHFFFAOYSA-N 50015142 4-Phenylbutyrohydroxamic acid::CHEMBL55895::N-Hydroxy-4-phenyl-butyramide Histone deacetylase 4 Homo sapiens 140000 ChEMBL 10.1021/ml1001954 10.7270/Q2TH8NQJ 21874153 Fass, DM; Shah, R; Ghosh, B; Hennig, K; Norton, S; Zhao, WN; Reis, SA; Klein, PS; Mazitschek, R; Maglathlin, RL; Lewis, TA; Haggarty, SJ Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50015142 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50015142&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4R9 7FJH 279980 103926985 CHEMBL55895 ZINC04962622 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50921487 CCCC(CCC)C(O)=O InChI=1S/C8H16O2/c1-3-5-7(6-4-2)8(9)10/h7H,3-6H2,1-2H3,(H,9,10) NIJJYAXOARWZEE-UHFFFAOYSA-N 50003616 2-n-propyl-n-valeric acid::CHEMBL109::DPA::Di-n-propylessigsaeure::VALPROIC ACID::Valproinsaeure::dipropylacetic acid::n-DPA Histone deacetylase 4 Homo sapiens >2000000 ChEMBL 10.1021/ml1001954 10.7270/Q2TH8NQJ 21874153 Fass, DM; Shah, R; Ghosh, B; Hennig, K; Norton, S; Zhao, WN; Reis, SA; Klein, PS; Mazitschek, R; Maglathlin, RL; Lewis, TA; Haggarty, SJ Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50003616 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50003616&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 2PP 1DIT 3121 103917584 39867 CHEMBL109 DB00313 7009 C07185 ZINC03008621 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50921496 CCCC(CCC)C(=O)NO InChI=1S/C8H17NO2/c1-3-5-7(6-4-2)8(10)9-11/h7,11H,3-6H2,1-2H3,(H,9,10) ROJGIRXXBBBMPL-UHFFFAOYSA-N 50336884 2-Propyl-pentanoic acid hydroxyamide::CHEMBL186311::Valpropylhydroxamic acid Histone deacetylase 4 Homo sapiens 170000 ChEMBL 10.1021/ml1001954 10.7270/Q2TH8NQJ 21874153 Fass, DM; Shah, R; Ghosh, B; Hennig, K; Norton, S; Zhao, WN; Reis, SA; Klein, PS; Mazitschek, R; Maglathlin, RL; Lewis, TA; Haggarty, SJ Broad Institute of Harvard and MIT http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50336884 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50336884&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 88129 125086986 CHEMBL186311 ZINC05298743 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50924603 CCC(=O)CCCCC[C@@H]1NC(=O)[C@H](C)NC(=O)C[C@H](CC(C)C)NC(=O)[C@H](Cc2cccc3ccccc23)NC1=O InChI=1S/C33H46N4O5/c1-5-26(38)15-7-6-8-17-28-32(41)37-29(19-24-14-11-13-23-12-9-10-16-27(23)24)33(42)35-25(18-21(2)3)20-30(39)34-22(4)31(40)36-28/h9-14,16,21-22,25,28-29H,5-8,15,17-20H2,1-4H3,(H,34,39)(H,35,42)(H,36,40)(H,37,41)/t22-,25-,28-,29-/m0/s1 HFDUFQFVUVYKCX-MQIQBBKZSA-N 50379131 CHEMBL2012815 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/ml200136e 10.7270/Q2GQ6ZRX 21984958 Hutt, DM; Olsen, CA; Vickers, CJ; Herman, D; Chalfant, M; Montero, A; Leman, LJ; Burkle, R; Maryanoff, BE; Balch, WE; Ghadiri, MR TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50379131 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50379131&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44598536 160858214 CHEMBL2012815 ZINC84602100 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50938283 Nc1ccccc1NC(=O)c1ccc(CNC(=O)OCc2cccnc2)cc1 InChI=1S/C21H20N4O3/c22-18-5-1-2-6-19(18)25-20(26)17-9-7-15(8-10-17)13-24-21(27)28-14-16-4-3-11-23-12-16/h1-12H,13-14,22H2,(H,24,27)(H,25,26) INVTYAOGFAGBOE-UHFFFAOYSA-N 19410 CHEMBL27759::MS-275::US11377423, MS-275::US11672788, Compound Entinostat::US9265734, MS-275::US9796664, Compound MS-275::benzamide-type inhibitor, 3::pyridin-3-ylmethyl N-({4-[(2-aminophenyl)carbamoyl]phenyl}methyl)carbamate Histone deacetylase 4 Homo sapiens 10700 ChEMBL 10.1016/j.ejmech.2012.03.058 10.7270/Q25M66QJ 22541394 Rajak, H; Kumar, P; Parmar, P; Thakur, BS; Veerasamy, R; Sharma, PC; Sharma, AK; Gupta, AK; Dangi, JS Guru Ghasidas University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19410 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19410&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4261 46519433 CHEMBL27759 7007 ZINC01488870 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50955463 NC(=O)c1ccccc1Nc1cccc(OCCc2ccccc2)c1 InChI=1S/C21H20N2O2/c22-21(24)19-11-4-5-12-20(19)23-17-9-6-10-18(15-17)25-14-13-16-7-2-1-3-8-16/h1-12,15,23H,13-14H2,(H2,22,24) VVRUXFPJOVUDCV-UHFFFAOYSA-N 50392111 CHEMBL2152613 Histone deacetylase 4 Homo sapiens >30000 ChEMBL 10.1021/jm3002108 10.7270/Q2WW7JRS 22642300 Suzuki, T; Khan, MN; Sawada, H; Imai, E; Itoh, Y; Yamatsuta, K; Tokuda, N; Takeuchi, J; Seko, T; Nakagawa, H; Miyata, N Kyoto Prefectural University of Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50392111 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50392111&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 8NO 5Y5N 56935695 163341135 CHEMBL2152613 ZINC95578829 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50972997 CN1C[C@H]([C@@H](C1)c1ccc(\C=C\C(=O)Nc2ccccc2N)cc1)C(=O)Nc1ccc(Cl)cc1 InChI=1S/C27H27ClN4O2/c1-32-16-22(23(17-32)27(34)30-21-13-11-20(28)12-14-21)19-9-6-18(7-10-19)8-15-26(33)31-25-5-3-2-4-24(25)29/h2-15,22-23H,16-17,29H2,1H3,(H,30,34)(H,31,33)/b15-8+/t22-,23+/m0/s1 CTJRRDKOXVXXEW-RNMWKOHKSA-N 50399005 CHEMBL2177588 Histone deacetylase 4 Homo sapiens 36000 ChEMBL 10.1021/jm3011838 10.7270/Q2TT4S3Q 23061376 Wong, JC; Tang, G; Wu, X; Liang, C; Zhang, Z; Guo, L; Peng, Z; Zhang, W; Lin, X; Wang, Z; Mei, J; Chen, J; Pan, S; Zhang, N; Liu, Y; Zhou, M; Feng, L; Zhao, W; Li, S; Zhang, C; Zhang, M; Rong, Y; Jin, TG; Zhang, X; Ren, S; Ji, Y; Zhao, R; She, J; Ren, Y; Xu, C; Chen, D; Cai, J; Shan, S; Pan, D; Ning, Z; Lu, X; Chen, T; He, Y; Chen, L Roche R & D Center China Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399005 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399005&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 59454252 163348029 CHEMBL2177588 ZINC95579813 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50972998 CN1C[C@@H]([C@H](C1)c1ccc(\C=C\C(=O)Nc2ccccc2N)cc1F)C(=O)Nc1ccc(Cl)cc1 InChI=1S/C27H26ClFN4O2/c1-33-15-21(22(16-33)27(35)31-19-10-8-18(28)9-11-19)20-12-6-17(14-23(20)29)7-13-26(34)32-25-5-3-2-4-24(25)30/h2-14,21-22H,15-16,30H2,1H3,(H,31,35)(H,32,34)/b13-7+/t21-,22+/m1/s1 PZYNOSYZPXJRNG-NAHVQIJJSA-N 50399004 CHEMBL2177582 Histone deacetylase 4 Homo sapiens 46000 ChEMBL 10.1021/jm3011838 10.7270/Q2TT4S3Q 23061376 Wong, JC; Tang, G; Wu, X; Liang, C; Zhang, Z; Guo, L; Peng, Z; Zhang, W; Lin, X; Wang, Z; Mei, J; Chen, J; Pan, S; Zhang, N; Liu, Y; Zhou, M; Feng, L; Zhao, W; Li, S; Zhang, C; Zhang, M; Rong, Y; Jin, TG; Zhang, X; Ren, S; Ji, Y; Zhao, R; She, J; Ren, Y; Xu, C; Chen, D; Cai, J; Shan, S; Pan, D; Ning, Z; Lu, X; Chen, T; He, Y; Chen, L Roche R & D Center China Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399004 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399004&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 59454220 163348028 CHEMBL2177582 ZINC95572157 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50972999 CN1C[C@@H]([C@H](C1)c1ccc(\C=C\C(=O)Nc2ccccc2N)cc1)C(=O)Nc1ccc(Cl)cc1 InChI=1S/C27H27ClN4O2/c1-32-16-22(23(17-32)27(34)30-21-13-11-20(28)12-14-21)19-9-6-18(7-10-19)8-15-26(33)31-25-5-3-2-4-24(25)29/h2-15,22-23H,16-17,29H2,1H3,(H,30,34)(H,31,33)/b15-8+/t22-,23+/m1/s1 CTJRRDKOXVXXEW-HNAOKYFASA-N 50399006 CHEMBL2177587 Histone deacetylase 4 Homo sapiens 13000 ChEMBL 10.1021/jm3011838 10.7270/Q2TT4S3Q 23061376 Wong, JC; Tang, G; Wu, X; Liang, C; Zhang, Z; Guo, L; Peng, Z; Zhang, W; Lin, X; Wang, Z; Mei, J; Chen, J; Pan, S; Zhang, N; Liu, Y; Zhou, M; Feng, L; Zhao, W; Li, S; Zhang, C; Zhang, M; Rong, Y; Jin, TG; Zhang, X; Ren, S; Ji, Y; Zhao, R; She, J; Ren, Y; Xu, C; Chen, D; Cai, J; Shan, S; Pan, D; Ning, Z; Lu, X; Chen, T; He, Y; Chen, L Roche R & D Center China Ltd http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399006 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399006&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 46896338 163348030 CHEMBL2177587 ZINC95578073 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50960713 CC(=O)SCCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@H](CCOCCSC(C)=O)NC(=O)C(C)(C)NC1=O InChI=1S/C26H42N4O7S2/c1-17(31)38-15-7-5-6-9-19-22(33)29-26(3,4)25(36)28-20(11-13-37-14-16-39-18(2)32)24(35)30-12-8-10-21(30)23(34)27-19/h19-21H,5-16H2,1-4H3,(H,27,34)(H,28,36)(H,29,33)/t19-,20-,21+/m0/s1 DUABJLZESSBUAG-PCCBWWKXSA-N 50394108 CHEMBL2158744 Histone deacetylase 4 Homo sapiens 120 ChEMBL 10.1016/j.bmcl.2012.03.004 10.7270/Q26M37XT 23021104 Hoque, MA; Arai, T; Nishino, N; Kim, HJ; Ito, A; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50394108 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50394108&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71462097 163343132 CHEMBL2158744 C04334 ZINC95573205 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50960714 CC(=O)SCCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@H](CCCCCSC(C)=O)NC(=O)C(C)(C)NC1=O InChI=1S/C27H44N4O6S2/c1-18(32)38-16-9-5-7-12-20-23(34)30-27(3,4)26(37)29-21(13-8-6-10-17-39-19(2)33)25(36)31-15-11-14-22(31)24(35)28-20/h20-22H,5-17H2,1-4H3,(H,28,35)(H,29,37)(H,30,34)/t20-,21-,22+/m0/s1 FISBIMNWLAHVKP-FDFHNCONSA-N 50394109 CHEMBL2158743 Histone deacetylase 4 Homo sapiens 100 ChEMBL 10.1016/j.bmcl.2012.03.004 10.7270/Q26M37XT 23021104 Hoque, MA; Arai, T; Nishino, N; Kim, HJ; Ito, A; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50394109 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50394109&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71453199 163343133 CHEMBL2158743 C04334 ZINC95573153 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50960715 O=C1N[C@H]2CCCCCSSCCOCC[C@@H](NC2=O)C(=O)N[C@@H](Cc2ccccc2)C(=O)N2CCC[C@H]12 InChI=1S/C27H38N4O5S2/c32-24-20-10-5-2-6-16-37-38-17-15-36-14-12-21(28-24)25(33)30-22(18-19-8-3-1-4-9-19)27(35)31-13-7-11-23(31)26(34)29-20/h1,3-4,8-9,20-23H,2,5-7,10-18H2,(H,28,32)(H,29,34)(H,30,33)/t20-,21+,22-,23+/m0/s1 OJBBUEJBPJGQNL-GSPCLOLRSA-N 50394110 CHEMBL2158742 Histone deacetylase 4 Homo sapiens 5.9 ChEMBL 10.1016/j.bmcl.2012.03.004 10.7270/Q26M37XT 23021104 Hoque, MA; Arai, T; Nishino, N; Kim, HJ; Ito, A; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50394110 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50394110&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71458560 163343134 CHEMBL2158742 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50960716 CC(=O)SCCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC(=O)[C@@H](CCOCCSC(C)=O)NC1=O InChI=1S/C31H44N4O7S2/c1-21(36)43-18-8-4-7-12-24-28(38)32-25(14-16-42-17-19-44-22(2)37)29(39)34-26(20-23-10-5-3-6-11-23)31(41)35-15-9-13-27(35)30(40)33-24/h3,5-6,10-11,24-27H,4,7-9,12-20H2,1-2H3,(H,32,38)(H,33,40)(H,34,39)/t24-,25+,26-,27+/m0/s1 QOVFQFLLZDKEDL-YYGZZXRFSA-N 50394107 CHEMBL2158741 Histone deacetylase 4 Homo sapiens 99 ChEMBL 10.1016/j.bmcl.2012.03.004 10.7270/Q26M37XT 23021104 Hoque, MA; Arai, T; Nishino, N; Kim, HJ; Ito, A; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50394107 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50394107&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71460412 163343131 CHEMBL2158741 C04334 ZINC95573134 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50960717 CC(=O)SCCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@H](CCOCCSC(C)=O)NC(=O)C(C)(C)NC1=O InChI=1S/C26H42N4O7S2/c1-17(31)38-15-7-5-6-9-19-22(33)29-26(3,4)25(36)28-20(11-13-37-14-16-39-18(2)32)24(35)30-12-8-10-21(30)23(34)27-19/h19-21H,5-16H2,1-4H3,(H,27,34)(H,28,36)(H,29,33)/t19-,20-,21+/m0/s1 DUABJLZESSBUAG-PCCBWWKXSA-N 50394108 CHEMBL2158744 Histone deacetylase 4 Homo sapiens 900 ChEMBL 10.1016/j.bmcl.2012.03.004 10.7270/Q26M37XT 23021104 Hoque, MA; Arai, T; Nishino, N; Kim, HJ; Ito, A; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50394108 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50394108&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71462097 163343132 CHEMBL2158744 C04334 ZINC95573205 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50960718 CC(=O)SCCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@H](CCCCCSC(C)=O)NC(=O)C(C)(C)NC1=O InChI=1S/C27H44N4O6S2/c1-18(32)38-16-9-5-7-12-20-23(34)30-27(3,4)26(37)29-21(13-8-6-10-17-39-19(2)33)25(36)31-15-11-14-22(31)24(35)28-20/h20-22H,5-17H2,1-4H3,(H,28,35)(H,29,37)(H,30,34)/t20-,21-,22+/m0/s1 FISBIMNWLAHVKP-FDFHNCONSA-N 50394109 CHEMBL2158743 Histone deacetylase 4 Homo sapiens 1200 ChEMBL 10.1016/j.bmcl.2012.03.004 10.7270/Q26M37XT 23021104 Hoque, MA; Arai, T; Nishino, N; Kim, HJ; Ito, A; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50394109 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50394109&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71453199 163343133 CHEMBL2158743 C04334 ZINC95573153 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50960719 O=C1N[C@H]2CCCCCSSCCOCC[C@@H](NC2=O)C(=O)N[C@@H](Cc2ccccc2)C(=O)N2CCC[C@H]12 InChI=1S/C27H38N4O5S2/c32-24-20-10-5-2-6-16-37-38-17-15-36-14-12-21(28-24)25(33)30-22(18-19-8-3-1-4-9-19)27(35)31-13-7-11-23(31)26(34)29-20/h1,3-4,8-9,20-23H,2,5-7,10-18H2,(H,28,32)(H,29,34)(H,30,33)/t20-,21+,22-,23+/m0/s1 OJBBUEJBPJGQNL-GSPCLOLRSA-N 50394110 CHEMBL2158742 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmcl.2012.03.004 10.7270/Q26M37XT 23021104 Hoque, MA; Arai, T; Nishino, N; Kim, HJ; Ito, A; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50394110 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50394110&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71458560 163343134 CHEMBL2158742 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50960720 CC(=O)SCCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC(=O)[C@@H](CCOCCSC(C)=O)NC1=O InChI=1S/C31H44N4O7S2/c1-21(36)43-18-8-4-7-12-24-28(38)32-25(14-16-42-17-19-44-22(2)37)29(39)34-26(20-23-10-5-3-6-11-23)31(41)35-15-9-13-27(35)30(40)33-24/h3,5-6,10-11,24-27H,4,7-9,12-20H2,1-2H3,(H,32,38)(H,33,40)(H,34,39)/t24-,25+,26-,27+/m0/s1 QOVFQFLLZDKEDL-YYGZZXRFSA-N 50394107 CHEMBL2158741 Histone deacetylase 4 Homo sapiens 990 ChEMBL 10.1016/j.bmcl.2012.03.004 10.7270/Q26M37XT 23021104 Hoque, MA; Arai, T; Nishino, N; Kim, HJ; Ito, A; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50394107 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50394107&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71460412 163343131 CHEMBL2158741 C04334 ZINC95573134 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50960721 C\C=C1/NC(=O)[C@H]2CSSCC\C=C\[C@H](CC(=O)N[C@H](C(C)C)C(=O)N2)OC(=O)[C@@H](NC1=O)C(C)C InChI=1S/C24H36N4O6S2/c1-6-16-21(30)28-20(14(4)5)24(33)34-15-9-7-8-10-35-36-12-17(22(31)25-16)26-23(32)19(13(2)3)27-18(29)11-15/h6-7,9,13-15,17,19-20H,8,10-12H2,1-5H3,(H,25,31)(H,26,32)(H,27,29)(H,28,30)/b9-7+,16-6-/t15-,17-,19-,20+/m1/s1 OHRURASPPZQGQM-GCCNXGTGSA-N 19151 (1S,4S,7Z,10S,16E,21R)-7-ethylidene-4,21-bis(propan-2-yl)-2-oxa-12,13-dithia-5,8,20,23-tetraazabicyclo[8.7.6]tricos-16-ene-3,6,9,19,22-pentone::Antibiotic FR 901228::CHEMBL343448::Depsipeptide::FK228::Romidepsin Histone deacetylase 4 Homo sapiens 510 ChEMBL 10.1016/j.bmcl.2012.03.004 10.7270/Q26M37XT 23021104 Hoque, MA; Arai, T; Nishino, N; Kim, HJ; Ito, A; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19151 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19151&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5352062 46519185 61080 CHEMBL343448 7006 ZINC03935130 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50960722 CC(C=CC(=O)NO)C=C(C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20) ALCVRKZFLFWUAZ-UHFFFAOYSA-N 19130 (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide::CHEMBL99::TSA::Trichostatin A (TSA) Histone deacetylase 4 Homo sapiens 34 ChEMBL 10.1016/j.bmcl.2012.03.004 10.7270/Q26M37XT 23021104 Hoque, MA; Arai, T; Nishino, N; Kim, HJ; Ito, A; Yoshida, M Graduate School of Life Science and Systems Engineering http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19130 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19130&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 91895926 46519165 46024 CHEMBL99 7005 ZINC05579377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50972213 CCCCN(Cc1ccc(cc1)C(=O)NO)C(=O)Nc1ccccc1 InChI=1S/C19H23N3O3/c1-2-3-13-22(19(24)20-17-7-5-4-6-8-17)14-15-9-11-16(12-10-15)18(23)21-25/h4-12,25H,2-3,13-14H2,1H3,(H,20,24)(H,21,23) JZWXMCPARMXZQV-UHFFFAOYSA-N 50398716 CHEMBL2179618::US10227295, Compound 5g::US9409858, 5g::US9751832, Compound 5g::US9956192, Compound 5g Histone deacetylase 4 Homo sapiens 9390 ChEMBL 10.1021/jm301098e 10.7270/Q2WQ04XP 23009203 Bergman, JA; Woan, K; Perez-Villarroel, P; Villagra, A; Sotomayor, EM; Kozikowski, AP University of Illinois at Chicago http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50398716 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50398716&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N4R 5G0J,5G0I 71462653 163347740 CHEMBL2179618 ZINC95573398 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50974746 ONC(=O)c1cccc(c1)-c1cn(CSc2ccccc2)nn1 InChI=1S/C16H14N4O2S/c21-16(18-22)13-6-4-5-12(9-13)15-10-20(19-17-15)11-23-14-7-2-1-3-8-14/h1-10,22H,11H2,(H,18,21) DORPIZJGSLWDIY-UHFFFAOYSA-N 50399672 CHEMBL2178342 Histone deacetylase 4 Homo sapiens 44000 ChEMBL 10.1021/jm300837y 10.7270/Q25X2B3Q 23116147 Suzuki, T; Ota, Y; Ri, M; Bando, M; Gotoh, A; Itoh, Y; Tsumoto, H; Tatum, PR; Mizukami, T; Nakagawa, H; Iida, S; Ueda, R; Shirahige, K; Miyata, N Kyoto Prefectural University of Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399672 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399672&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search GM5 6HSG,6HRQ 53327227 163348696 CHEMBL2178342 ZINC72316041 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50974747 ONC(=O)c1cccc(c1)-c1cn(CCc2ccsc2)nn1 InChI=1S/C15H14N4O2S/c20-15(17-21)13-3-1-2-12(8-13)14-9-19(18-16-14)6-4-11-5-7-22-10-11/h1-3,5,7-10,21H,4,6H2,(H,17,20) AIOBOFRJLHUCLQ-UHFFFAOYSA-N 50399673 CHEMBL2178343 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/jm300837y 10.7270/Q25X2B3Q 23116147 Suzuki, T; Ota, Y; Ri, M; Bando, M; Gotoh, A; Itoh, Y; Tsumoto, H; Tatum, PR; Mizukami, T; Nakagawa, H; Iida, S; Ueda, R; Shirahige, K; Miyata, N Kyoto Prefectural University of Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399673 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399673&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 53327226 163348697 CHEMBL2178343 ZINC72316040 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50974748 ONC(=O)c1cccc(c1)-c1cn(CCc2ccccc2)nn1 InChI=1S/C17H16N4O2/c22-17(19-23)15-8-4-7-14(11-15)16-12-21(20-18-16)10-9-13-5-2-1-3-6-13/h1-8,11-12,23H,9-10H2,(H,19,22) HWLOIPFPGVBJBC-UHFFFAOYSA-N 50399674 CHEMBL2178344 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/jm300837y 10.7270/Q25X2B3Q 23116147 Suzuki, T; Ota, Y; Ri, M; Bando, M; Gotoh, A; Itoh, Y; Tsumoto, H; Tatum, PR; Mizukami, T; Nakagawa, H; Iida, S; Ueda, R; Shirahige, K; Miyata, N Kyoto Prefectural University of Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399674 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399674&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 53327225 163348698 CHEMBL2178344 ZINC95577975 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50974749 ONC(=O)c1cccc(c1)-c1cn(Cc2ccccc2)nn1 InChI=1S/C16H14N4O2/c21-16(18-22)14-8-4-7-13(9-14)15-11-20(19-17-15)10-12-5-2-1-3-6-12/h1-9,11,22H,10H2,(H,18,21) NMOSUYKJZIGNFZ-UHFFFAOYSA-N 50399675 CHEMBL2178345 Histone deacetylase 4 Homo sapiens 30000 ChEMBL 10.1021/jm300837y 10.7270/Q25X2B3Q 23116147 Suzuki, T; Ota, Y; Ri, M; Bando, M; Gotoh, A; Itoh, Y; Tsumoto, H; Tatum, PR; Mizukami, T; Nakagawa, H; Iida, S; Ueda, R; Shirahige, K; Miyata, N Kyoto Prefectural University of Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50399675 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50399675&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 53327224 163348699 CHEMBL2178345 ZINC95572332 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50974750 COc1ccc(Cn2ccc3ccc(cc23)C(=O)NO)cc1 InChI=1S/C17H16N2O3/c1-22-15-6-2-12(3-7-15)11-19-9-8-13-4-5-14(10-16(13)19)17(20)18-21/h2-10,21H,11H2,1H3,(H,18,20) AJRGHIGYPXNABY-UHFFFAOYSA-N 50397360 CHEMBL2170177::US10188756, Compound CN110 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/jm300837y 10.7270/Q25X2B3Q 23116147 Suzuki, T; Ota, Y; Ri, M; Bando, M; Gotoh, A; Itoh, Y; Tsumoto, H; Tatum, PR; Mizukami, T; Nakagawa, H; Iida, S; Ueda, R; Shirahige, K; Miyata, N Kyoto Prefectural University of Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50397360 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50397360&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search GKW 6HQY,6HSF 24753719 163346384 CHEMBL2170177 ZINC43178454 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50974751 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/jm300837y 10.7270/Q25X2B3Q 23116147 Suzuki, T; Ota, Y; Ri, M; Bando, M; Gotoh, A; Itoh, Y; Tsumoto, H; Tatum, PR; Mizukami, T; Nakagawa, H; Iida, S; Ueda, R; Shirahige, K; Miyata, N Kyoto Prefectural University of Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51053118 CN1CCc2c(C1)c1ccccc1n2Cc1ccc(cc1)C(=O)NO InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::Tubastatin A::US10227295, Compound Tubastatin A::US10456394, Tubastatin A::US11207431, Example D::US8748451, 6::US9249087, Tubacin::US9751832, Tubastatin A::US9956192, Compound Tubastatin-A Histone deacetylase 4 Homo sapiens 1100 25.00 C ChEMBL 10.1021/jm301355j 10.7270/Q2XK8GWB 23368884 Wagner, FF; Olson, DE; Gale, JP; Kaya, T; Weiwer, M; Aidoud, N; Thomas, M; Davoine, EL; Lemercier, BC; Zhang, YL; Holson, EB Broad Institute of MIT and Harvard http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 ZINC51951670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51053119 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >33330 25.00 C ChEMBL 10.1021/jm301355j 10.7270/Q2XK8GWB 23368884 Wagner, FF; Olson, DE; Gale, JP; Kaya, T; Weiwer, M; Aidoud, N; Thomas, M; Davoine, EL; Lemercier, BC; Zhang, YL; Holson, EB Broad Institute of MIT and Harvard http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51053120 ONC(=O)C1=CCCC1 InChI=1S/C6H9NO2/c8-6(7-9)5-3-1-2-4-5/h3,9H,1-2,4H2,(H,7,8) RYYGSXXWQSXKRP-UHFFFAOYSA-N 50429525 CHEMBL2333346 Histone deacetylase 4 Homo sapiens 21800 25.00 C ChEMBL 10.1021/jm301355j 10.7270/Q2XK8GWB 23368884 Wagner, FF; Olson, DE; Gale, JP; Kaya, T; Weiwer, M; Aidoud, N; Thomas, M; Davoine, EL; Lemercier, BC; Zhang, YL; Holson, EB Broad Institute of MIT and Harvard http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50429525 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50429525&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search FBJ 6CSS 71655802 164158400 CHEMBL2333346 ZINC95589020 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51053121 ONC(=O)C1CCCCC1 InChI=1S/C7H13NO2/c9-7(8-10)6-4-2-1-3-5-6/h6,10H,1-5H2,(H,8,9) RFWDAWXPYZTVSN-UHFFFAOYSA-N 50429526 CHEMBL2333345::N-Hydroxycyclohexanecarboxamide Histone deacetylase 4 Homo sapiens >33330 25.00 C ChEMBL 10.1021/jm301355j 10.7270/Q2XK8GWB 23368884 Wagner, FF; Olson, DE; Gale, JP; Kaya, T; Weiwer, M; Aidoud, N; Thomas, M; Davoine, EL; Lemercier, BC; Zhang, YL; Holson, EB Broad Institute of MIT and Harvard http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50429526 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50429526&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search F9P 6CSQ 3432579 164158401 CHEMBL2333345 ZINC06415504 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51053122 ONC(=O)C1=CCCCC1 InChI=1S/C7H11NO2/c9-7(8-10)6-4-2-1-3-5-6/h4,10H,1-3,5H2,(H,8,9) NMUKJRPCVOESRU-UHFFFAOYSA-N 50429527 CHEMBL2333344 Histone deacetylase 4 Homo sapiens 9130 25.00 C ChEMBL 10.1021/jm301355j 10.7270/Q2XK8GWB 23368884 Wagner, FF; Olson, DE; Gale, JP; Kaya, T; Weiwer, M; Aidoud, N; Thomas, M; Davoine, EL; Lemercier, BC; Zhang, YL; Holson, EB Broad Institute of MIT and Harvard http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50429527 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50429527&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search FBM 6CSP 20459443 164158402 CHEMBL2333344 ZINC39063959 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51053123 ONC(=O)\C=C\c1ccccc1 InChI=1S/C9H9NO2/c11-9(10-12)7-6-8-4-2-1-3-5-8/h1-7,12H,(H,10,11)/b7-6+ UVDDFTZLVFIQFL-VOTSOKGWSA-N 50015088 (E)-N-Hydroxy-3-phenyl-acrylamide::(E)-N-Hydroxy-3-phenylacrylamide::CHEMBL154574::N-Hydroxy-3-phenyl-acrylamide::US10188756, Compound CN86::trans-N-Hydroxy-3-phenyl-acrylamide Histone deacetylase 4 Homo sapiens 19460 25.00 C ChEMBL 10.1021/jm301355j 10.7270/Q2XK8GWB 23368884 Wagner, FF; Olson, DE; Gale, JP; Kaya, T; Weiwer, M; Aidoud, N; Thomas, M; Davoine, EL; Lemercier, BC; Zhang, YL; Holson, EB Broad Institute of MIT and Harvard http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50015088 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50015088&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5355635 103926931 CHEMBL154574 ZINC08615353 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51053124 ONC(=O)CCc1ccccc1 InChI=1S/C9H11NO2/c11-9(10-12)7-6-8-4-2-1-3-5-8/h1-5,12H,6-7H2,(H,10,11) HYBGBWAPFWWJRE-UHFFFAOYSA-N 50015112 CHEMBL152162::N-Hydroxy-3-phenyl-propionamide::N-hydroxy-3-phenylpropionamide Histone deacetylase 4 Homo sapiens >33330 25.00 C ChEMBL 10.1021/jm301355j 10.7270/Q2XK8GWB 23368884 Wagner, FF; Olson, DE; Gale, JP; Kaya, T; Weiwer, M; Aidoud, N; Thomas, M; Davoine, EL; Lemercier, BC; Zhang, YL; Holson, EB Broad Institute of MIT and Harvard http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50015112 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50015112&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4118131 103926955 CHEMBL152162 ZINC13205634 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51053125 ONC(=O)Cc1ccccc1 InChI=1S/C8H9NO2/c10-8(9-11)6-7-4-2-1-3-5-7/h1-5,11H,6H2,(H,9,10) FPOQLQZHRCEVOT-UHFFFAOYSA-N 50015094 CHEMBL152665::N-Hydroxy-2-phenyl-acetamide::N-hydroxy-2-phenylacetamide::Phenylacetohydroxamic acid Histone deacetylase 4 Homo sapiens >33330 25.00 C ChEMBL 10.1021/jm301355j 10.7270/Q2XK8GWB 23368884 Wagner, FF; Olson, DE; Gale, JP; Kaya, T; Weiwer, M; Aidoud, N; Thomas, M; Davoine, EL; Lemercier, BC; Zhang, YL; Holson, EB Broad Institute of MIT and Harvard http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50015094 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50015094&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 220184 103926937 CHEMBL152665 ZINC16887669 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51053126 ONC(=O)c1ccccc1 InChI=1S/C7H7NO2/c9-7(8-10)6-4-2-1-3-5-6/h1-5,10H,(H,8,9) VDEUYMSGMPQMIK-UHFFFAOYSA-N 50015184 BENZHYDROXAMIC ACID::BENZOHYDROXAMATE::CHEMBL16300::N-Hydroxy-benzamide::N-hydroxybenzamide::benzoyl hydroxamic acid Histone deacetylase 4 Homo sapiens >33330 25.00 C ChEMBL 10.1021/jm301355j 10.7270/Q2XK8GWB 23368884 Wagner, FF; Olson, DE; Gale, JP; Kaya, T; Weiwer, M; Aidoud, N; Thomas, M; Davoine, EL; Lemercier, BC; Zhang, YL; Holson, EB Broad Institute of MIT and Harvard http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50015184 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50015184&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search BHO 3GCK,2BOY,4FL7,1GX2,4ATJ,3UXK,2ATJ,1HSR,3ATJ,5SXJ,6CSR 10313 103927027 50520 CHEMBL16300 DB01924 ZINC04701351 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51053127 CNC(=O)c1ccc(cc1)C(=O)NO InChI=1S/C9H10N2O3/c1-10-8(12)6-2-4-7(5-3-6)9(13)11-14/h2-5,14H,1H3,(H,10,12)(H,11,13) PVWFSNDIULQQLV-UHFFFAOYSA-N 50429528 CHEMBL2333343 Histone deacetylase 4 Homo sapiens >33330 25.00 C ChEMBL 10.1021/jm301355j 10.7270/Q2XK8GWB 23368884 Wagner, FF; Olson, DE; Gale, JP; Kaya, T; Weiwer, M; Aidoud, N; Thomas, M; Davoine, EL; Lemercier, BC; Zhang, YL; Holson, EB Broad Institute of MIT and Harvard http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50429528 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50429528&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71574949 164158403 CHEMBL2333343 ZINC95589859 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51053128 ONC(=O)c1ccc(cc1)C(=O)Nc1ccccc1 InChI=1S/C14H12N2O3/c17-13(15-12-4-2-1-3-5-12)10-6-8-11(9-7-10)14(18)16-19/h1-9,19H,(H,15,17)(H,16,18) HCPFWRDPFXZWGW-UHFFFAOYSA-N 50429529 CHEMBL2333342 Histone deacetylase 4 Homo sapiens >33330 25.00 C ChEMBL 10.1021/jm301355j 10.7270/Q2XK8GWB 23368884 Wagner, FF; Olson, DE; Gale, JP; Kaya, T; Weiwer, M; Aidoud, N; Thomas, M; Davoine, EL; Lemercier, BC; Zhang, YL; Holson, EB Broad Institute of MIT and Harvard http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50429529 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50429529&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11514394 164158404 CHEMBL2333342 ZINC34605362 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51053129 ONC(=O)c1ccc(cc1)C(=O)NCc1ccccc1 InChI=1S/C15H14N2O3/c18-14(16-10-11-4-2-1-3-5-11)12-6-8-13(9-7-12)15(19)17-20/h1-9,20H,10H2,(H,16,18)(H,17,19) TUFKQRHNFPOOSZ-UHFFFAOYSA-N 50429530 CHEMBL2333341 Histone deacetylase 4 Homo sapiens >33330 25.00 C ChEMBL 10.1021/jm301355j 10.7270/Q2XK8GWB 23368884 Wagner, FF; Olson, DE; Gale, JP; Kaya, T; Weiwer, M; Aidoud, N; Thomas, M; Davoine, EL; Lemercier, BC; Zhang, YL; Holson, EB Broad Institute of MIT and Harvard http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50429530 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50429530&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 9835152 164158405 CHEMBL2333341 ZINC33976425 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51053130 ONC(=O)c1ccc(cc1)C(=O)NCCc1ccccc1 InChI=1S/C16H16N2O3/c19-15(17-11-10-12-4-2-1-3-5-12)13-6-8-14(9-7-13)16(20)18-21/h1-9,21H,10-11H2,(H,17,19)(H,18,20) UKIHJVNAWJGYAJ-UHFFFAOYSA-N 50429531 CHEMBL2333340 Histone deacetylase 4 Homo sapiens >33330 25.00 C ChEMBL 10.1021/jm301355j 10.7270/Q2XK8GWB 23368884 Wagner, FF; Olson, DE; Gale, JP; Kaya, T; Weiwer, M; Aidoud, N; Thomas, M; Davoine, EL; Lemercier, BC; Zhang, YL; Holson, EB Broad Institute of MIT and Harvard http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50429531 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50429531&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 9965621 164158406 CHEMBL2333340 ZINC34051306 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51053131 ONC(=O)c1ccc(cc1)C(=O)NCCc1ccncc1 InChI=1S/C15H15N3O3/c19-14(17-10-7-11-5-8-16-9-6-11)12-1-3-13(4-2-12)15(20)18-21/h1-6,8-9,21H,7,10H2,(H,17,19)(H,18,20) XJUUYALJVALNFT-UHFFFAOYSA-N 50429532 CHEMBL2333339 Histone deacetylase 4 Homo sapiens >33330 25.00 C ChEMBL 10.1021/jm301355j 10.7270/Q2XK8GWB 23368884 Wagner, FF; Olson, DE; Gale, JP; Kaya, T; Weiwer, M; Aidoud, N; Thomas, M; Davoine, EL; Lemercier, BC; Zhang, YL; Holson, EB Broad Institute of MIT and Harvard http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50429532 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50429532&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71574948 164158407 CHEMBL2333339 ZINC95590940 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51053132 CN1CCN(CCNC(=O)c2ccc(cc2)C(=O)NO)CC1 InChI=1S/C15H22N4O3/c1-18-8-10-19(11-9-18)7-6-16-14(20)12-2-4-13(5-3-12)15(21)17-22/h2-5,22H,6-11H2,1H3,(H,16,20)(H,17,21) LTGGLOIVZJRPDI-UHFFFAOYSA-N 50429533 CHEMBL2333338 Histone deacetylase 4 Homo sapiens >33330 25.00 C ChEMBL 10.1021/jm301355j 10.7270/Q2XK8GWB 23368884 Wagner, FF; Olson, DE; Gale, JP; Kaya, T; Weiwer, M; Aidoud, N; Thomas, M; Davoine, EL; Lemercier, BC; Zhang, YL; Holson, EB Broad Institute of MIT and Harvard http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50429533 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50429533&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71574856 164158408 CHEMBL2333338 ZINC95586242 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51041241 CC(C=CC(=O)NO)C=C(C)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-12,22H,1-4H3,(H,18,20) ALCVRKZFLFWUAZ-UHFFFAOYSA-N 19130 (2E,4E,6R)-7-[4-(dimethylamino)phenyl]-N-hydroxy-4,6-dimethyl-7-oxohepta-2,4-dienamide::CHEMBL99::TSA::Trichostatin A (TSA) Histone deacetylase 4 Homo sapiens 8439 ChEMBL 10.1021/jm301254q 10.7270/Q2D79CRK 23252603 Marek, L; Hamacher, A; Hansen, FK; Kuna, K; Gohlke, H; Kassack, MU; Kurz, T Heinrich Heine Universit£t http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19130 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19130&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 91895926 46519165 46024 CHEMBL99 7005 ZINC05579377 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51041242 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 48300 ChEMBL 10.1021/jm301254q 10.7270/Q2D79CRK 23252603 Marek, L; Hamacher, A; Hansen, FK; Kuna, K; Gohlke, H; Kassack, MU; Kurz, T Heinrich Heine Universit£t http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51041243 Cc1cc(C)cc(c1)C(=O)NOCCCCCC(=O)NO InChI=1S/C15H22N2O4/c1-11-8-12(2)10-13(9-11)15(19)17-21-7-5-3-4-6-14(18)16-20/h8-10,20H,3-7H2,1-2H3,(H,16,18)(H,17,19) VRYZCEONIWEUAV-UHFFFAOYSA-N 50424996 CHEMBL2312168 Histone deacetylase 4 Homo sapiens 12 ChEMBL 10.1021/jm301254q 10.7270/Q2D79CRK 23252603 Marek, L; Hamacher, A; Hansen, FK; Kuna, K; Gohlke, H; Kassack, MU; Kurz, T Heinrich Heine Universit£t http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50424996 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50424996&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71520717 164153871 CHEMBL2312168 ZINC95593440 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51041244 Cc1ccc(cc1C)C(=O)NOCCCCCC(=O)NO InChI=1S/C15H22N2O4/c1-11-7-8-13(10-12(11)2)15(19)17-21-9-5-3-4-6-14(18)16-20/h7-8,10,20H,3-6,9H2,1-2H3,(H,16,18)(H,17,19) XBQPEXDCROFSOE-UHFFFAOYSA-N 50424997 CHEMBL2312167 Histone deacetylase 4 Homo sapiens 83 ChEMBL 10.1021/jm301254q 10.7270/Q2D79CRK 23252603 Marek, L; Hamacher, A; Hansen, FK; Kuna, K; Gohlke, H; Kassack, MU; Kurz, T Heinrich Heine Universit£t http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50424997 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50424997&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71520716 164153872 CHEMBL2312167 ZINC95593586 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51041245 Cc1cccc(c1)C(=O)NOCCCCCC(=O)NO InChI=1S/C14H20N2O4/c1-11-6-5-7-12(10-11)14(18)16-20-9-4-2-3-8-13(17)15-19/h5-7,10,19H,2-4,8-9H2,1H3,(H,15,17)(H,16,18) BAKKPDUWEXRTIN-UHFFFAOYSA-N 50424998 CHEMBL2312164 Histone deacetylase 4 Homo sapiens 16 ChEMBL 10.1021/jm301254q 10.7270/Q2D79CRK 23252603 Marek, L; Hamacher, A; Hansen, FK; Kuna, K; Gohlke, H; Kassack, MU; Kurz, T Heinrich Heine Universit£t http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50424998 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50424998&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71520631 164153873 CHEMBL2312164 ZINC95594315 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 487010 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1(CN2CCCC3(CC3)C2)CC1 InChI=1S/C21H23F3N4O2/c22-21(23,24)18-25-16(27-30-18)14-2-4-15(5-3-14)17(29)26-20(9-10-20)13-28-11-1-6-19(12-28)7-8-19/h2-5H,1,6-13H2,(H,26,29) SOUBSJUNNDFMBE-UHFFFAOYSA-N 228159 US10047073, 1 Histone deacetylase 4 Homo sapiens 50.0 US Patent 10.7270/Q2PG1TQC aid1795129 US10047073 Maillard, MC; Breccia, P; Dominguez, C; Haughan, AF; Jarvis, RE; Luckhurst, CA; Saville-Stones, EA; Stott, AJ; Van de Poel, A; Wall, M; Wishart, G CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=228159 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=228159&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90331748 375077102 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 487011 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1(CN2CCC3(COC3)CC2)CC1 InChI=1S/C21H23F3N4O3/c22-21(23,24)18-25-16(27-31-18)14-1-3-15(4-2-14)17(29)26-20(5-6-20)11-28-9-7-19(8-10-28)12-30-13-19/h1-4H,5-13H2,(H,26,29) RIXICKUDZTYFDS-UHFFFAOYSA-N 228160 US10047073, 2 Histone deacetylase 4 Homo sapiens 110 US Patent 10.7270/Q2PG1TQC aid1795129 US10047073 Maillard, MC; Breccia, P; Dominguez, C; Haughan, AF; Jarvis, RE; Luckhurst, CA; Saville-Stones, EA; Stott, AJ; Van de Poel, A; Wall, M; Wishart, G CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=228160 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=228160&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 89473650 375077103 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 487012 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1(CN2CCCC22COC2)CCC1 InChI=1S/C21H23F3N4O3/c22-21(23,24)18-25-16(27-31-18)14-3-5-15(6-4-14)17(29)26-19(7-1-8-19)11-28-10-2-9-20(28)12-30-13-20/h3-6H,1-2,7-13H2,(H,26,29) APPYRJBKNMMYBG-UHFFFAOYSA-N 228161 US10047073, 3 Histone deacetylase 4 Homo sapiens 750 US Patent 10.7270/Q2PG1TQC aid1795129 US10047073 Maillard, MC; Breccia, P; Dominguez, C; Haughan, AF; Jarvis, RE; Luckhurst, CA; Saville-Stones, EA; Stott, AJ; Van de Poel, A; Wall, M; Wishart, G CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=228161 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=228161&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 89462246 375077104 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 487013 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1(CN2CC3CCC(C3)C2)CC1 InChI=1S/C21H23F3N4O2/c22-21(23,24)19-25-17(27-30-19)15-3-5-16(6-4-15)18(29)26-20(7-8-20)12-28-10-13-1-2-14(9-13)11-28/h3-6,13-14H,1-2,7-12H2,(H,26,29) JOAQFUQHIMMIMB-UHFFFAOYSA-N 228162 US10047073, 4 Histone deacetylase 4 Homo sapiens 330 US Patent 10.7270/Q2PG1TQC aid1795129 US10047073 Maillard, MC; Breccia, P; Dominguez, C; Haughan, AF; Jarvis, RE; Luckhurst, CA; Saville-Stones, EA; Stott, AJ; Van de Poel, A; Wall, M; Wishart, G CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=228162 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=228162&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 89462354 375077105 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 487014 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1(CN2CCC3(CC3)CC2)CC1 InChI=1S/C21H23F3N4O2/c22-21(23,24)18-25-16(27-30-18)14-1-3-15(4-2-14)17(29)26-20(7-8-20)13-28-11-9-19(5-6-19)10-12-28/h1-4H,5-13H2,(H,26,29) BIULWZLYCZLVJY-UHFFFAOYSA-N 228163 US10047073, 5 Histone deacetylase 4 Homo sapiens 89.0 US Patent 10.7270/Q2PG1TQC aid1795129 US10047073 Maillard, MC; Breccia, P; Dominguez, C; Haughan, AF; Jarvis, RE; Luckhurst, CA; Saville-Stones, EA; Stott, AJ; Van de Poel, A; Wall, M; Wishart, G CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=228163 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=228163&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 89473750 375077106 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 487015 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1(CN2CCCC2C2CC2)CC1 InChI=1S/C21H23F3N4O2/c22-21(23,24)19-25-17(27-30-19)14-5-7-15(8-6-14)18(29)26-20(9-10-20)12-28-11-1-2-16(28)13-3-4-13/h5-8,13,16H,1-4,9-12H2,(H,26,29) DOPPWJINMUXMJR-UHFFFAOYSA-N 228164 US10047073, 6::US10047073, 7 Histone deacetylase 4 Homo sapiens 8.00 US Patent 10.7270/Q2PG1TQC aid1795129 US10047073 Maillard, MC; Breccia, P; Dominguez, C; Haughan, AF; Jarvis, RE; Luckhurst, CA; Saville-Stones, EA; Stott, AJ; Van de Poel, A; Wall, M; Wishart, G CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=228164 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=228164&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 89473756 375077107 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 487016 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1(CN2CCCC2C2CC2)CC1 InChI=1S/C21H23F3N4O2/c22-21(23,24)19-25-17(27-30-19)14-5-7-15(8-6-14)18(29)26-20(9-10-20)12-28-11-1-2-16(28)13-3-4-13/h5-8,13,16H,1-4,9-12H2,(H,26,29) DOPPWJINMUXMJR-UHFFFAOYSA-N 228164 US10047073, 6::US10047073, 7 Histone deacetylase 4 Homo sapiens 3.00 US Patent 10.7270/Q2PG1TQC aid1795129 US10047073 Maillard, MC; Breccia, P; Dominguez, C; Haughan, AF; Jarvis, RE; Luckhurst, CA; Saville-Stones, EA; Stott, AJ; Van de Poel, A; Wall, M; Wishart, G CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=228164 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=228164&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 89473756 375077107 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 487017 CC1(C)CCC[NH+](CC2(CC2)NC(=O)c2ccc(cc2)-c2noc(n2)C(F)(F)F)C1 InChI=1S/C21H25F3N4O2/c1-19(2)8-3-11-28(12-19)13-20(9-10-20)26-17(29)15-6-4-14(5-7-15)16-25-18(30-27-16)21(22,23)24/h4-7H,3,8-13H2,1-2H3,(H,26,29)/p+1 UWBSPFFYHKFGOE-UHFFFAOYSA-O 228166 US10047073, 8 Histone deacetylase 4 Homo sapiens 30.0 US Patent 10.7270/Q2PG1TQC aid1795129 US10047073 Maillard, MC; Breccia, P; Dominguez, C; Haughan, AF; Jarvis, RE; Luckhurst, CA; Saville-Stones, EA; Stott, AJ; Van de Poel, A; Wall, M; Wishart, G CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=228166 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=228166&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 89473757 375077109 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 487018 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1(CN2CCC3(CC3)C2)CCC1 InChI=1S/C21H23F3N4O2/c22-21(23,24)18-25-16(27-30-18)14-2-4-15(5-3-14)17(29)26-20(6-1-7-20)13-28-11-10-19(12-28)8-9-19/h2-5H,1,6-13H2,(H,26,29) KDTCSZKKTPRSAS-UHFFFAOYSA-N 228169 US10047073, 9 Histone deacetylase 4 Homo sapiens 58.0 US Patent 10.7270/Q2PG1TQC aid1795129 US10047073 Maillard, MC; Breccia, P; Dominguez, C; Haughan, AF; Jarvis, RE; Luckhurst, CA; Saville-Stones, EA; Stott, AJ; Van de Poel, A; Wall, M; Wishart, G CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=228169 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=228169&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 89473758 375077112 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 487019 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1(CN2CCCC22COC2)CC1 InChI=1S/C20H21F3N4O3/c21-20(22,23)17-24-15(26-30-17)13-2-4-14(5-3-13)16(28)25-18(7-8-18)10-27-9-1-6-19(27)11-29-12-19/h2-5H,1,6-12H2,(H,25,28) XXRQRMAWAPFYPS-UHFFFAOYSA-N 228171 US10047073, 10 Histone deacetylase 4 Homo sapiens 750 US Patent 10.7270/Q2PG1TQC aid1795129 US10047073 Maillard, MC; Breccia, P; Dominguez, C; Haughan, AF; Jarvis, RE; Luckhurst, CA; Saville-Stones, EA; Stott, AJ; Van de Poel, A; Wall, M; Wishart, G CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=228171 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=228171&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90331921 375077114 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 487020 C[C@H]1CCC[NH+]1CC1CC1NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C19H21F3N4O2/c1-11-3-2-8-26(11)10-14-9-15(14)23-17(27)13-6-4-12(5-7-13)16-24-18(28-25-16)19(20,21)22/h4-7,11,14-15H,2-3,8-10H2,1H3,(H,23,27)/p+1/t11-,14?,15?/m0/s1 IPJFJVIZXMOMKU-QGLTVNCISA-O 228172 US10047073, 11 Histone deacetylase 4 Homo sapiens 230 US Patent 10.7270/Q2PG1TQC aid1795129 US10047073 Maillard, MC; Breccia, P; Dominguez, C; Haughan, AF; Jarvis, RE; Luckhurst, CA; Saville-Stones, EA; Stott, AJ; Van de Poel, A; Wall, M; Wishart, G CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=228172 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=228172&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 89473755 375077115 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 487021 CC1(C)CCCN(CC2(CC2)NC(=O)c2ccc(-c3noc(n3)C(F)(F)F)c(F)c2)C1 InChI=1S/C21H24F4N4O2/c1-19(2)6-3-9-29(11-19)12-20(7-8-20)27-17(30)13-4-5-14(15(22)10-13)16-26-18(31-28-16)21(23,24)25/h4-5,10H,3,6-9,11-12H2,1-2H3,(H,27,30) BUBDEPORMDPYGT-UHFFFAOYSA-N 228173 US10047073, 12 Histone deacetylase 4 Homo sapiens 76.0 US Patent 10.7270/Q2PG1TQC aid1795129 US10047073 Maillard, MC; Breccia, P; Dominguez, C; Haughan, AF; Jarvis, RE; Luckhurst, CA; Saville-Stones, EA; Stott, AJ; Van de Poel, A; Wall, M; Wishart, G CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=228173 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=228173&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 89462072 375077116 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560006 Cc1c(F)cccc1[C@]1(CCC(=C1)c1ccccc1)C(=O)NO InChI=1S/C19H18FNO2/c1-13-16(8-5-9-17(13)20)19(18(22)21-23)11-10-15(12-19)14-6-3-2-4-7-14/h2-9,12,23H,10-11H2,1H3,(H,21,22)/t19-/m1/s1 SCXQMYOBRMHEHW-LJQANCHMSA-N 293875 (R)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3- phenylcyclopent-2- enecarboxamide::US10106535, Example 1::US9617259, 1 Histone deacetylase 4 Homo sapiens 7600 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293875 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293875&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302815 381614145 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560007 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccccc1)C(=O)NO InChI=1S/C19H18FNO2/c1-13-16(8-5-9-17(13)20)19(18(22)21-23)11-10-15(12-19)14-6-3-2-4-7-14/h2-9,12,23H,10-11H2,1H3,(H,21,22)/t19-/m0/s1 SCXQMYOBRMHEHW-IBGZPJMESA-N 293876 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3- phenylcyclopent-2- enecarboxamide::US10106535, Example 2::US9617259, 2 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293876 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293876&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302816 381614146 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560008 Cc1ccccc1C1=C[C@@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C20H20FNO2/c1-13-6-3-4-7-16(13)15-10-11-20(12-15,19(23)22-24)17-8-5-9-18(21)14(17)2/h3-9,12,24H,10-11H2,1-2H3,(H,22,23)/t20-/m1/s1 XMEPHEZCBJENHK-HXUWFJFHSA-N 293877 (R)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(o- tolyl)cyclopent-2- enecarboxamide::US10106535, Example 3::US9617259, 3 Histone deacetylase 4 Homo sapiens 230 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293877 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293877&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302817 381614147 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560009 Cc1ccccc1C1=C[C@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C20H20FNO2/c1-13-6-3-4-7-16(13)15-10-11-20(12-15,19(23)22-24)17-8-5-9-18(21)14(17)2/h3-9,12,24H,10-11H2,1-2H3,(H,22,23)/t20-/m0/s1 XMEPHEZCBJENHK-FQEVSTJZSA-N 293878 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(o- tolyl)cyclopent-2- enecarboxamide::US10106535, Example 4::US9617259, 4 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293878 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293878&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302818 381614148 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560010 Cc1c(F)cccc1[C@]1(CCC(=C1)c1cncc(F)c1)C(=O)NO InChI=1S/C18H16F2N2O2/c1-11-15(3-2-4-16(11)20)18(17(23)22-24)6-5-12(8-18)13-7-14(19)10-21-9-13/h2-4,7-10,24H,5-6H2,1H3,(H,22,23)/t18-/m1/s1 UBYLOIIQGDRWBE-GOSISDBHSA-N 293879 (R)-1-(3-Fluoro-2- methylphenyl)-3-(5- fluoropyridin-3-yl)-N- hydroxycyclopent-2- enecarboxamide::US10106535, Example 5::US9617259, 5 Histone deacetylase 4 Homo sapiens 670 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293879 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293879&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302819 381614149 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560011 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cncc(F)c1)C(=O)NO InChI=1S/C18H16F2N2O2/c1-11-15(3-2-4-16(11)20)18(17(23)22-24)6-5-12(8-18)13-7-14(19)10-21-9-13/h2-4,7-10,24H,5-6H2,1H3,(H,22,23)/t18-/m0/s1 UBYLOIIQGDRWBE-SFHVURJKSA-N 293880 (S)-1-(3-Fluoro-2- methylphenyl)-3-(5- fluoropyridin-3-yl)-N- hydroxycyclopent-2- enecarboxamide::US10106535, Example 6::US9617259, 6 Histone deacetylase 4 Homo sapiens 10.00 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293880 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293880&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302820 381614150 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560012 Cc1c(F)cccc1[C@]1(CCC(=C1)c1cnccn1)C(=O)NO InChI=1S/C17H16FN3O2/c1-11-13(3-2-4-14(11)18)17(16(22)21-23)6-5-12(9-17)15-10-19-7-8-20-15/h2-4,7-10,23H,5-6H2,1H3,(H,21,22)/t17-/m1/s1 KPAWOECHWHNXRI-QGZVFWFLSA-N 293881 (R)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(pyrazin-2- yl)cyclopent-2- enecarboxamide::US10106535, Example 7::US9617259, 7 Histone deacetylase 4 Homo sapiens >50000 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293881 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293881&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302821 381614151 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560013 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cnccn1)C(=O)NO InChI=1S/C17H16FN3O2/c1-11-13(3-2-4-14(11)18)17(16(22)21-23)6-5-12(9-17)15-10-19-7-8-20-15/h2-4,7-10,23H,5-6H2,1H3,(H,21,22)/t17-/m0/s1 KPAWOECHWHNXRI-KRWDZBQOSA-N 293882 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(pyrazin-2- yl)cyclopent-2- enecarboxamide::US10106535, Example 8::US9617259, 8 Histone deacetylase 4 Homo sapiens 2400 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293882 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293882&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302977 381614152 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560014 Cc1ncc(cn1)C1=C[C@@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C18H18FN3O2/c1-11-15(4-3-5-16(11)19)18(17(23)22-24)7-6-13(8-18)14-9-20-12(2)21-10-14/h3-5,8-10,24H,6-7H2,1-2H3,(H,22,23)/t18-/m1/s1 MXGUWZUPIAJYLA-GOSISDBHSA-N 293883 (R)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(2- methylpyrimidin-5- yl)cyclopent-2- enecarboxamide::US10106535, Example 9 Histone deacetylase 4 Homo sapiens 26800 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293883 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293883&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302978 381614153 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560015 Cc1ncc(cn1)C1=C[C@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C18H18FN3O2/c1-11-15(4-3-5-16(11)19)18(17(23)22-24)7-6-13(8-18)14-9-20-12(2)21-10-14/h3-5,8-10,24H,6-7H2,1-2H3,(H,22,23)/t18-/m0/s1 MXGUWZUPIAJYLA-SFHVURJKSA-N 293884 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(2- methylpyrimidin-5- yl)cyclopent-2- enecarboxamide::US10106535, Example 10 Histone deacetylase 4 Homo sapiens 40.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293884 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293884&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302979 381614154 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560016 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cncc(Cl)c1)C(=O)NO InChI=1S/C18H16ClFN2O2/c1-11-15(3-2-4-16(11)20)18(17(23)22-24)6-5-12(8-18)13-7-14(19)10-21-9-13/h2-4,7-10,24H,5-6H2,1H3,(H,22,23)/t18-/m0/s1 RHEXMBJUOFFAAI-SFHVURJKSA-N 293885 (S)-3-(5-Chloropyridin-3- yl)-1-(3-fluoro-2- methylphenyl)-N- hydroxycyclopent-2- enecarboxamide::US10106535, Example 11::US9617259, 11 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293885 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293885&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302980 381614155 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560017 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccc2nccnc2c1)C(=O)NO InChI=1S/C21H18FN3O2/c1-13-16(3-2-4-17(13)22)21(20(26)25-27)8-7-15(12-21)14-5-6-18-19(11-14)24-10-9-23-18/h2-6,9-12,27H,7-8H2,1H3,(H,25,26)/t21-/m0/s1 CHWSCSWQGMLYOD-NRFANRHFSA-N 293886 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(quinoxalin-6- yl)cyclopent-2- enecarboxamide::US10106535, Example 12::US9617259, 12 Histone deacetylase 4 Homo sapiens 10.00 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293886 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293886&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302981 381614156 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560018 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccnc(c1)C(F)(F)F)C(=O)NO InChI=1S/C19H16F4N2O2/c1-11-14(3-2-4-15(11)20)18(17(26)25-27)7-5-13(10-18)12-6-8-24-16(9-12)19(21,22)23/h2-4,6,8-10,27H,5,7H2,1H3,(H,25,26)/t18-/m0/s1 RTXWXKMNNKTFFM-SFHVURJKSA-N 293887 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(2- (trifluoromethyl)pyridin- 4-yl)cyclopent-2- enecarboxamide::US10106535, Example 13::US9617259, 13 Histone deacetylase 4 Homo sapiens 40.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293887 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293887&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302982 381614157 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560019 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cncnc1)C(=O)NO InChI=1S/C17H16FN3O2/c1-11-14(3-2-4-15(11)18)17(16(22)21-23)6-5-12(7-17)13-8-19-10-20-9-13/h2-4,7-10,23H,5-6H2,1H3,(H,21,22)/t17-/m0/s1 WIBZOPAYZTWUAG-KRWDZBQOSA-N 293888 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(pyrimidin-5- yl)cyclopent-2- enecarboxamide::US10106535, Example 14::US9617259, 14 Histone deacetylase 4 Homo sapiens 30.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293888 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293888&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302983 381614158 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560020 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccc(F)cn1)C(=O)NO InChI=1S/C18H16F2N2O2/c1-11-14(3-2-4-15(11)20)18(17(23)22-24)8-7-12(9-18)16-6-5-13(19)10-21-16/h2-6,9-10,24H,7-8H2,1H3,(H,22,23)/t18-/m0/s1 IKZXPALLSJENTD-SFHVURJKSA-N 293889 (S)-1-(3-Fluoro-2- methylphenyl)-3-(5- fluoropyridin-2-yl)-N- hydroxycyclopent-2- enecarboxamide::US10106535, Example 15::US9617259, 15 Histone deacetylase 4 Homo sapiens 40.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293889 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293889&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303139 381614159 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560021 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccc(nc1)C(F)(F)F)C(=O)NO InChI=1S/C19H16F4N2O2/c1-11-14(3-2-4-15(11)20)18(17(26)25-27)8-7-12(9-18)13-5-6-16(24-10-13)19(21,22)23/h2-6,9-10,27H,7-8H2,1H3,(H,25,26)/t18-/m0/s1 HQDKBLZLYAJTGA-SFHVURJKSA-N 293890 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(6- (trifluoromethyl)pyridin- 3-yl)cyclopent-2- enecarboxamide::US10106535, Example 16::US9617259, 16 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293890 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293890&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303140 381614160 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560022 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cncc(c1)C(F)(F)F)C(=O)NO InChI=1S/C19H16F4N2O2/c1-11-15(3-2-4-16(11)20)18(17(26)25-27)6-5-12(8-18)13-7-14(10-24-9-13)19(21,22)23/h2-4,7-10,27H,5-6H2,1H3,(H,25,26)/t18-/m0/s1 GGFUMFGWFPMRIT-SFHVURJKSA-N 293891 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(5- (trifluoromethyl)pyridin- 3-yl)cyclopent-2- enecarboxamide::US10106535, Example 17::US9617259, 17 Histone deacetylase 4 Homo sapiens 30.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293891 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293891&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303141 381614161 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560023 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cnn(c1)C(F)F)C(=O)NO InChI=1S/C17H16F3N3O2/c1-10-13(3-2-4-14(10)18)17(15(24)22-25)6-5-11(7-17)12-8-21-23(9-12)16(19)20/h2-4,7-9,16,25H,5-6H2,1H3,(H,22,24)/t17-/m0/s1 FOMINESAMTVGQU-KRWDZBQOSA-N 293892 (S)-3-(1-(Difluoromethyl)- 1H-pyrazol-4-yl)-1-(3- fluoro-2-methylphenyl)- N-hydroxycyclopent-2- enecarboxamide::US10106535, Example 18::US9617259, 18 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293892 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293892&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303142 381614162 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560024 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cc(F)cnc1C1CC1)C(=O)NO InChI=1S/C21H20F2N2O2/c1-12-17(3-2-4-18(12)23)21(20(26)25-27)8-7-14(10-21)16-9-15(22)11-24-19(16)13-5-6-13/h2-4,9-11,13,27H,5-8H2,1H3,(H,25,26)/t21-/m0/s1 OETMIHHGNBWUIE-NRFANRHFSA-N 293893 (S)-3-(2-Cyclopropyl-5- fluoropyridin-3-yl)-1-(3- fluoro-2-methylphenyl)- N-hydroxycyclopent-2- enecarboxamide::US10106535, Example 19::US9617259, 19 Histone deacetylase 4 Homo sapiens 40.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293893 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293893&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303143 381614163 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560025 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccc2nc(cnc2c1)C(F)(F)F)C(=O)NO InChI=1S/C22H17F4N3O2/c1-12-15(3-2-4-16(12)23)21(20(30)29-31)8-7-14(10-21)13-5-6-17-18(9-13)27-11-19(28-17)22(24,25)26/h2-6,9-11,31H,7-8H2,1H3,(H,29,30)/t21-/m0/s1 PEGKKBIYYUMQNV-NRFANRHFSA-N 293894 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(2- (trifluoromethyl)quinoxalin- 6-yl)cyclopent-2- enecarboxamide::US10106535, Example 20::US9617259, 20 Histone deacetylase 4 Homo sapiens 70.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293894 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293894&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303144 381614164 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560026 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccn2ccnc2c1)C(=O)NO InChI=1S/C20H18FN3O2/c1-13-16(3-2-4-17(13)21)20(19(25)23-26)7-5-15(12-20)14-6-9-24-10-8-22-18(24)11-14/h2-4,6,8-12,26H,5,7H2,1H3,(H,23,25)/t20-/m0/s1 YZHROUDNYPZPHH-FQEVSTJZSA-N 293895 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(imidazo[1,2- a]pyridin-7-yl)cyclopent- 2-enecarboxamide::US10106535, Example 21::US9617259, 21 Histone deacetylase 4 Homo sapiens 10.00 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293895 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293895&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303145 381614165 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560027 Cc1noc2ccc(cc12)C1=C[C@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C21H19FN2O3/c1-12-17(4-3-5-18(12)22)21(20(25)23-26)9-8-15(11-21)14-6-7-19-16(10-14)13(2)24-27-19/h3-7,10-11,26H,8-9H2,1-2H3,(H,23,25)/t21-/m0/s1 XEIQOCJVBFLFRP-NRFANRHFSA-N 293896 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(3- methylbenzo[d]isoxazol- 5-yl)cyclopent-2- enecarboxamide::US10106535, Example 22::US9617259, 22 Histone deacetylase 4 Homo sapiens 30.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293896 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293896&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303609 381614166 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560028 COc1ncc(cc1F)C1=C[C@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C19H18F2N2O3/c1-11-14(4-3-5-15(11)20)19(18(24)23-25)7-6-12(9-19)13-8-16(21)17(26-2)22-10-13/h3-5,8-10,25H,6-7H2,1-2H3,(H,23,24)/t19-/m0/s1 GQXSBKPOHFDJCM-IBGZPJMESA-N 293897 (S)-1-(3-Fluoro-2- methylphenyl)-3-(5- fluoro-6-methoxypyridin- 3-yl)-N- hydroxycyclopent-2- enecarboxamide::US10106535, Example 23::US9617259, 23 Histone deacetylase 4 Homo sapiens 40.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293897 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293897&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303294 381614167 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560029 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cnc(nc1)C1CC1)C(=O)NO InChI=1S/C20H20FN3O2/c1-12-16(3-2-4-17(12)21)20(19(25)24-26)8-7-14(9-20)15-10-22-18(23-11-15)13-5-6-13/h2-4,9-11,13,26H,5-8H2,1H3,(H,24,25)/t20-/m0/s1 LXFQZWLCATUSEA-FQEVSTJZSA-N 293898 (S)-3-(2- Cyclopropylpyrimidin-5- yl)-1-(3-fluoro-2- methylphenyl)-N- hydroxycyclopent-2- enecarboxamide::US10106535, Example 24::US9617259, 24 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293898 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293898&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303295 381614168 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560030 Cc1ccc(cn1)C1=C[C@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C19H19FN2O2/c1-12-6-7-15(11-21-12)14-8-9-19(10-14,18(23)22-24)16-4-3-5-17(20)13(16)2/h3-7,10-11,24H,8-9H2,1-2H3,(H,22,23)/t19-/m0/s1 QJUUVIUVFUKTMQ-IBGZPJMESA-N 293899 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(6- methylpyridin-3- yl)cyclopent-2- enecarboxamide::US10106535, Example 25::US9617259, 25 Histone deacetylase 4 Homo sapiens 10.00 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293899 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293899&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303298 381614169 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560031 Cc1ncc(cc1Cl)C1=C[C@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C19H18ClFN2O2/c1-11-15(4-3-5-17(11)21)19(18(24)23-25)7-6-13(9-19)14-8-16(20)12(2)22-10-14/h3-5,8-10,25H,6-7H2,1-2H3,(H,23,24)/t19-/m0/s1 IZSSBCOCGWWLDH-IBGZPJMESA-N 293900 (S)-3-(5-Chloro-6- methylpyridin-3-yl)-1-(3- fluoro-2-methylphenyl)- N-hydroxycyclopent-2- enecarboxamide::US10106535, Example 26::US9617259, 26 Histone deacetylase 4 Homo sapiens 10.00 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293900 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293900&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303297 381614170 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560032 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccnn1C)C(=O)NO InChI=1S/C17H18FN3O2/c1-11-13(4-3-5-14(11)18)17(16(22)20-23)8-6-12(10-17)15-7-9-19-21(15)2/h3-5,7,9-10,23H,6,8H2,1-2H3,(H,20,22)/t17-/m0/s1 FCSQJTXZDUDBJM-KRWDZBQOSA-N 293901 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(1-methyl-1H- pyrazol-5-yl)cyclopent-2- enecarboxamide::US10106535, Example 27::US9617259, 27 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293901 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293901&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303296 381614171 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560033 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cnn(CC(F)(F)F)c1)C(=O)NO InChI=1S/C18H17F4N3O2/c1-11-14(3-2-4-15(11)19)17(16(26)24-27)6-5-12(7-17)13-8-23-25(9-13)10-18(20,21)22/h2-4,7-9,27H,5-6,10H2,1H3,(H,24,26)/t17-/m0/s1 UEBUMEGYICYBBJ-KRWDZBQOSA-N 293902 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(1-(2,2,2- trifluoroethyl)-1H- pyrazol-4-yl)cyclopent-2- enecarboxamide::US10106535, Example 28::US9617259, 28 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293902 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293902&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303299 381617018 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560034 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cccc2cnsc12)C(=O)NO InChI=1S/C20H17FN2O2S/c1-12-16(6-3-7-17(12)21)20(19(24)23-25)9-8-13(10-20)15-5-2-4-14-11-22-26-18(14)15/h2-7,10-11,25H,8-9H2,1H3,(H,23,24)/t20-/m0/s1 CNBJREROOOWMRM-FQEVSTJZSA-N 293903 (S)-3-(Benzo[d]isothiazol- 7-yl)-1-(3-fluoro-2- methylphenyl)-N- hydroxycyclopent-2- enecarboxamide::US10106535, Example 29::US9617259, 29 Histone deacetylase 4 Homo sapiens 30.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293903 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293903&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303610 381617019 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560035 ONC(=O)C1C=CCC1c1ccccc1 InChI=1S/C12H13NO2/c14-12(13-15)11-8-4-7-10(11)9-5-2-1-3-6-9/h1-6,8,10-11,15H,7H2,(H,13,14) BQPHFUDWHOHTGO-UHFFFAOYSA-N 293904 N-Hydroxy-1- phenylcyclopent-3- enecarboxamide::US10106535, Example 30 Histone deacetylase 4 Homo sapiens 12300 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293904 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293904&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 132042690 381617020 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560036 ONC(=O)C1(CC=CC1)c1ccccc1F InChI=1S/C12H12FNO2/c13-10-6-2-1-5-9(10)12(11(15)14-16)7-3-4-8-12/h1-6,16H,7-8H2,(H,14,15) PGXHBLNNBFBHQE-UHFFFAOYSA-N 293905 1-(2-Fluorophenyl)-N- hydroxycyclopent-3- enecarboxamide::US10106535, Example 31::US9617259, 31 Histone deacetylase 4 Homo sapiens 8300 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293905 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293905&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303301 381617021 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560037 Cc1c(F)cccc1[C@@]1(CCC(=C1)C1CC1)C(=O)NO InChI=1S/C16H18FNO2/c1-10-13(3-2-4-14(10)17)16(15(19)18-20)8-7-12(9-16)11-5-6-11/h2-4,9,11,20H,5-8H2,1H3,(H,18,19)/t16-/m0/s1 SSJSHINFMGPHNV-INIZCTEOSA-N 293906 (S)-3-Cyclopropyl-1-(3- fluoro-2-methylphenyl)- N-hydroxycyclopent-2- enecarboxamide::US10106535, Example 32::US9617259, 32 Histone deacetylase 4 Homo sapiens 40.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293906 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293906&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303452 381617022 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560038 ONC(=O)[C@]1(CCC(=C1)c1ccccc1)c1ccccc1 InChI=1S/C18H17NO2/c20-17(19-21)18(16-9-5-2-6-10-16)12-11-15(13-18)14-7-3-1-4-8-14/h1-10,13,21H,11-12H2,(H,19,20)/t18-/m0/s1 LTWVYNGVRLUGEE-SFHVURJKSA-N 293907 (S)-N-Hydroxy-1,3- diphenylcyclopent-2- enecarboxamide::US10106535, Example 33::US9617259, 33 Histone deacetylase 4 Homo sapiens 190 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293907 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293907&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303453 381617023 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560039 ONC(=O)[C@@]1(CCC(=C1)c1ccccc1)c1ccccc1 InChI=1S/C18H17NO2/c20-17(19-21)18(16-9-5-2-6-10-16)12-11-15(13-18)14-7-3-1-4-8-14/h1-10,13,21H,11-12H2,(H,19,20)/t18-/m1/s1 LTWVYNGVRLUGEE-GOSISDBHSA-N 293908 (R)-N-Hydroxy-1,3- diphenylcyclopent-2- enecarboxamide::US10106535, Example 34::US9617259, 34 Histone deacetylase 4 Homo sapiens 31000 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293908 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293908&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303454 381617024 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560040 ONC(=O)[C@]1(CCC(=C1)c1cncc(F)c1)c1ccccc1 InChI=1S/C17H15FN2O2/c18-15-8-13(10-19-11-15)12-6-7-17(9-12,16(21)20-22)14-4-2-1-3-5-14/h1-5,8-11,22H,6-7H2,(H,20,21)/t17-/m0/s1 WVTONWZRSXXBPD-KRWDZBQOSA-N 293909 (S)-3-(5-Fluoropyridin-3- yl)-N-hydroxy-1- phenylcyclopent-2- enecarboxamide::US10106535, Example 35::US9617259, 35 Histone deacetylase 4 Homo sapiens 340 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293909 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293909&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117618898 381617025 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560041 Cc1ncc(Cl)cc1C1=C[C@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C19H18ClFN2O2/c1-11-16(4-3-5-17(11)21)19(18(24)23-25)7-6-13(9-19)15-8-14(20)10-22-12(15)2/h3-5,8-10,25H,6-7H2,1-2H3,(H,23,24)/t19-/m0/s1 RKCKQADYDVNGMV-IBGZPJMESA-N 293910 (S)-3-(5-Chloro-2- methylpyridin-3-yl)-1-(3- fluoro-2-methylphenyl)- N-hydroxycyclopent-2- enecarboxamide::US10106535, Example 36::US9617259, 36 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293910 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293910&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303455 381617026 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560042 Cc1ncccc1C1=C[C@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C19H19FN2O2/c1-12-16(6-3-7-17(12)20)19(18(23)22-24)9-8-14(11-19)15-5-4-10-21-13(15)2/h3-7,10-11,24H,8-9H2,1-2H3,(H,22,23)/t19-/m0/s1 GQGVQIFPWSLOPP-IBGZPJMESA-N 293911 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(2- methylpyridin-3- yl)cyclopent-2- enecarboxamide::US10106535, Example 37::US9617259, 37 Histone deacetylase 4 Homo sapiens 10.00 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293911 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293911&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303457 381617027 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560043 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccc2cnn(C)c2c1)C(=O)NO InChI=1S/C21H20FN3O2/c1-13-17(4-3-5-18(13)22)21(20(26)24-27)9-8-15(11-21)14-6-7-16-12-23-25(2)19(16)10-14/h3-7,10-12,27H,8-9H2,1-2H3,(H,24,26)/t21-/m0/s1 ZDSIXTBAUGAZCR-NRFANRHFSA-N 293912 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(1-methyl-1H- indazol-6-yl)cyclopent-2- enecarboxamide::US10106535, Example 38::US9617259, 38 Histone deacetylase 4 Homo sapiens 10.00 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293912 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293912&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 78426345 381617028 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560044 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccc2cnn(C(F)F)c2c1)C(=O)NO InChI=1S/C21H18F3N3O2/c1-12-16(3-2-4-17(12)22)21(19(28)26-29)8-7-14(10-21)13-5-6-15-11-25-27(20(23)24)18(15)9-13/h2-6,9-11,20,29H,7-8H2,1H3,(H,26,28)/t21-/m0/s1 LVTKXKMYMQSINN-NRFANRHFSA-N 293913 (S)-3-(1-(Difluoromethyl)- 1H-indazol-6-yl)-1-(3- fluoro-2-methylphenyl)- N-hydroxycyclopent-2- enecarboxamide::US10106535, Example 39::US9617259, 39 Histone deacetylase 4 Homo sapiens 30.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293913 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293913&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303458 381617029 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560045 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccc2scnc2c1)C(=O)NO InChI=1S/C20H17FN2O2S/c1-12-15(3-2-4-16(12)21)20(19(24)23-25)8-7-14(10-20)13-5-6-18-17(9-13)22-11-26-18/h2-6,9-11,25H,7-8H2,1H3,(H,23,24)/t20-/m0/s1 HXAIVDPOBQLVPY-FQEVSTJZSA-N 293914 (S)-3-(Benzo[d]thiazol-5- yl)-1-(3-fluoro-2- methylphenyl)-N- hydroxycyclopent-2- enecarboxamide::US10106535, Example 40::US9617259, 40 Histone deacetylase 4 Homo sapiens 10.00 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293914 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293914&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117622260 381617030 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560046 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cc2ccccc2s1)C(=O)NO InChI=1S/C21H18FNO2S/c1-13-16(6-4-7-17(13)22)21(20(24)23-25)10-9-15(12-21)19-11-14-5-2-3-8-18(14)26-19/h2-8,11-12,25H,9-10H2,1H3,(H,23,24)/t21-/m0/s1 FWPZFEGPZBVSGU-NRFANRHFSA-N 293915 (S)-3-(Benzo[b]thiophen- 2-yl)-1-(3-fluoro-2- methylphenyl)-N- hydroxycyclopent-2- enecarboxamide::US10106535, Example 41::US9617259, 41 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293915 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293915&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303606 381617031 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560047 Cc1c(F)c(F)ccc1[C@@]1(CCC(=C1)c1ccc2cnn(C)c2c1)C(=O)NO InChI=1S/C21H19F2N3O2/c1-12-16(5-6-17(22)19(12)23)21(20(27)25-28)8-7-14(10-21)13-3-4-15-11-24-26(2)18(15)9-13/h3-6,9-11,28H,7-8H2,1-2H3,(H,25,27)/t21-/m0/s1 PKUPZMGABYXSCK-NRFANRHFSA-N 293916 (S)-1-(3,4-Difluoro-2- methylphenyl)-N- hydroxy-3-(1-methyl-1H- indazol-6-yl)cyclopent-2- enecarboxamide::US10106535, Example 42::US9617259, 42 Histone deacetylase 4 Homo sapiens 10.00 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293916 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293916&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303607 381617032 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560048 ONC(=O)C1(CCC(=CC1)c1cncc(F)c1)c1ccccc1 InChI=1S/C18H17FN2O2/c19-16-10-14(11-20-12-16)13-6-8-18(9-7-13,17(22)21-23)15-4-2-1-3-5-15/h1-6,10-12,23H,7-9H2,(H,21,22) VZJBRHOEUHTLHH-UHFFFAOYSA-N 293917 4-(5-Fluoropyridin-3-yl)- N-hydroxy-1,2,3,6- tetrahydro-[1,1'-biphenyl]- 1-carboxamide::US10106535, Example 43::US9617259, 43 Histone deacetylase 4 Homo sapiens 3600 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293917 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293917&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303608 381617033 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560049 Cc1c(F)cccc1C1(CCC(=CC1)c1cncc(F)c1)C(=O)NO InChI=1S/C19H18F2N2O2/c1-12-16(3-2-4-17(12)21)19(18(24)23-25)7-5-13(6-8-19)14-9-15(20)11-22-10-14/h2-5,9-11,25H,6-8H2,1H3,(H,23,24) ICXLDDDYWDJOGL-UHFFFAOYSA-N 293918 3'-Fluoro-4-(5- fluoropyridin-3-yl)-N- hydroxy-2'-methyl- 1,2,3,6-tetrahydro-[1,1'- biphenyl]-1-carboxamide::US10106535, Example 44::US9617259, 44 Histone deacetylase 4 Homo sapiens 490 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293918 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293918&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117604088 381617034 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 560050 Cc1c(F)cccc1C1(CCC(=CC1)c1ccc2nccnc2c1)C(=O)NO InChI=1S/C22H20FN3O2/c1-14-17(3-2-4-18(14)23)22(21(27)26-28)9-7-15(8-10-22)16-5-6-19-20(13-16)25-12-11-24-19/h2-7,11-13,28H,8-10H2,1H3,(H,26,27) NJRAEAUTKHCVFM-UHFFFAOYSA-N 293919 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(quinoxalin-6- yl)cyclopent-2- enecarboxamide::US10106535, Example 45::US9617259, 45 Histone deacetylase 4 Homo sapiens 550 US Patent 10.7270/Q2F47R6G aid1795898 US10106535 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293919 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293919&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117622261 381617035 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619603 Cc1c(F)cccc1[C@]1(CCC(=C1)c1ccccc1)C(=O)NO InChI=1S/C19H18FNO2/c1-13-16(8-5-9-17(13)20)19(18(22)21-23)11-10-15(12-19)14-6-3-2-4-7-14/h2-9,12,23H,10-11H2,1H3,(H,21,22)/t19-/m1/s1 SCXQMYOBRMHEHW-LJQANCHMSA-N 293875 (R)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3- phenylcyclopent-2- enecarboxamide::US10106535, Example 1::US9617259, 1 Histone deacetylase 4 Homo sapiens 7600 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293875 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293875&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302815 381614145 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619604 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccccc1)C(=O)NO InChI=1S/C19H18FNO2/c1-13-16(8-5-9-17(13)20)19(18(22)21-23)11-10-15(12-19)14-6-3-2-4-7-14/h2-9,12,23H,10-11H2,1H3,(H,21,22)/t19-/m0/s1 SCXQMYOBRMHEHW-IBGZPJMESA-N 293876 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3- phenylcyclopent-2- enecarboxamide::US10106535, Example 2::US9617259, 2 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293876 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293876&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302816 381614146 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619605 Cc1ccccc1C1=C[C@@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C20H20FNO2/c1-13-6-3-4-7-16(13)15-10-11-20(12-15,19(23)22-24)17-8-5-9-18(21)14(17)2/h3-9,12,24H,10-11H2,1-2H3,(H,22,23)/t20-/m1/s1 XMEPHEZCBJENHK-HXUWFJFHSA-N 293877 (R)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(o- tolyl)cyclopent-2- enecarboxamide::US10106535, Example 3::US9617259, 3 Histone deacetylase 4 Homo sapiens 230 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293877 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293877&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302817 381614147 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619606 Cc1ccccc1C1=C[C@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C20H20FNO2/c1-13-6-3-4-7-16(13)15-10-11-20(12-15,19(23)22-24)17-8-5-9-18(21)14(17)2/h3-9,12,24H,10-11H2,1-2H3,(H,22,23)/t20-/m0/s1 XMEPHEZCBJENHK-FQEVSTJZSA-N 293878 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(o- tolyl)cyclopent-2- enecarboxamide::US10106535, Example 4::US9617259, 4 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293878 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293878&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302818 381614148 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619607 Cc1c(F)cccc1[C@]1(CCC(=C1)c1cncc(F)c1)C(=O)NO InChI=1S/C18H16F2N2O2/c1-11-15(3-2-4-16(11)20)18(17(23)22-24)6-5-12(8-18)13-7-14(19)10-21-9-13/h2-4,7-10,24H,5-6H2,1H3,(H,22,23)/t18-/m1/s1 UBYLOIIQGDRWBE-GOSISDBHSA-N 293879 (R)-1-(3-Fluoro-2- methylphenyl)-3-(5- fluoropyridin-3-yl)-N- hydroxycyclopent-2- enecarboxamide::US10106535, Example 5::US9617259, 5 Histone deacetylase 4 Homo sapiens 670 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293879 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293879&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302819 381614149 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619608 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cncc(F)c1)C(=O)NO InChI=1S/C18H16F2N2O2/c1-11-15(3-2-4-16(11)20)18(17(23)22-24)6-5-12(8-18)13-7-14(19)10-21-9-13/h2-4,7-10,24H,5-6H2,1H3,(H,22,23)/t18-/m0/s1 UBYLOIIQGDRWBE-SFHVURJKSA-N 293880 (S)-1-(3-Fluoro-2- methylphenyl)-3-(5- fluoropyridin-3-yl)-N- hydroxycyclopent-2- enecarboxamide::US10106535, Example 6::US9617259, 6 Histone deacetylase 4 Homo sapiens 10.00 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293880 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293880&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302820 381614150 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619609 Cc1c(F)cccc1[C@]1(CCC(=C1)c1cnccn1)C(=O)NO InChI=1S/C17H16FN3O2/c1-11-13(3-2-4-14(11)18)17(16(22)21-23)6-5-12(9-17)15-10-19-7-8-20-15/h2-4,7-10,23H,5-6H2,1H3,(H,21,22)/t17-/m1/s1 KPAWOECHWHNXRI-QGZVFWFLSA-N 293881 (R)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(pyrazin-2- yl)cyclopent-2- enecarboxamide::US10106535, Example 7::US9617259, 7 Histone deacetylase 4 Homo sapiens >50000 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293881 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293881&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302821 381614151 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619610 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cnccn1)C(=O)NO InChI=1S/C17H16FN3O2/c1-11-13(3-2-4-14(11)18)17(16(22)21-23)6-5-12(9-17)15-10-19-7-8-20-15/h2-4,7-10,23H,5-6H2,1H3,(H,21,22)/t17-/m0/s1 KPAWOECHWHNXRI-KRWDZBQOSA-N 293882 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(pyrazin-2- yl)cyclopent-2- enecarboxamide::US10106535, Example 8::US9617259, 8 Histone deacetylase 4 Homo sapiens 2400 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293882 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293882&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302977 381614152 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619611 Cc1cnc(cn1)C1=C[C@@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C18H18FN3O2/c1-11-9-21-16(10-20-11)13-6-7-18(8-13,17(23)22-24)14-4-3-5-15(19)12(14)2/h3-5,8-10,24H,6-7H2,1-2H3,(H,22,23)/t18-/m1/s1 WWBZXBJOLGECDP-GOSISDBHSA-N 316848 (R)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(2- methylpyrimidin-5- yl)cyclopent-2- enecarboxamide::US9617259, 9 Histone deacetylase 4 Homo sapiens 26800 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=316848 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=316848&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118699129 384220180 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619612 Cc1cnc(cn1)C1=C[C@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C18H18FN3O2/c1-11-9-21-16(10-20-11)13-6-7-18(8-13,17(23)22-24)14-4-3-5-15(19)12(14)2/h3-5,8-10,24H,6-7H2,1-2H3,(H,22,23)/t18-/m0/s1 WWBZXBJOLGECDP-SFHVURJKSA-N 316849 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(2- methylpyrimidin-5- yl)cyclopent-2- enecarboxamide::US9617259, 10 Histone deacetylase 4 Homo sapiens 40.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=316849 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=316849&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118699119 384220181 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619613 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cncc(Cl)c1)C(=O)NO InChI=1S/C18H16ClFN2O2/c1-11-15(3-2-4-16(11)20)18(17(23)22-24)6-5-12(8-18)13-7-14(19)10-21-9-13/h2-4,7-10,24H,5-6H2,1H3,(H,22,23)/t18-/m0/s1 RHEXMBJUOFFAAI-SFHVURJKSA-N 293885 (S)-3-(5-Chloropyridin-3- yl)-1-(3-fluoro-2- methylphenyl)-N- hydroxycyclopent-2- enecarboxamide::US10106535, Example 11::US9617259, 11 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293885 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293885&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302980 381614155 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619614 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccc2nccnc2c1)C(=O)NO InChI=1S/C21H18FN3O2/c1-13-16(3-2-4-17(13)22)21(20(26)25-27)8-7-15(12-21)14-5-6-18-19(11-14)24-10-9-23-18/h2-6,9-12,27H,7-8H2,1H3,(H,25,26)/t21-/m0/s1 CHWSCSWQGMLYOD-NRFANRHFSA-N 293886 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(quinoxalin-6- yl)cyclopent-2- enecarboxamide::US10106535, Example 12::US9617259, 12 Histone deacetylase 4 Homo sapiens 10.00 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293886 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293886&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302981 381614156 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619615 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccnc(c1)C(F)(F)F)C(=O)NO InChI=1S/C19H16F4N2O2/c1-11-14(3-2-4-15(11)20)18(17(26)25-27)7-5-13(10-18)12-6-8-24-16(9-12)19(21,22)23/h2-4,6,8-10,27H,5,7H2,1H3,(H,25,26)/t18-/m0/s1 RTXWXKMNNKTFFM-SFHVURJKSA-N 293887 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(2- (trifluoromethyl)pyridin- 4-yl)cyclopent-2- enecarboxamide::US10106535, Example 13::US9617259, 13 Histone deacetylase 4 Homo sapiens 40.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293887 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293887&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302982 381614157 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619616 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cncnc1)C(=O)NO InChI=1S/C17H16FN3O2/c1-11-14(3-2-4-15(11)18)17(16(22)21-23)6-5-12(7-17)13-8-19-10-20-9-13/h2-4,7-10,23H,5-6H2,1H3,(H,21,22)/t17-/m0/s1 WIBZOPAYZTWUAG-KRWDZBQOSA-N 293888 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(pyrimidin-5- yl)cyclopent-2- enecarboxamide::US10106535, Example 14::US9617259, 14 Histone deacetylase 4 Homo sapiens 30.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293888 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293888&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86302983 381614158 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619617 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccc(F)cn1)C(=O)NO InChI=1S/C18H16F2N2O2/c1-11-14(3-2-4-15(11)20)18(17(23)22-24)8-7-12(9-18)16-6-5-13(19)10-21-16/h2-6,9-10,24H,7-8H2,1H3,(H,22,23)/t18-/m0/s1 IKZXPALLSJENTD-SFHVURJKSA-N 293889 (S)-1-(3-Fluoro-2- methylphenyl)-3-(5- fluoropyridin-2-yl)-N- hydroxycyclopent-2- enecarboxamide::US10106535, Example 15::US9617259, 15 Histone deacetylase 4 Homo sapiens 40.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293889 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293889&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303139 381614159 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619618 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccc(nc1)C(F)(F)F)C(=O)NO InChI=1S/C19H16F4N2O2/c1-11-14(3-2-4-15(11)20)18(17(26)25-27)8-7-12(9-18)13-5-6-16(24-10-13)19(21,22)23/h2-6,9-10,27H,7-8H2,1H3,(H,25,26)/t18-/m0/s1 HQDKBLZLYAJTGA-SFHVURJKSA-N 293890 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(6- (trifluoromethyl)pyridin- 3-yl)cyclopent-2- enecarboxamide::US10106535, Example 16::US9617259, 16 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293890 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293890&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303140 381614160 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619619 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cncc(c1)C(F)(F)F)C(=O)NO InChI=1S/C19H16F4N2O2/c1-11-15(3-2-4-16(11)20)18(17(26)25-27)6-5-12(8-18)13-7-14(10-24-9-13)19(21,22)23/h2-4,7-10,27H,5-6H2,1H3,(H,25,26)/t18-/m0/s1 GGFUMFGWFPMRIT-SFHVURJKSA-N 293891 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(5- (trifluoromethyl)pyridin- 3-yl)cyclopent-2- enecarboxamide::US10106535, Example 17::US9617259, 17 Histone deacetylase 4 Homo sapiens 30.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293891 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293891&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303141 381614161 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619620 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cnn(c1)C(F)F)C(=O)NO InChI=1S/C17H16F3N3O2/c1-10-13(3-2-4-14(10)18)17(15(24)22-25)6-5-11(7-17)12-8-21-23(9-12)16(19)20/h2-4,7-9,16,25H,5-6H2,1H3,(H,22,24)/t17-/m0/s1 FOMINESAMTVGQU-KRWDZBQOSA-N 293892 (S)-3-(1-(Difluoromethyl)- 1H-pyrazol-4-yl)-1-(3- fluoro-2-methylphenyl)- N-hydroxycyclopent-2- enecarboxamide::US10106535, Example 18::US9617259, 18 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293892 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293892&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303142 381614162 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619621 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cc(F)cnc1C1CC1)C(=O)NO InChI=1S/C21H20F2N2O2/c1-12-17(3-2-4-18(12)23)21(20(26)25-27)8-7-14(10-21)16-9-15(22)11-24-19(16)13-5-6-13/h2-4,9-11,13,27H,5-8H2,1H3,(H,25,26)/t21-/m0/s1 OETMIHHGNBWUIE-NRFANRHFSA-N 293893 (S)-3-(2-Cyclopropyl-5- fluoropyridin-3-yl)-1-(3- fluoro-2-methylphenyl)- N-hydroxycyclopent-2- enecarboxamide::US10106535, Example 19::US9617259, 19 Histone deacetylase 4 Homo sapiens 40.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293893 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293893&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303143 381614163 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619622 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccc2nc(cnc2c1)C(F)(F)F)C(=O)NO InChI=1S/C22H17F4N3O2/c1-12-15(3-2-4-16(12)23)21(20(30)29-31)8-7-14(10-21)13-5-6-17-18(9-13)27-11-19(28-17)22(24,25)26/h2-6,9-11,31H,7-8H2,1H3,(H,29,30)/t21-/m0/s1 PEGKKBIYYUMQNV-NRFANRHFSA-N 293894 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(2- (trifluoromethyl)quinoxalin- 6-yl)cyclopent-2- enecarboxamide::US10106535, Example 20::US9617259, 20 Histone deacetylase 4 Homo sapiens 70.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293894 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293894&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303144 381614164 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619623 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccn2ccnc2c1)C(=O)NO InChI=1S/C20H18FN3O2/c1-13-16(3-2-4-17(13)21)20(19(25)23-26)7-5-15(12-20)14-6-9-24-10-8-22-18(24)11-14/h2-4,6,8-12,26H,5,7H2,1H3,(H,23,25)/t20-/m0/s1 YZHROUDNYPZPHH-FQEVSTJZSA-N 293895 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(imidazo[1,2- a]pyridin-7-yl)cyclopent- 2-enecarboxamide::US10106535, Example 21::US9617259, 21 Histone deacetylase 4 Homo sapiens 10.00 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293895 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293895&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303145 381614165 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619624 Cc1noc2ccc(cc12)C1=C[C@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C21H19FN2O3/c1-12-17(4-3-5-18(12)22)21(20(25)23-26)9-8-15(11-21)14-6-7-19-16(10-14)13(2)24-27-19/h3-7,10-11,26H,8-9H2,1-2H3,(H,23,25)/t21-/m0/s1 XEIQOCJVBFLFRP-NRFANRHFSA-N 293896 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(3- methylbenzo[d]isoxazol- 5-yl)cyclopent-2- enecarboxamide::US10106535, Example 22::US9617259, 22 Histone deacetylase 4 Homo sapiens 30.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293896 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293896&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303609 381614166 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619625 COc1ncc(cc1F)C1=C[C@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C19H18F2N2O3/c1-11-14(4-3-5-15(11)20)19(18(24)23-25)7-6-12(9-19)13-8-16(21)17(26-2)22-10-13/h3-5,8-10,25H,6-7H2,1-2H3,(H,23,24)/t19-/m0/s1 GQXSBKPOHFDJCM-IBGZPJMESA-N 293897 (S)-1-(3-Fluoro-2- methylphenyl)-3-(5- fluoro-6-methoxypyridin- 3-yl)-N- hydroxycyclopent-2- enecarboxamide::US10106535, Example 23::US9617259, 23 Histone deacetylase 4 Homo sapiens 40.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293897 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293897&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303294 381614167 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619626 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cnc(nc1)C1CC1)C(=O)NO InChI=1S/C20H20FN3O2/c1-12-16(3-2-4-17(12)21)20(19(25)24-26)8-7-14(9-20)15-10-22-18(23-11-15)13-5-6-13/h2-4,9-11,13,26H,5-8H2,1H3,(H,24,25)/t20-/m0/s1 LXFQZWLCATUSEA-FQEVSTJZSA-N 293898 (S)-3-(2- Cyclopropylpyrimidin-5- yl)-1-(3-fluoro-2- methylphenyl)-N- hydroxycyclopent-2- enecarboxamide::US10106535, Example 24::US9617259, 24 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293898 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293898&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303295 381614168 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619627 Cc1ccc(cn1)C1=C[C@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C19H19FN2O2/c1-12-6-7-15(11-21-12)14-8-9-19(10-14,18(23)22-24)16-4-3-5-17(20)13(16)2/h3-7,10-11,24H,8-9H2,1-2H3,(H,22,23)/t19-/m0/s1 QJUUVIUVFUKTMQ-IBGZPJMESA-N 293899 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(6- methylpyridin-3- yl)cyclopent-2- enecarboxamide::US10106535, Example 25::US9617259, 25 Histone deacetylase 4 Homo sapiens 10.00 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293899 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293899&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303298 381614169 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619628 Cc1ncc(cc1Cl)C1=C[C@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C19H18ClFN2O2/c1-11-15(4-3-5-17(11)21)19(18(24)23-25)7-6-13(9-19)14-8-16(20)12(2)22-10-14/h3-5,8-10,25H,6-7H2,1-2H3,(H,23,24)/t19-/m0/s1 IZSSBCOCGWWLDH-IBGZPJMESA-N 293900 (S)-3-(5-Chloro-6- methylpyridin-3-yl)-1-(3- fluoro-2-methylphenyl)- N-hydroxycyclopent-2- enecarboxamide::US10106535, Example 26::US9617259, 26 Histone deacetylase 4 Homo sapiens 10.00 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293900 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293900&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303297 381614170 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619629 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccnn1C)C(=O)NO InChI=1S/C17H18FN3O2/c1-11-13(4-3-5-14(11)18)17(16(22)20-23)8-6-12(10-17)15-7-9-19-21(15)2/h3-5,7,9-10,23H,6,8H2,1-2H3,(H,20,22)/t17-/m0/s1 FCSQJTXZDUDBJM-KRWDZBQOSA-N 293901 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(1-methyl-1H- pyrazol-5-yl)cyclopent-2- enecarboxamide::US10106535, Example 27::US9617259, 27 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293901 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293901&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303296 381614171 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619630 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cnn(CC(F)(F)F)c1)C(=O)NO InChI=1S/C18H17F4N3O2/c1-11-14(3-2-4-15(11)19)17(16(26)24-27)6-5-12(7-17)13-8-23-25(9-13)10-18(20,21)22/h2-4,7-9,27H,5-6,10H2,1H3,(H,24,26)/t17-/m0/s1 UEBUMEGYICYBBJ-KRWDZBQOSA-N 293902 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(1-(2,2,2- trifluoroethyl)-1H- pyrazol-4-yl)cyclopent-2- enecarboxamide::US10106535, Example 28::US9617259, 28 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293902 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293902&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303299 381617018 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619631 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cccc2cnsc12)C(=O)NO InChI=1S/C20H17FN2O2S/c1-12-16(6-3-7-17(12)21)20(19(24)23-25)9-8-13(10-20)15-5-2-4-14-11-22-26-18(14)15/h2-7,10-11,25H,8-9H2,1H3,(H,23,24)/t20-/m0/s1 CNBJREROOOWMRM-FQEVSTJZSA-N 293903 (S)-3-(Benzo[d]isothiazol- 7-yl)-1-(3-fluoro-2- methylphenyl)-N- hydroxycyclopent-2- enecarboxamide::US10106535, Example 29::US9617259, 29 Histone deacetylase 4 Homo sapiens 30.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293903 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293903&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303610 381617019 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619632 ONC(=O)C1(CC=CC1)c1ccccc1 InChI=1S/C12H13NO2/c14-11(13-15)12(8-4-5-9-12)10-6-2-1-3-7-10/h1-7,15H,8-9H2,(H,13,14) LZEJGKGJKBWHBU-UHFFFAOYSA-N 316869 N-Hydroxy-1- phenylcyclopent-3- enecarboxamide::US9617259, 30 Histone deacetylase 4 Homo sapiens 12300 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=316869 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=316869&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117622244 384220201 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619633 ONC(=O)C1(CC=CC1)c1ccccc1F InChI=1S/C12H12FNO2/c13-10-6-2-1-5-9(10)12(11(15)14-16)7-3-4-8-12/h1-6,16H,7-8H2,(H,14,15) PGXHBLNNBFBHQE-UHFFFAOYSA-N 293905 1-(2-Fluorophenyl)-N- hydroxycyclopent-3- enecarboxamide::US10106535, Example 31::US9617259, 31 Histone deacetylase 4 Homo sapiens 8300 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293905 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293905&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303301 381617021 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619634 Cc1c(F)cccc1[C@@]1(CCC(=C1)C1CC1)C(=O)NO InChI=1S/C16H18FNO2/c1-10-13(3-2-4-14(10)17)16(15(19)18-20)8-7-12(9-16)11-5-6-11/h2-4,9,11,20H,5-8H2,1H3,(H,18,19)/t16-/m0/s1 SSJSHINFMGPHNV-INIZCTEOSA-N 293906 (S)-3-Cyclopropyl-1-(3- fluoro-2-methylphenyl)- N-hydroxycyclopent-2- enecarboxamide::US10106535, Example 32::US9617259, 32 Histone deacetylase 4 Homo sapiens 40.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293906 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293906&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303452 381617022 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619635 ONC(=O)[C@]1(CCC(=C1)c1ccccc1)c1ccccc1 InChI=1S/C18H17NO2/c20-17(19-21)18(16-9-5-2-6-10-16)12-11-15(13-18)14-7-3-1-4-8-14/h1-10,13,21H,11-12H2,(H,19,20)/t18-/m0/s1 LTWVYNGVRLUGEE-SFHVURJKSA-N 293907 (S)-N-Hydroxy-1,3- diphenylcyclopent-2- enecarboxamide::US10106535, Example 33::US9617259, 33 Histone deacetylase 4 Homo sapiens 190 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293907 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293907&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303453 381617023 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619636 ONC(=O)[C@@]1(CCC(=C1)c1ccccc1)c1ccccc1 InChI=1S/C18H17NO2/c20-17(19-21)18(16-9-5-2-6-10-16)12-11-15(13-18)14-7-3-1-4-8-14/h1-10,13,21H,11-12H2,(H,19,20)/t18-/m1/s1 LTWVYNGVRLUGEE-GOSISDBHSA-N 293908 (R)-N-Hydroxy-1,3- diphenylcyclopent-2- enecarboxamide::US10106535, Example 34::US9617259, 34 Histone deacetylase 4 Homo sapiens 31000 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293908 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293908&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303454 381617024 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619637 ONC(=O)[C@]1(CCC(=C1)c1cncc(F)c1)c1ccccc1 InChI=1S/C17H15FN2O2/c18-15-8-13(10-19-11-15)12-6-7-17(9-12,16(21)20-22)14-4-2-1-3-5-14/h1-5,8-11,22H,6-7H2,(H,20,21)/t17-/m0/s1 WVTONWZRSXXBPD-KRWDZBQOSA-N 293909 (S)-3-(5-Fluoropyridin-3- yl)-N-hydroxy-1- phenylcyclopent-2- enecarboxamide::US10106535, Example 35::US9617259, 35 Histone deacetylase 4 Homo sapiens 340 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293909 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293909&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117618898 381617025 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619638 Cc1ncc(Cl)cc1C1=C[C@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C19H18ClFN2O2/c1-11-16(4-3-5-17(11)21)19(18(24)23-25)7-6-13(9-19)15-8-14(20)10-22-12(15)2/h3-5,8-10,25H,6-7H2,1-2H3,(H,23,24)/t19-/m0/s1 RKCKQADYDVNGMV-IBGZPJMESA-N 293910 (S)-3-(5-Chloro-2- methylpyridin-3-yl)-1-(3- fluoro-2-methylphenyl)- N-hydroxycyclopent-2- enecarboxamide::US10106535, Example 36::US9617259, 36 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293910 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293910&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303455 381617026 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619639 Cc1ncccc1C1=C[C@](CC1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C19H19FN2O2/c1-12-16(6-3-7-17(12)20)19(18(23)22-24)9-8-14(11-19)15-5-4-10-21-13(15)2/h3-7,10-11,24H,8-9H2,1-2H3,(H,22,23)/t19-/m0/s1 GQGVQIFPWSLOPP-IBGZPJMESA-N 293911 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(2- methylpyridin-3- yl)cyclopent-2- enecarboxamide::US10106535, Example 37::US9617259, 37 Histone deacetylase 4 Homo sapiens 10.00 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293911 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293911&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303457 381617027 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619640 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccc2cnn(C)c2c1)C(=O)NO InChI=1S/C21H20FN3O2/c1-13-17(4-3-5-18(13)22)21(20(26)24-27)9-8-15(11-21)14-6-7-16-12-23-25(2)19(16)10-14/h3-7,10-12,27H,8-9H2,1-2H3,(H,24,26)/t21-/m0/s1 ZDSIXTBAUGAZCR-NRFANRHFSA-N 293912 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(1-methyl-1H- indazol-6-yl)cyclopent-2- enecarboxamide::US10106535, Example 38::US9617259, 38 Histone deacetylase 4 Homo sapiens 10.00 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293912 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293912&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 78426345 381617028 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619641 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccc2cnn(C(F)F)c2c1)C(=O)NO InChI=1S/C21H18F3N3O2/c1-12-16(3-2-4-17(12)22)21(19(28)26-29)8-7-14(10-21)13-5-6-15-11-25-27(20(23)24)18(15)9-13/h2-6,9-11,20,29H,7-8H2,1H3,(H,26,28)/t21-/m0/s1 LVTKXKMYMQSINN-NRFANRHFSA-N 293913 (S)-3-(1-(Difluoromethyl)- 1H-indazol-6-yl)-1-(3- fluoro-2-methylphenyl)- N-hydroxycyclopent-2- enecarboxamide::US10106535, Example 39::US9617259, 39 Histone deacetylase 4 Homo sapiens 30.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293913 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293913&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303458 381617029 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619642 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1ccc2scnc2c1)C(=O)NO InChI=1S/C20H17FN2O2S/c1-12-15(3-2-4-16(12)21)20(19(24)23-25)8-7-14(10-20)13-5-6-18-17(9-13)22-11-26-18/h2-6,9-11,25H,7-8H2,1H3,(H,23,24)/t20-/m0/s1 HXAIVDPOBQLVPY-FQEVSTJZSA-N 293914 (S)-3-(Benzo[d]thiazol-5- yl)-1-(3-fluoro-2- methylphenyl)-N- hydroxycyclopent-2- enecarboxamide::US10106535, Example 40::US9617259, 40 Histone deacetylase 4 Homo sapiens 10.00 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293914 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293914&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117622260 381617030 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619643 Cc1c(F)cccc1[C@@]1(CCC(=C1)c1cc2ccccc2s1)C(=O)NO InChI=1S/C21H18FNO2S/c1-13-16(6-4-7-17(13)22)21(20(24)23-25)10-9-15(12-21)19-11-14-5-2-3-8-18(14)26-19/h2-8,11-12,25H,9-10H2,1H3,(H,23,24)/t21-/m0/s1 FWPZFEGPZBVSGU-NRFANRHFSA-N 293915 (S)-3-(Benzo[b]thiophen- 2-yl)-1-(3-fluoro-2- methylphenyl)-N- hydroxycyclopent-2- enecarboxamide::US10106535, Example 41::US9617259, 41 Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293915 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293915&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303606 381617031 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619644 Cc1c(F)c(F)ccc1[C@@]1(CCC(=C1)c1ccc2cnn(C)c2c1)C(=O)NO InChI=1S/C21H19F2N3O2/c1-12-16(5-6-17(22)19(12)23)21(20(27)25-28)8-7-14(10-21)13-3-4-15-11-24-26(2)18(15)9-13/h3-6,9-11,28H,7-8H2,1-2H3,(H,25,27)/t21-/m0/s1 PKUPZMGABYXSCK-NRFANRHFSA-N 293916 (S)-1-(3,4-Difluoro-2- methylphenyl)-N- hydroxy-3-(1-methyl-1H- indazol-6-yl)cyclopent-2- enecarboxamide::US10106535, Example 42::US9617259, 42 Histone deacetylase 4 Homo sapiens 10.00 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293916 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293916&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303607 381617032 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619645 ONC(=O)C1(CCC(=CC1)c1cncc(F)c1)c1ccccc1 InChI=1S/C18H17FN2O2/c19-16-10-14(11-20-12-16)13-6-8-18(9-7-13,17(22)21-23)15-4-2-1-3-5-15/h1-6,10-12,23H,7-9H2,(H,21,22) VZJBRHOEUHTLHH-UHFFFAOYSA-N 293917 4-(5-Fluoropyridin-3-yl)- N-hydroxy-1,2,3,6- tetrahydro-[1,1'-biphenyl]- 1-carboxamide::US10106535, Example 43::US9617259, 43 Histone deacetylase 4 Homo sapiens 3600 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293917 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293917&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86303608 381617033 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619646 Cc1c(F)cccc1C1(CCC(=CC1)c1cncc(F)c1)C(=O)NO InChI=1S/C19H18F2N2O2/c1-12-16(3-2-4-17(12)21)19(18(24)23-25)7-5-13(6-8-19)14-9-15(20)11-22-10-14/h2-5,9-11,25H,6-8H2,1H3,(H,23,24) ICXLDDDYWDJOGL-UHFFFAOYSA-N 293918 3'-Fluoro-4-(5- fluoropyridin-3-yl)-N- hydroxy-2'-methyl- 1,2,3,6-tetrahydro-[1,1'- biphenyl]-1-carboxamide::US10106535, Example 44::US9617259, 44 Histone deacetylase 4 Homo sapiens 490 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293918 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293918&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117604088 381617034 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 619647 Cc1c(F)cccc1C1(CCC(=CC1)c1ccc2nccnc2c1)C(=O)NO InChI=1S/C22H20FN3O2/c1-14-17(3-2-4-18(14)23)22(21(27)26-28)9-7-15(8-10-22)16-5-6-19-20(13-16)25-12-11-24-19/h2-7,11-13,28H,8-10H2,1H3,(H,26,27) NJRAEAUTKHCVFM-UHFFFAOYSA-N 293919 (S)-1-(3-Fluoro-2- methylphenyl)-N- hydroxy-3-(quinoxalin-6- yl)cyclopent-2- enecarboxamide::US10106535, Example 45::US9617259, 45 Histone deacetylase 4 Homo sapiens 550 US Patent 10.7270/Q2DN4743 aid1796543 US9617259 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Luckhurst, CA; Jarvis, RE; Burli, RW; Allen, DR; Haughan, AF; Breccia, P; Vater, HD; Stott, AJ; Penrose, SD; Wall, M; Saville-Stones, EA; Wishart, G; Hughes, SJ CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=293919 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=293919&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117622261 381617035 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 636582 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q20Z75CX aid1796735 US10188756 Hooker, JM; Wang, C; Schroeder, FA The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 636606 ONC(=O)\C=C\c1ccccc1 InChI=1S/C9H9NO2/c11-9(10-12)7-6-8-4-2-1-3-5-8/h1-7,12H,(H,10,11)/b7-6+ UVDDFTZLVFIQFL-VOTSOKGWSA-N 50015088 (E)-N-Hydroxy-3-phenyl-acrylamide::(E)-N-Hydroxy-3-phenylacrylamide::CHEMBL154574::N-Hydroxy-3-phenyl-acrylamide::US10188756, Compound CN86::trans-N-Hydroxy-3-phenyl-acrylamide Histone deacetylase 4 Homo sapiens >10000 US Patent 10.7270/Q20Z75CX aid1796735 US10188756 Hooker, JM; Wang, C; Schroeder, FA The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50015088 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50015088&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5355635 103926931 CHEMBL154574 ZINC08615353 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 636615 COc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C10H11NO3/c1-14-9-5-2-8(3-6-9)4-7-10(12)11-13/h2-7,13H,1H3,(H,11,12)/b7-4+ BQDLTSGIXOYYHY-QPJJXVBHSA-N 23269 (2E)-N-hydroxy-3-(4-methoxyphenyl)prop-2-enamide::Cinnamic hydroxamate deriv., 13::US10188756, Compound CN87::US11505523, Compound PCI34051 Histone deacetylase 4 Homo sapiens >70000 US Patent 10.7270/Q20Z75CX aid1796735 US10188756 Hooker, JM; Wang, C; Schroeder, FA The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=23269 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=23269&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6433883 50091534 ZINC05298904 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 636624 CN(c1ccccc1)S(=O)(=O)c1cccc(\C=C\C(=O)NO)c1 InChI=1S/C16H16N2O4S/c1-18(14-7-3-2-4-8-14)23(21,22)15-9-5-6-13(12-15)10-11-16(19)17-20/h2-12,20H,1H3,(H,17,19)/b11-10+ XDGZMSJUKYHOFR-ZHACJKMWSA-N 323701 US10188756, Compound CN88 Histone deacetylase 4 Homo sapiens 3831 US Patent 10.7270/Q20Z75CX aid1796735 US10188756 Hooker, JM; Wang, C; Schroeder, FA The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=323701 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=323701&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 10131653 384578780 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 636633 CN(CCc1ccccc1)S(=O)(=O)c1cccc(\C=C\C(=O)NO)c1 InChI=1S/C18H20N2O4S/c1-20(13-12-15-6-3-2-4-7-15)25(23,24)17-9-5-8-16(14-17)10-11-18(21)19-22/h2-11,14,22H,12-13H2,1H3,(H,19,21)/b11-10+ VLCXJLKMJMKPJC-ZHACJKMWSA-N 323702 US10188756, Compound CN89 Histone deacetylase 4 Homo sapiens 500 US Patent 10.7270/Q20Z75CX aid1796735 US10188756 Hooker, JM; Wang, C; Schroeder, FA The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=323702 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=323702&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122548372 384578781 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 636642 CCCCc1nc2cc(\C=C\C(=O)NO)ccc2n1CCN(C)C InChI=1S/C18H26N4O2/c1-4-5-6-17-19-15-13-14(8-10-18(23)20-24)7-9-16(15)22(17)12-11-21(2)3/h7-10,13,24H,4-6,11-12H2,1-3H3,(H,20,23)/b10-8+ FDTJPEFUCCISMT-CSKARUKUSA-N 50353238 CHEMBL1830399::US10188756, Compound CN101 Histone deacetylase 4 Homo sapiens >10000 US Patent 10.7270/Q20Z75CX aid1796735 US10188756 Hooker, JM; Wang, C; Schroeder, FA The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50353238 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50353238&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 16068694 136359924 CHEMBL1830399 ZINC34987454 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 636651 Cn1cc(CCNCc2ccc(\C=C\C(=O)NO)cc2)c2ccccc12 InChI=1S/C21H23N3O2/c1-24-15-18(19-4-2-3-5-20(19)24)12-13-22-14-17-8-6-16(7-9-17)10-11-21(25)23-26/h2-11,15,22,26H,12-14H2,1H3,(H,23,25)/b11-10+ AEDUBEGTPWKDCX-ZHACJKMWSA-N 323704 US10188756, Compound CN107 Histone deacetylase 4 Homo sapiens 655 US Patent 10.7270/Q20Z75CX aid1796735 US10188756 Hooker, JM; Wang, C; Schroeder, FA The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=323704 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=323704&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11024529 384578783 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 636668 COc1ccc2Sc3ccccc3N(CCCCCC(=O)NO)C(=O)c2c1 InChI=1S/C20H22N2O4S/c1-26-14-10-11-17-15(13-14)20(24)22(12-6-2-3-9-19(23)21-25)16-7-4-5-8-18(16)27-17/h4-5,7-8,10-11,13,25H,2-3,6,9,12H2,1H3,(H,21,23) PQLSOSKDLAENJC-UHFFFAOYSA-N 323706 US10188756, Compound CN112 Histone deacetylase 4 Homo sapiens >10000 US Patent 10.7270/Q20Z75CX aid1796735 US10188756 Hooker, JM; Wang, C; Schroeder, FA The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=323706 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=323706&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122548365 384578785 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 636677 COc1ccc2c(c1)C(=O)N(CCCCCC(=O)NO)c1ccccc1S2(=O)=O InChI=1S/C20H22N2O6S/c1-28-14-10-11-17-15(13-14)20(24)22(12-6-2-3-9-19(23)21-25)16-7-4-5-8-18(16)29(17,26)27/h4-5,7-8,10-11,13,25H,2-3,6,9,12H2,1H3,(H,21,23) MRIGHUMOWXZEEI-UHFFFAOYSA-N 323707 US10188756, Compound CN113 Histone deacetylase 4 Homo sapiens 9450 US Patent 10.7270/Q20Z75CX aid1796735 US10188756 Hooker, JM; Wang, C; Schroeder, FA The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=323707 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=323707&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122548369 384578786 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 636693 CN(Cc1ccc(\C=C\C(=O)NO)cc1)CC12CC3CC(CC(C3)C1)C2 InChI=1S/C22H30N2O2/c1-24(14-17-4-2-16(3-5-17)6-7-21(25)23-26)15-22-11-18-8-19(12-22)10-20(9-18)13-22/h2-7,18-20,26H,8-15H2,1H3,(H,23,25)/b7-6+ WNIDBXBLQFPAJA-VOTSOKGWSA-N 323709 US10188756, Compound CN133::US11207431, Martinostat Histone deacetylase 4 Homo sapiens 1970 US Patent 10.7270/Q20Z75CX aid1796735 US10188756 Hooker, JM; Wang, C; Schroeder, FA The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=323709 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=323709&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90479372 384578788 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 636701 ONC(=O)\C=C\c1cccc(CNC23CC4CC(CC(C4)C2)C3)c1 InChI=1S/C20H26N2O2/c23-19(22-24)5-4-14-2-1-3-15(6-14)13-21-20-10-16-7-17(11-20)9-18(8-16)12-20/h1-6,16-18,21,24H,7-13H2,(H,22,23)/b5-4+ TUQJHTWUEYMRMU-SNAWJCMRSA-N 323710 US10188756, Compound CN139 Histone deacetylase 4 Homo sapiens 2534 US Patent 10.7270/Q20Z75CX aid1796735 US10188756 Hooker, JM; Wang, C; Schroeder, FA The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=323710 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=323710&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122548367 384578789 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 636709 CN(Cc1ccc2C=C(CCc2c1)C(=O)NO)CC12CC3CC(CC(C3)C1)C2 InChI=1S/C24H32N2O2/c1-26(15-24-11-17-6-18(12-24)8-19(7-17)13-24)14-16-2-3-21-10-22(23(27)25-28)5-4-20(21)9-16/h2-3,9-10,17-19,28H,4-8,11-15H2,1H3,(H,25,27) GOBRTECWEHXUDO-UHFFFAOYSA-N 323711 US10188756, Compound CN141 Histone deacetylase 4 Homo sapiens 389 US Patent 10.7270/Q20Z75CX aid1796735 US10188756 Hooker, JM; Wang, C; Schroeder, FA The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=323711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=323711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122548366 384578790 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 636717 ONC(=O)\C=C\c1ccc(CNCC2CCCCC2)cc1 InChI=1S/C17H24N2O2/c20-17(19-21)11-10-14-6-8-16(9-7-14)13-18-12-15-4-2-1-3-5-15/h6-11,15,18,21H,1-5,12-13H2,(H,19,20)/b11-10+ BVUOAXSMACMJMQ-ZHACJKMWSA-N 323712 US10188756, Compound CN143 Histone deacetylase 4 Homo sapiens 927 US Patent 10.7270/Q20Z75CX aid1796735 US10188756 Hooker, JM; Wang, C; Schroeder, FA The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=323712 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=323712&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118699477 384578791 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 636729 ONC(=O)\C=C\c1ccc(CN(CCF)CC23CC4CC(CC(C4)C2)C3)cc1 InChI=1S/C23H31FN2O2/c24-7-8-26(15-18-3-1-17(2-4-18)5-6-22(27)25-28)16-23-12-19-9-20(13-23)11-21(10-19)14-23/h1-6,19-21,28H,7-16H2,(H,25,27)/b6-5+ XRCTUUQPMJAHKQ-AATRIKPKSA-N 323716 US10188756, Compound CN146 Histone deacetylase 4 Homo sapiens >10000 US Patent 10.7270/Q20Z75CX aid1796735 US10188756 Hooker, JM; Wang, C; Schroeder, FA The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=323716 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=323716&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118699476 384578795 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 636738 ONC(=O)\C=C\c1ccc(CNCC23CC4CC(CC(C4)C2)C3)c(F)c1 InChI=1S/C21H27FN2O2/c22-19-8-14(2-4-20(25)24-26)1-3-18(19)12-23-13-21-9-15-5-16(10-21)7-17(6-15)11-21/h1-4,8,15-17,23,26H,5-7,9-13H2,(H,24,25)/b4-2+ AZODTJZLKVAKDP-DUXPYHPUSA-N 323717 US10188756, Compound CN148 Histone deacetylase 4 Homo sapiens >70000 US Patent 10.7270/Q20Z75CX aid1796735 US10188756 Hooker, JM; Wang, C; Schroeder, FA The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=323717 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=323717&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118699494 384578796 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 636747 CN(Cc1ccc(\C=C\C(=O)NO)cc1F)CC12CC3CC(CC(C3)C1)C2 InChI=1S/C22H29FN2O2/c1-25(14-22-10-16-6-17(11-22)8-18(7-16)12-22)13-19-4-2-15(9-20(19)23)3-5-21(26)24-27/h2-5,9,16-18,27H,6-8,10-14H2,1H3,(H,24,26)/b5-3+ JJVJGQDLQUPOQJ-HWKANZROSA-N 323718 US10188756, Compound CN149::US11207431, Example B Histone deacetylase 4 Homo sapiens 20312 US Patent 10.7270/Q20Z75CX aid1796735 US10188756 Hooker, JM; Wang, C; Schroeder, FA The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=323718 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=323718&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122550533 384578797 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681682 Cc1c(F)cccc1C1(CCC(C1)c1cccnc1)C(=O)NO InChI=1S/C18H19FN2O2/c1-12-15(5-2-6-16(12)19)18(17(22)21-23)8-7-13(10-18)14-4-3-9-20-11-14/h2-6,9,11,13,23H,7-8,10H2,1H3,(H,21,22) FQCQYLHWAYISOF-UHFFFAOYSA-N 344292 1-(3-fluoro-2-methylphenyl)-N-hydroxy-3-(pyridin-3-yl)cyclopentanecarboxamide::US9783488, Example 1 Histone deacetylase 4 Homo sapiens 190 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344292 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344292&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273207 385450380 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681683 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1cncnc1)C(=O)NO InChI=1S/C17H18FN3O2/c1-11-14(3-2-4-15(11)18)17(16(22)21-23)6-5-12(7-17)13-8-19-10-20-9-13/h2-4,8-10,12,23H,5-7H2,1H3,(H,21,22)/t12-,17+/m1/s1 HMWLZLYOKXKPDZ-PXAZEXFGSA-N 344293 (+-)-(1S*,3R*)-1-(3-Fluoro- 2-methylphenyl)-N- hydroxy-3-(pyrimidin-5- yl)cyclopentanecarboxamide::US9783488, Example 2 Histone deacetylase 4 Homo sapiens 290 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344293 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344293&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273208 385450381 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681684 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)c1cncnc1)C(=O)NO InChI=1S/C17H18FN3O2/c1-11-14(3-2-4-15(11)18)17(16(22)21-23)6-5-12(7-17)13-8-19-10-20-9-13/h2-4,8-10,12,23H,5-7H2,1H3,(H,21,22)/t12-,17-/m0/s1 HMWLZLYOKXKPDZ-SJCJKPOMSA-N 344294 (+-)-(1S*,3S*)-1-(3-Fluoro- 2-methylphenyl)-N- hydroxy-3-(pyrimidin-5- yl)cyclopentanecarboxamide::US9783488, Example 3 Histone deacetylase 4 Homo sapiens 390 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344294 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344294&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273452 385450382 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681685 Cc1c(F)cccc1[C@]1(CC[C@@H](C1)c1ccccc1)C(=O)NO InChI=1S/C19H20FNO2/c1-13-16(8-5-9-17(13)20)19(18(22)21-23)11-10-15(12-19)14-6-3-2-4-7-14/h2-9,15,23H,10-12H2,1H3,(H,21,22)/t15-,19+/m0/s1 JYKNQHQPUVIRAZ-HNAYVOBHSA-N 344295 (1R*,3S*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3- phenylcyclopentanecarboxamide::US9783488, Example 4 Histone deacetylase 4 Homo sapiens 40.0 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344295 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344295&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 78425882 385450383 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681686 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccccc1)C(=O)NO InChI=1S/C19H20FNO2/c1-13-16(8-5-9-17(13)20)19(18(22)21-23)11-10-15(12-19)14-6-3-2-4-7-14/h2-9,15,23H,10-12H2,1H3,(H,21,22)/t15-,19+/m1/s1 JYKNQHQPUVIRAZ-BEFAXECRSA-N 344296 (1S*,3R*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3- phenylcyclopentanecarboxamide::US9783488, Example 5 Histone deacetylase 4 Homo sapiens 1100 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344296 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344296&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273451 385450384 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681687 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)c1ccccc1)C(=O)NO InChI=1S/C19H20FNO2/c1-13-16(8-5-9-17(13)20)19(18(22)21-23)11-10-15(12-19)14-6-3-2-4-7-14/h2-9,15,23H,10-12H2,1H3,(H,21,22)/t15-,19-/m0/s1 JYKNQHQPUVIRAZ-KXBFYZLASA-N 344297 (1S*,3S*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3- phenylcyclopentanecarboxamide::US9783488, Example 6 Histone deacetylase 4 Homo sapiens 100.0 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344297 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344297&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273453 385450385 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681688 Cc1c(F)cccc1[C@]1(CC[C@H](C1)c1ccccc1)C(=O)NO InChI=1S/C19H20FNO2/c1-13-16(8-5-9-17(13)20)19(18(22)21-23)11-10-15(12-19)14-6-3-2-4-7-14/h2-9,15,23H,10-12H2,1H3,(H,21,22)/t15-,19-/m1/s1 JYKNQHQPUVIRAZ-DNVCBOLYSA-N 344298 (1R*,3R*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3- phenylcyclopentanecarboxamide::US9783488, Example 7 Histone deacetylase 4 Homo sapiens 50.0 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344298 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344298&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273454 385450386 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681689 Cc1ccccc1[C@H]1CC[C@@](C1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C20H22FNO2/c1-13-6-3-4-7-16(13)15-10-11-20(12-15,19(23)22-24)17-8-5-9-18(21)14(17)2/h3-9,15,24H,10-12H2,1-2H3,(H,22,23)/t15-,20-/m0/s1 RZUMZBGJTQFKEV-YWZLYKJASA-N 344299 (+-)-(1S*,3S*)1-(3-fluoro-2-methylphenyl)-N-hydroxy-3-(o-tolyl)cyclopentane carboxamide::US9783488, Example 8 Histone deacetylase 4 Homo sapiens 170 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344299 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344299&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273455 385450387 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681690 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)c1cncc(F)c1)C(=O)NO InChI=1S/C18H18F2N2O2/c1-11-15(3-2-4-16(11)20)18(17(23)22-24)6-5-12(8-18)13-7-14(19)10-21-9-13/h2-4,7,9-10,12,24H,5-6,8H2,1H3,(H,22,23)/t12-,18-/m0/s1 HZPQUCRMKHUJSP-SGTLLEGYSA-N 344300 (1S,3S*)-1-(3-Fluoro-2- methyl-phenyl)-3-(5- fluoropyridin-3-yl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 9 Histone deacetylase 4 Homo sapiens 150 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344300 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344300&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273456 385450388 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681691 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1cncc(F)c1)C(=O)NO InChI=1S/C18H18F2N2O2/c1-11-15(3-2-4-16(11)20)18(17(23)22-24)6-5-12(8-18)13-7-14(19)10-21-9-13/h2-4,7,9-10,12,24H,5-6,8H2,1H3,(H,22,23)/t12-,18+/m1/s1 HZPQUCRMKHUJSP-XIKOKIGWSA-N 344301 (1S,3R*)-1-(3-Fluoro-2- methyl-phenyl)-3-(5- fluoropyridin-3-yl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 10 Histone deacetylase 4 Homo sapiens 140 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344301 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344301&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273457 385450389 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681692 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)c1ccc(F)cn1)C(=O)NO InChI=1S/C18H18F2N2O2/c1-11-14(3-2-4-15(11)20)18(17(23)22-24)8-7-12(9-18)16-6-5-13(19)10-21-16/h2-6,10,12,24H,7-9H2,1H3,(H,22,23)/t12-,18-/m0/s1 IZQVGCIYVQFAAL-SGTLLEGYSA-N 344304 (1S,3S*)-1-(3-Fluoro-2- methylphenyl)-3-(5- fluoropyridin-2-yl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 11 Histone deacetylase 4 Homo sapiens 200 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344304 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344304&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117618952 385450392 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681693 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccc(F)cn1)C(=O)NO InChI=1S/C18H18F2N2O2/c1-11-14(3-2-4-15(11)20)18(17(23)22-24)8-7-12(9-18)16-6-5-13(19)10-21-16/h2-6,10,12,24H,7-9H2,1H3,(H,22,23)/t12-,18+/m1/s1 IZQVGCIYVQFAAL-XIKOKIGWSA-N 344305 (1S,3R*)-1-(3-Fluoro-2- methylphenyl)-3-(5- fluoropyridin-2-yl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 12 Histone deacetylase 4 Homo sapiens 240 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344305 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344305&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117618950 385450393 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681694 ONC(=O)[C@]1(CC[C@@H](CC1)c1cncc(F)c1)c1ccccc1 InChI=1S/C18H19FN2O2/c19-16-10-14(11-20-12-16)13-6-8-18(9-7-13,17(22)21-23)15-4-2-1-3-5-15/h1-5,10-13,23H,6-9H2,(H,21,22)/t13-,18- CPUCNCCKUXGHIN-KTXOBNNYSA-N 344306 (1r,4r)-4-(5-Fluoropyridin- 3-yl)-N-hydroxy-1- phenylcyclohexanecarboxamide::US9783488, Example 13 Histone deacetylase 4 Homo sapiens 6400 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344306 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344306&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273685 385450394 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681695 ONC(=O)[C@@]1(CC[C@@H](CC1)c1cncc(F)c1)c1ccccc1 InChI=1S/C18H19FN2O2/c19-16-10-14(11-20-12-16)13-6-8-18(9-7-13,17(22)21-23)15-4-2-1-3-5-15/h1-5,10-13,23H,6-9H2,(H,21,22)/t13-,18+ CPUCNCCKUXGHIN-QGGXVJLZSA-N 344307 (1s,4s)-4-(5- Fluoropyridin-3-yl)-N- hydroxy-1- phenylcyclohexanecarboxamide::US9783488, Example 14 Histone deacetylase 4 Homo sapiens >50000 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344307 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344307&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273685 385450395 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681696 ONC(=O)C1(CCCC1)c1cccc(F)c1F InChI=1S/C12H13F2NO2/c13-9-5-3-4-8(10(9)14)12(11(16)15-17)6-1-2-7-12/h3-5,17H,1-2,6-7H2,(H,15,16) LHRKGBYKIAKIKJ-UHFFFAOYSA-N 344308 1-(2,3-difluorophenyl)-N-hydroxycyclopentanecarboxamide::US9783488, Example 15 Histone deacetylase 4 Homo sapiens 2500 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344308 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344308&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273692 385450396 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681697 ONC(=O)C1(CCCC1)c1cccc2CCOc12 InChI=1S/C14H17NO3/c16-13(15-17)14(7-1-2-8-14)11-5-3-4-10-6-9-18-12(10)11/h3-5,17H,1-2,6-9H2,(H,15,16) YVOQLQIEYXSWML-UHFFFAOYSA-N 344309 1-(2,3-dihydrobenzofuran-7-yl)-N-hydroxycyclopentanecarboxamide::US9783488, Example 16 Histone deacetylase 4 Homo sapiens >50000 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344309 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344309&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273691 385450397 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681698 Cc1c(Cl)cccc1C1(CCCC1)C(=O)NO InChI=1S/C13H16ClNO2/c1-9-10(5-4-6-11(9)14)13(12(16)15-17)7-2-3-8-13/h4-6,17H,2-3,7-8H2,1H3,(H,15,16) DRZPXUYYAJUGPP-UHFFFAOYSA-N 344310 1-(3-chloro-2-methylphenyl)-N-hydroxycyclopentanecarboxamide::US9783488, Example 17 Histone deacetylase 4 Homo sapiens 280 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344310 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344310&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273690 385450398 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681699 Cc1c(F)cccc1C1(CCCC1)C(=O)NO InChI=1S/C13H16FNO2/c1-9-10(5-4-6-11(9)14)13(12(16)15-17)7-2-3-8-13/h4-6,17H,2-3,7-8H2,1H3,(H,15,16) NKYNMYBZTUJQRI-UHFFFAOYSA-N 344311 1-(3-fluoro-2-methylphenyl)-N-hydroxycyclopentanecarboxamide::US9783488, Example 18 Histone deacetylase 4 Homo sapiens 270 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344311 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344311&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273689 385450399 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681700 ONC(=O)C1(CCCC1)c1ccccc1F InChI=1S/C12H14FNO2/c13-10-6-2-1-5-9(10)12(11(15)14-16)7-3-4-8-12/h1-2,5-6,16H,3-4,7-8H2,(H,14,15) DZZCYEPNBKDHNR-UHFFFAOYSA-N 344312 1-(2-fluorophenyl)-N-hydroxycyclopentanecarboxamide::US9783488, Example 19 Histone deacetylase 4 Homo sapiens 4600 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344312 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344312&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273688 385450400 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681701 ONC(=O)C1(CCCC1)c1ccc(Cl)cc1 InChI=1S/C12H14ClNO2/c13-10-5-3-9(4-6-10)12(11(15)14-16)7-1-2-8-12/h3-6,16H,1-2,7-8H2,(H,14,15) DJLVFSLMNGQWFK-UHFFFAOYSA-N 344313 1-(4-chlorophenyl)-N-hydroxycyclopentanecarboxamide::US9783488, Example 20 Histone deacetylase 4 Homo sapiens 24000 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344313 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344313&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273928 385450401 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681702 ONC(=O)C1(CCCC1)c1ccccc1 InChI=1S/C12H15NO2/c14-11(13-15)12(8-4-5-9-12)10-6-2-1-3-7-10/h1-3,6-7,15H,4-5,8-9H2,(H,13,14) GXYJXDPYMIKIBT-UHFFFAOYSA-N 344314 N-Hydroxy-1- phenylcyclopentanecarboxamide::US9783488, Example 21 Histone deacetylase 4 Homo sapiens 11400 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344314 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344314&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 59191078 385450402 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681703 ONC(=O)C1(CCCC1)c1c(F)cccc1Cl InChI=1S/C12H13ClFNO2/c13-8-4-3-5-9(14)10(8)12(11(16)15-17)6-1-2-7-12/h3-5,17H,1-2,6-7H2,(H,15,16) SRYTUPRIDVCLNZ-UHFFFAOYSA-N 344315 1-(2-Chloro-6-fluorophenyl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 22 Histone deacetylase 4 Homo sapiens 2500 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344315 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344315&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273929 385450403 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681704 COc1ccccc1C1(CCCC1)C(=O)NO InChI=1S/C13H17NO3/c1-17-11-7-3-2-6-10(11)13(12(15)14-16)8-4-5-9-13/h2-3,6-7,16H,4-5,8-9H2,1H3,(H,14,15) OMFNZSZKNPTXRA-UHFFFAOYSA-N 344317 N-Hydroxy-1-(2- methoxyphenyl) cyclopentanecarboxamide::US9783488, Example 23 Histone deacetylase 4 Homo sapiens >50000 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344317 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344317&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117618949 385450405 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681705 Cc1ccccc1C1(CCCC1)C(=O)NO InChI=1S/C13H17NO2/c1-10-6-2-3-7-11(10)13(12(15)14-16)8-4-5-9-13/h2-3,6-7,16H,4-5,8-9H2,1H3,(H,14,15) HFFPLDGWCBIFKQ-UHFFFAOYSA-N 344318 N-Hydroxy-1-o- tolylcyclopentanecarboxamide::US9783488, Example 24 Histone deacetylase 4 Homo sapiens 730 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344318 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344318&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273930 385450406 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681706 Cc1cccc(c1)C1(CCCC1)C(=O)NO InChI=1S/C13H17NO2/c1-10-5-4-6-11(9-10)13(12(15)14-16)7-2-3-8-13/h4-6,9,16H,2-3,7-8H2,1H3,(H,14,15) HVFIBXAWOUMCEC-UHFFFAOYSA-N 344319 N-Hydroxy-1-m- tolylcyclopentanecarboxamide::US9783488, Example 25 Histone deacetylase 4 Homo sapiens 8200 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344319 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344319&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273931 385450407 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681707 ONC(=O)C1(CCCC1)c1ccccc1Cl InChI=1S/C12H14ClNO2/c13-10-6-2-1-5-9(10)12(11(15)14-16)7-3-4-8-12/h1-2,5-6,16H,3-4,7-8H2,(H,14,15) NKJCIAOSWCVLPI-UHFFFAOYSA-N 344320 1-(2-Chlorophenyl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 26 Histone deacetylase 4 Homo sapiens 1900 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344320 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344320&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273932 385450408 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681708 ONC(=O)C1(CCCC1)c1ccccc1C#N InChI=1S/C13H14N2O2/c14-9-10-5-1-2-6-11(10)13(12(16)15-17)7-3-4-8-13/h1-2,5-6,17H,3-4,7-8H2,(H,15,16) VBVKXZXDHRQDAM-UHFFFAOYSA-N 344321 1-(2-Cyanophenyl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 27 Histone deacetylase 4 Homo sapiens >50000 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344321 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344321&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273933 385450409 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681709 ONC(=O)C1(CCCC1)c1cccc(c1)C#N InChI=1S/C13H14N2O2/c14-9-10-4-3-5-11(8-10)13(12(16)15-17)6-1-2-7-13/h3-5,8,17H,1-2,6-7H2,(H,15,16) SZDCTCHEFMPRFE-UHFFFAOYSA-N 344322 1-(3-Cyanophenyl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 28 Histone deacetylase 4 Homo sapiens >50000 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344322 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344322&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273934 385450410 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681710 Cc1c(F)c(F)ccc1C1(CCCC1)C(=O)NO InChI=1S/C13H15F2NO2/c1-8-9(4-5-10(14)11(8)15)13(12(17)16-18)6-2-3-7-13/h4-5,18H,2-3,6-7H2,1H3,(H,16,17) LPGDISHQDPWDKY-UHFFFAOYSA-N 344323 1-(3,4-Difluoro-2-methylphenyl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 29 Histone deacetylase 4 Homo sapiens 150 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344323 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344323&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273935 385450411 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681711 Cc1c(F)cc(F)cc1C1(CCCC1)C(=O)NO InChI=1S/C13H15F2NO2/c1-8-10(6-9(14)7-11(8)15)13(12(17)16-18)4-2-3-5-13/h6-7,18H,2-5H2,1H3,(H,16,17) CUZYFAKUCIRUKL-UHFFFAOYSA-N 344326 1-(3,5-Difluoro-2-methylphenyl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 30 Histone deacetylase 4 Homo sapiens 330 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344326 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344326&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274170 385450414 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681712 Cc1cccc(Cl)c1C1(CCCC1)C(=O)NO InChI=1S/C13H16ClNO2/c1-9-5-4-6-10(14)11(9)13(12(16)15-17)7-2-3-8-13/h4-6,17H,2-3,7-8H2,1H3,(H,15,16) NHVWSMHNBRRYJF-UHFFFAOYSA-N 344327 1-(2-Chloro-6-methylphenyl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 31 Histone deacetylase 4 Homo sapiens 910 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344327 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344327&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274169 385450415 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681713 CCc1ccccc1C1(CCCC1)C(=O)NO InChI=1S/C14H19NO2/c1-2-11-7-3-4-8-12(11)14(13(16)15-17)9-5-6-10-14/h3-4,7-8,17H,2,5-6,9-10H2,1H3,(H,15,16) KYNFTETVTGETHL-UHFFFAOYSA-N 344328 1-(2-Ethylphenyl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 32 Histone deacetylase 4 Homo sapiens 1100 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344328 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344328&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86273936 385450416 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681714 COc1cccc(c1C(F)(F)F)C1(CCCC1)C(=O)NO InChI=1S/C14H16F3NO3/c1-21-10-6-4-5-9(11(10)14(15,16)17)13(12(19)18-20)7-2-3-8-13/h4-6,20H,2-3,7-8H2,1H3,(H,18,19) HSNKZNYIRFJNHD-UHFFFAOYSA-N 344331 N-Hydroxy-1-(3-methoxy-2- (trifluoromethyl)phenyl) cyclopentanecarboxamide::US9783488, Example 33 Histone deacetylase 4 Homo sapiens >50000 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344331 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344331&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274176 385450419 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681715 ONC(=O)C1(CCCC1)c1ccccc1C(F)(F)F InChI=1S/C13H14F3NO2/c14-13(15,16)10-6-2-1-5-9(10)12(11(18)17-19)7-3-4-8-12/h1-2,5-6,19H,3-4,7-8H2,(H,17,18) GGRLEWASOWASJU-UHFFFAOYSA-N 344332 N-Hydroxy-1-(2- (trifluoromethyl)phenyl) cyclopentanecarboxamide::US9783488, Example 34 Histone deacetylase 4 Homo sapiens 11000 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344332 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344332&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274175 385450420 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681716 Cc1cc(F)ccc1C1(CCCC1)C(=O)NO InChI=1S/C13H16FNO2/c1-9-8-10(14)4-5-11(9)13(12(16)15-17)6-2-3-7-13/h4-5,8,17H,2-3,6-7H2,1H3,(H,15,16) KOJCYZOEPDSPLL-UHFFFAOYSA-N 344333 1-(4-Fluoro-2-methylphenyl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 35 Histone deacetylase 4 Homo sapiens 570 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344333 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344333&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274174 385450421 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681717 Cc1ccc(F)cc1C1(CCCC1)C(=O)NO InChI=1S/C13H16FNO2/c1-9-4-5-10(14)8-11(9)13(12(16)15-17)6-2-3-7-13/h4-5,8,17H,2-3,6-7H2,1H3,(H,15,16) IGPNBHDPLHZJDJ-UHFFFAOYSA-N 344334 1-(5-Fluoro-2-methylphenyl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 36 Histone deacetylase 4 Homo sapiens 830 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344334 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344334&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274173 385450422 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681718 Cc1cccc(F)c1C1(CCCC1)C(=O)NO InChI=1S/C13H16FNO2/c1-9-5-4-6-10(14)11(9)13(12(16)15-17)7-2-3-8-13/h4-6,17H,2-3,7-8H2,1H3,(H,15,16) OITAEWUFLYMMDF-UHFFFAOYSA-N 344341 1-(2-Fluoro-6-methylphenyl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 37 Histone deacetylase 4 Homo sapiens 1500 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344341 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344341&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274172 385450429 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681719 ONC(=O)C1(CCCC1)c1cccc2ccsc12 InChI=1S/C14H15NO2S/c16-13(15-17)14(7-1-2-8-14)11-5-3-4-10-6-9-18-12(10)11/h3-6,9,17H,1-2,7-8H2,(H,15,16) RLJGGZYGTXXWLE-UHFFFAOYSA-N 344342 1-(Benzo[b]thiophen-7-yl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 38 Histone deacetylase 4 Homo sapiens 610 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344342 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344342&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117618986 385450430 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681720 Cc1c(F)cccc1[C@]1(CC[C@@H](C1)c1cncc(F)c1)C(=O)NO InChI=1S/C18H18F2N2O2/c1-11-15(3-2-4-16(11)20)18(17(23)22-24)6-5-12(8-18)13-7-14(19)10-21-9-13/h2-4,7,9-10,12,24H,5-6,8H2,1H3,(H,22,23)/t12-,18+/m0/s1 HZPQUCRMKHUJSP-KPZWWZAWSA-N 344343 (1R,3S*)-1-(3-Fluoro-2- methylphenyl)-3-(5- fluoropyridin-3-yl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 39 Histone deacetylase 4 Homo sapiens 720 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344343 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344343&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274177 385450431 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681721 Cc1c(F)cccc1[C@]1(CC[C@H](C1)c1cncc(F)c1)C(=O)NO InChI=1S/C18H18F2N2O2/c1-11-15(3-2-4-16(11)20)18(17(23)22-24)6-5-12(8-18)13-7-14(19)10-21-9-13/h2-4,7,9-10,12,24H,5-6,8H2,1H3,(H,22,23)/t12-,18-/m1/s1 HZPQUCRMKHUJSP-KZULUSFZSA-N 344344 (1R,3R*)-1-(3-Fluoro-2- methylphenyl)-3-(5- fluoropyridin-3-yl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 40 Histone deacetylase 4 Homo sapiens 3600 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344344 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344344&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274410 385450432 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681722 ONC(=O)[C@]1(CC[C@H](C1)c1cncc(F)c1)c1ccccc1 InChI=1S/C17H17FN2O2/c18-15-8-13(10-19-11-15)12-6-7-17(9-12,16(21)20-22)14-4-2-1-3-5-14/h1-5,8,10-12,22H,6-7,9H2,(H,20,21)/t12-,17+/m1/s1 XUCNSDHIOWERNL-PXAZEXFGSA-N 344349 (1S,3R)-3-(5- Fluoropyridin-3-yl)-N- hydroxy-1- phenylcyclopentanecarboxamide::US9783488, Example 41 Histone deacetylase 4 Homo sapiens 1900 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344349 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344349&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274411 385450437 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681723 ONC(=O)[C@]1(CC[C@@H](C1)c1cncc(F)c1)c1ccccc1 InChI=1S/C17H17FN2O2/c18-15-8-13(10-19-11-15)12-6-7-17(9-12,16(21)20-22)14-4-2-1-3-5-14/h1-5,8,10-12,22H,6-7,9H2,(H,20,21)/t12-,17-/m0/s1 XUCNSDHIOWERNL-SJCJKPOMSA-N 344350 (1S,3S)-3-(5- Fluoropyridin-3-yl)-N- hydroxy-1- phenylcyclopentanecarboxamide::US9783488, Example 42 Histone deacetylase 4 Homo sapiens 1400 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344350 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344350&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274412 385450438 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681724 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1cc(F)cnc1C1CC1)C(=O)NO InChI=1S/C21H22F2N2O2/c1-12-17(3-2-4-18(12)23)21(20(26)25-27)8-7-14(10-21)16-9-15(22)11-24-19(16)13-5-6-13/h2-4,9,11,13-14,27H,5-8,10H2,1H3,(H,25,26)/t14-,21+/m1/s1 HUTWBAQGKNJMMD-SZNDQCEHSA-N 344351 (1S,3R)-3-(2-cyclopropyl-5-fluoropyridin-3-yl)-1-(3-fluoro-2-methylphenyl)-N-hydroxycyclopentanecarboxamide::US9783488, Example 43 Histone deacetylase 4 Homo sapiens 240 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344351 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344351&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274413 385450439 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681725 COc1ncc(cc1F)[C@H]1CC[C@@](C1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C19H20F2N2O3/c1-11-14(4-3-5-15(11)20)19(18(24)23-25)7-6-12(9-19)13-8-16(21)17(26-2)22-10-13/h3-5,8,10,12,25H,6-7,9H2,1-2H3,(H,23,24)/t12-,19-/m0/s1 BQQAHYSWOXIMKG-BUXKBTBVSA-N 344352 (1S,3S*)-1-(3-Fluoro-2- methylphenyl)-3-(5-fluoro- 6-methoxypyridin-3-yl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 44 Histone deacetylase 4 Homo sapiens 330 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344352 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344352&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274647 385450440 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681726 COc1ncc(cc1F)[C@@H]1CC[C@@](C1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C19H20F2N2O3/c1-11-14(4-3-5-15(11)20)19(18(24)23-25)7-6-12(9-19)13-8-16(21)17(26-2)22-10-13/h3-5,8,10,12,25H,6-7,9H2,1-2H3,(H,23,24)/t12-,19+/m1/s1 BQQAHYSWOXIMKG-BLVKFPJESA-N 344353 (1S,3R*)-1-(3-Fluoro-2- methylphenyl)-3-(5-fluoro- 6-methoxypyridin-3-yl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 45 Histone deacetylase 4 Homo sapiens 190 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344353 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344353&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274646 385450441 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681727 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1cnn(c1)C(F)F)C(=O)NO InChI=1S/C17H18F3N3O2/c1-10-13(3-2-4-14(10)18)17(15(24)22-25)6-5-11(7-17)12-8-21-23(9-12)16(19)20/h2-4,8-9,11,16,25H,5-7H2,1H3,(H,22,24)/t11-,17+/m1/s1 MBWFMNVECJSEDM-DIFFPNOSSA-N 344354 (1S,3R*)-3-(1-(Difluoromethyl)-1H-pyrazol-4-yl)-1-(3-fluoro-2-methylphenyl)-N-hydroxy cyclopentane carboxamide::US9783488, Example 46 Histone deacetylase 4 Homo sapiens 95.0 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344354 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344354&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274645 385450442 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681728 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1cnn(CCN2CCOCC2)c1)C(=O)NO InChI=1S/C22H29FN4O3/c1-16-19(3-2-4-20(16)23)22(21(28)25-29)6-5-17(13-22)18-14-24-27(15-18)8-7-26-9-11-30-12-10-26/h2-4,14-15,17,29H,5-13H2,1H3,(H,25,28)/t17-,22+/m1/s1 KPWHXBUVQGQCDT-VGSWGCGISA-N 344355 (1S,3R*)-1-(3-fluoro-2-methylphenyl)-N-hydroxy-3-(1-(2-morpholinoethyl)-1H-pyrazol-4-yl)cyclopentanecarboxamide::US9783488, Example 47 Histone deacetylase 4 Homo sapiens 140 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344355 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344355&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274644 385450443 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681729 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1cnc(OCCN2CCCC2)c(F)c1)C(=O)NO InChI=1S/C24H29F2N3O3/c1-16-19(5-4-6-20(16)25)24(23(30)28-31)8-7-17(14-24)18-13-21(26)22(27-15-18)32-12-11-29-9-2-3-10-29/h4-6,13,15,17,31H,2-3,7-12,14H2,1H3,(H,28,30)/t17-,24+/m1/s1 FRFMGCFWJFUXBT-OSPHWJPCSA-N 344356 (1 S,3R*)-1-(3-Fluoro-2-methylphenyl)-3-(5-fluoro-6-(2-(pyrrolidin-1-yl)ethoxy)pyridin-3-yl)-N-hydroxycyclopentanecarboxamide::US9783488, Example 48 Histone deacetylase 4 Homo sapiens 320 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344356 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344356&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274643 385450444 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681730 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccnn1C)C(=O)NO InChI=1S/C17H20FN3O2/c1-11-13(4-3-5-14(11)18)17(16(22)20-23)8-6-12(10-17)15-7-9-19-21(15)2/h3-5,7,9,12,23H,6,8,10H2,1-2H3,(H,20,22)/t12-,17+/m1/s1 RERSZXIBQVTMBT-PXAZEXFGSA-N 344357 (1S,3R*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3-(1-methyl-1H-pyrazol-5- yl)cyclopentanecarboxamide::US9783488, Example 49 Histone deacetylase 4 Homo sapiens 170 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344357 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344357&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274415 385450445 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681731 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)c1ccnn1C)C(=O)NO InChI=1S/C17H20FN3O2/c1-11-13(4-3-5-14(11)18)17(16(22)20-23)8-6-12(10-17)15-7-9-19-21(15)2/h3-5,7,9,12,23H,6,8,10H2,1-2H3,(H,20,22)/t12-,17-/m0/s1 RERSZXIBQVTMBT-SJCJKPOMSA-N 344358 (1S,3S*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3-(1-methyl-1H-pyrazol-5- yl)cyclopentanecarboxamide::US9783488, Example 50 Histone deacetylase 4 Homo sapiens 250 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344358 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344358&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274414 385450446 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681732 CCN(CC)CCn1cc(cn1)[C@@H]1CC[C@@](C1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C22H31FN4O2/c1-4-26(5-2)11-12-27-15-18(14-24-27)17-9-10-22(13-17,21(28)25-29)19-7-6-8-20(23)16(19)3/h6-8,14-15,17,29H,4-5,9-13H2,1-3H3,(H,25,28)/t17-,22+/m1/s1 LHOKZZCIENTAEE-VGSWGCGISA-N 344359 (1S,3R*)-3-(1-(2-(diethylamino)ethyl)-1H-pyrazol-4-yl)-1-(3-fluoro-2-methylphenyl)-N-hydroxycyclopentanecarboxamide::US9783488, Example 51 Histone deacetylase 4 Homo sapiens 82.0 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344359 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344359&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274416 385450447 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681733 CCCN(CCC)C[C@@H](C)NC(=O)c1ccc(cc1)[C@@H]1CC[C@@](C1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C29H40FN3O3/c1-5-16-33(17-6-2)19-20(3)31-27(34)23-12-10-22(11-13-23)24-14-15-29(18-24,28(35)32-36)25-8-7-9-26(30)21(25)4/h7-13,20,24,36H,5-6,14-19H2,1-4H3,(H,31,34)(H,32,35)/t20-,24-,29+/m1/s1 ISDOXTZTTMFQEJ-IFVWFWILSA-N 344362 N-((R)-1- (Dipropylamino)propan-2- yl)-4-((1R*,3S)-3-(3- fluoro-2-methylphenyl)-3- (hydroxycarbamoyl) cyclopentyl)benzamide::US9783488, Example 52 Histone deacetylase 4 Homo sapiens 200 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344362 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344362&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274648 385450450 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681734 CCCN(CCC)C[C@@H](C)NC(=O)c1ccc(cc1)[C@H]1CC[C@@](C1)(C(=O)NO)c1cccc(F)c1C InChI=1S/C29H40FN3O3/c1-5-16-33(17-6-2)19-20(3)31-27(34)23-12-10-22(11-13-23)24-14-15-29(18-24,28(35)32-36)25-8-7-9-26(30)21(25)4/h7-13,20,24,36H,5-6,14-19H2,1-4H3,(H,31,34)(H,32,35)/t20-,24+,29+/m1/s1 ISDOXTZTTMFQEJ-WMQVBLFHSA-N 344363 N-((R)-1- (Dipropylamino)propan-2- yl)-4-((1S*,3S)-3-(3- fluoro-2-methylphenyl)-3- (hydroxycarbamoyl) cyclopentyl)benzamide::US9783488, Example 53 Histone deacetylase 4 Homo sapiens 160 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344363 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344363&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274882 385450451 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681735 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccc2cnn(C(F)F)c2c1)C(=O)NO InChI=1S/C21H20F3N3O2/c1-12-16(3-2-4-17(12)22)21(19(28)26-29)8-7-14(10-21)13-5-6-15-11-25-27(20(23)24)18(15)9-13/h2-6,9,11,14,20,29H,7-8,10H2,1H3,(H,26,28)/t14-,21+/m1/s1 STLBNVLRCLGAHR-SZNDQCEHSA-N 344364 (1S,3R*)-3-(1- (Difluoromethyl)-1H- indazol-6-yl)-1-(3-fluoro- 2-methylphenyl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 54 Histone deacetylase 4 Homo sapiens 72.0 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344364 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344364&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274883 385450452 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681736 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)c1ccc2cnn(C(F)F)c2c1)C(=O)NO InChI=1S/C21H20F3N3O2/c1-12-16(3-2-4-17(12)22)21(19(28)26-29)8-7-14(10-21)13-5-6-15-11-25-27(20(23)24)18(15)9-13/h2-6,9,11,14,20,29H,7-8,10H2,1H3,(H,26,28)/t14-,21-/m0/s1 STLBNVLRCLGAHR-QKKBWIMNSA-N 344365 (1S,3S*)-3-(1- (Difluoromethyl)-1H- indazol-6-yl)-1-(3-fluoro- 2-methylphenyl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 55 Histone deacetylase 4 Homo sapiens 46.0 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344365 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344365&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274884 385450453 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681737 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccc2cnn(C)c2c1)C(=O)NO InChI=1S/C21H22FN3O2/c1-13-17(4-3-5-18(13)22)21(20(26)24-27)9-8-15(11-21)14-6-7-16-12-23-25(2)19(16)10-14/h3-7,10,12,15,27H,8-9,11H2,1-2H3,(H,24,26)/t15-,21+/m1/s1 ICCWFLUFOVTOGC-VFNWGFHPSA-N 344366 (1S,3R*)-1-(3-fluoro-2-methylphenyl)-N-hydroxy-3-(1-methyl-1H-indazol-6-yl)cyclopentanecarboxamide::US9783488, Example 56 Histone deacetylase 4 Homo sapiens 140 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344366 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344366&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274885 385450454 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681738 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccn2ccnc2c1)C(=O)NO InChI=1S/C20H20FN3O2/c1-13-16(3-2-4-17(13)21)20(19(25)23-26)7-5-15(12-20)14-6-9-24-10-8-22-18(24)11-14/h2-4,6,8-11,15,26H,5,7,12H2,1H3,(H,23,25)/t15-,20+/m1/s1 OODLWMVDOVNHED-QRWLVFNGSA-N 344367 (1S,3R*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3-(imidazo[1,2-a]pyridin- 7- yl)cyclopentanecarboxamide::US9783488, Example 57 Histone deacetylase 4 Homo sapiens 98.0 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344367 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344367&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86275129 385450455 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681739 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)c1ccn2ccnc2c1)C(=O)NO InChI=1S/C20H20FN3O2/c1-13-16(3-2-4-17(13)21)20(19(25)23-26)7-5-15(12-20)14-6-9-24-10-8-22-18(24)11-14/h2-4,6,8-11,15,26H,5,7,12H2,1H3,(H,23,25)/t15-,20-/m0/s1 OODLWMVDOVNHED-YWZLYKJASA-N 344368 (1S,3S*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3-(imidazo[1,2-a]pyridin- 7- yl)cyclopentanecarboxamide::US9783488, Example 58 Histone deacetylase 4 Homo sapiens 82.0 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344368 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344368&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274887 385450456 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681740 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccc2C(=O)N(Cc2c1)C1CC1)C(=O)NO InChI=1S/C24H25FN2O3/c1-14-20(3-2-4-21(14)25)24(23(29)26-30)10-9-16(12-24)15-5-8-19-17(11-15)13-27(22(19)28)18-6-7-18/h2-5,8,11,16,18,30H,6-7,9-10,12-13H2,1H3,(H,26,29)/t16-,24+/m1/s1 RONPOJXAFIWVBG-GYCJOSAFSA-N 344369 (1S,3R*)-3-(2-cyclopropyl-1-oxoisoindolin-5-yl)-1-(3-fluoro-2-methylphenyl)-N-hydroxycyclopentanecarboxamide::US9783488, Example 59 Histone deacetylase 4 Homo sapiens 140 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344369 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344369&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86274886 385450457 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681741 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1cccc2cnn(C)c12)C(=O)NO InChI=1S/C21H22FN3O2/c1-13-17(7-4-8-18(13)22)21(20(26)24-27)10-9-14(11-21)16-6-3-5-15-12-23-25(2)19(15)16/h3-8,12,14,27H,9-11H2,1-2H3,(H,24,26)/t14-,21+/m1/s1 OCQSPWATZYHFJK-SZNDQCEHSA-N 344376 (1S,3R*)-1-(3-fluoro-2-methylphenyl)-N-hydroxy-3-(1-methyl-1H-indazol-7-yl)cyclopentanecarboxamide::US9783488, Example 60 Histone deacetylase 4 Homo sapiens 360 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344376 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344376&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86275130 385450464 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681742 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccc2cn[nH]c2c1F)C(=O)NO 344377 (1S,3R*)-3-(7-fluoro-1H-indazol-6-yl)-1-(3-fluoro-2-methylphenyl)-N-hydroxycyclopentanecarboxamide::US9783488, Example 61 Histone deacetylase 4 Homo sapiens 73.0 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344377 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344377&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86275131 385450465 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681743 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccc2oc(nc2c1)C1CC1)C(=O)NO InChI=1S/C23H23FN2O3/c1-13-17(3-2-4-18(13)24)23(22(27)26-28)10-9-16(12-23)15-7-8-20-19(11-15)25-21(29-20)14-5-6-14/h2-4,7-8,11,14,16,28H,5-6,9-10,12H2,1H3,(H,26,27)/t16-,23+/m1/s1 XOLDAHGURUBIRR-MWTRTKDXSA-N 344378 (1S,3R*)-3-(2-cyclopropylbenzo[d]oxazol-5-yl)-1-(3-fluoro-2-methylphenyl)-N-hydroxycyclopentanecarboxamide::US9783488, Example 62 Histone deacetylase 4 Homo sapiens 280 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=344378 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=344378&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86275378 385450466 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681744 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccc2n(C)ncc2c1)C(=O)NO InChI=1S/C21H22FN3O2/c1-13-17(4-3-5-18(13)22)21(20(26)24-27)9-8-15(11-21)14-6-7-19-16(10-14)12-23-25(19)2/h3-7,10,12,15,27H,8-9,11H2,1-2H3,(H,24,26)/t15-,21+/m1/s1 JEKQOVILUATGAE-VFNWGFHPSA-N 345153 (1S,3R*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3-(1-methyl-1H-indazol-5- yl)cyclopentanecarboxamide::US9783488, Example 63 Histone deacetylase 4 Homo sapiens 110 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345153 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345153&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86275377 385451216 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681745 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)c1ccc2n(C)ncc2c1)C(=O)NO InChI=1S/C21H22FN3O2/c1-13-17(4-3-5-18(13)22)21(20(26)24-27)9-8-15(11-21)14-6-7-19-16(10-14)12-23-25(19)2/h3-7,10,12,15,27H,8-9,11H2,1-2H3,(H,24,26)/t15-,21-/m0/s1 JEKQOVILUATGAE-BTYIYWSLSA-N 345156 (1S,3S*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3-(1-methyl-1H-indazol-5- yl)cyclopentanecarboxamide::US9783488, Example 64 Histone deacetylase 4 Homo sapiens 100.0 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345156 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345156&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86275376 385451219 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681746 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccc2cn(nc2c1)C(F)F)C(=O)NO InChI=1S/C21H20F3N3O2/c1-12-16(3-2-4-17(12)22)21(19(28)26-29)8-7-14(10-21)13-5-6-15-11-27(20(23)24)25-18(15)9-13/h2-6,9,11,14,20,29H,7-8,10H2,1H3,(H,26,28)/t14-,21+/m1/s1 ZFRAPBHCTYCXJE-SZNDQCEHSA-N 345160 (1S,3R*)-3-(2- (Difluoromethyl)-2H- indazol-6-yl)-1-(3-fluoro- 2-methylphenyl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 65 Histone deacetylase 4 Homo sapiens 110 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345160 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345160&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86275134 385451223 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681747 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)c1ccc2cn(nc2c1)C(F)F)C(=O)NO InChI=1S/C21H20F3N3O2/c1-12-16(3-2-4-17(12)22)21(19(28)26-29)8-7-14(10-21)13-5-6-15-11-27(20(23)24)25-18(15)9-13/h2-6,9,11,14,20,29H,7-8,10H2,1H3,(H,26,28)/t14-,21-/m0/s1 ZFRAPBHCTYCXJE-QKKBWIMNSA-N 345173 (1S,3S*)-3-(2- (Difluoromethyl)-2H- indazol-6-yl)-1-(3-fluoro- 2-methylphenyl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 66 Histone deacetylase 4 Homo sapiens 220 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345173 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345173&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86275375 385451236 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681748 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccc2c(F)nn(C)c2c1)C(=O)NO InChI=1S/C21H21F2N3O2/c1-12-16(4-3-5-17(12)22)21(20(27)25-28)9-8-14(11-21)13-6-7-15-18(10-13)26(2)24-19(15)23/h3-7,10,14,28H,8-9,11H2,1-2H3,(H,25,27)/t14-,21+/m1/s1 IZYKRBVWHHZVKE-SZNDQCEHSA-N 345188 (1S,3R*)-3-(3-Fluoro-1- methyl-1H-indazol-6-yl)-1- (3-fluoro-2-methylphenyl)- N- hydroxycyclopentanecarboxamide::US9783488, Example 67 Histone deacetylase 4 Homo sapiens 400 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345188 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345188&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86275132 385451251 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681749 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)c1ccc2c(F)nn(C)c2c1)C(=O)NO InChI=1S/C21H21F2N3O2/c1-12-16(4-3-5-17(12)22)21(20(27)25-28)9-8-14(11-21)13-6-7-15-18(10-13)26(2)24-19(15)23/h3-7,10,14,28H,8-9,11H2,1-2H3,(H,25,27)/t14-,21-/m0/s1 IZYKRBVWHHZVKE-QKKBWIMNSA-N 345194 (1S,3S*)-3-(3-Fluoro-1- methyl-1H-indazol-6-yl)-1- (3-fluoro-2-methylphenyl)- N- hydroxycyclopentanecarboxamide::US9783488, Example 68 Histone deacetylase 4 Homo sapiens 320 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345194 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345194&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86275133 385451257 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681750 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccc2n(C)cnc2c1)C(=O)NO InChI=1S/C21H22FN3O2/c1-13-16(4-3-5-17(13)22)21(20(26)24-27)9-8-15(11-21)14-6-7-19-18(10-14)23-12-25(19)2/h3-7,10,12,15,27H,8-9,11H2,1-2H3,(H,24,26)/t15-,21+/m1/s1 QGHNXNLNZRPJAO-VFNWGFHPSA-N 345195 (1S,3R*)-1-(3-fluoro-2-methylphenyl)-N-hydroxy-3-(1-methyl-1H-benzo[d]imidazol-5-yl)cyclopentanecarboxamide::US9783488, Example 69 Histone deacetylase 4 Homo sapiens 90.0 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345195 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345195&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86275379 385451258 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681751 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccc2ncn(C)c2c1)C(=O)NO InChI=1S/C21H22FN3O2/c1-13-16(4-3-5-17(13)22)21(20(26)24-27)9-8-15(11-21)14-6-7-18-19(10-14)25(2)12-23-18/h3-7,10,12,15,27H,8-9,11H2,1-2H3,(H,24,26)/t15-,21+/m1/s1 DSWVROBJZBNBHT-VFNWGFHPSA-N 345217 (1S,3R*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3-(1-methyl-1H- benzo[d]imidazol-6- yl)cyclopentanecarboxamide::US9783488, Example 70 Histone deacetylase 4 Homo sapiens 110 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345217 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345217&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86275380 385451280 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681752 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)c1ccc2ncn(C)c2c1)C(=O)NO InChI=1S/C21H22FN3O2/c1-13-16(4-3-5-17(13)22)21(20(26)24-27)9-8-15(11-21)14-6-7-18-19(10-14)25(2)12-23-18/h3-7,10,12,15,27H,8-9,11H2,1-2H3,(H,24,26)/t15-,21-/m0/s1 DSWVROBJZBNBHT-BTYIYWSLSA-N 345218 (1S,3S*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3-(1-methyl-1H- benzo[d]imidazol-6- yl)cyclopentanecarboxamide::US9783488, Example 71 Histone deacetylase 4 Homo sapiens 59.0 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345218 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345218&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86275605 385451281 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681753 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccc2OC(C)(C)CNc2c1)C(=O)NO InChI=1S/C23H27FN2O3/c1-14-17(5-4-6-18(14)24)23(21(27)26-28)10-9-16(12-23)15-7-8-20-19(11-15)25-13-22(2,3)29-20/h4-8,11,16,25,28H,9-10,12-13H2,1-3H3,(H,26,27)/t16-,23+/m1/s1 KDMZPLGXEDEZIU-MWTRTKDXSA-N 345219 (1S,3R*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3-(1-methyl-1H- benzo[d]imidazol-6- yl)cyclopentanecarboxamide::US9783488, Example 72 Histone deacetylase 4 Homo sapiens 300 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345219 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345219&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86275606 385451282 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681754 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)c1ccc2OC(C)(C)CNc2c1)C(=O)NO InChI=1S/C23H27FN2O3/c1-14-17(5-4-6-18(14)24)23(21(27)26-28)10-9-16(12-23)15-7-8-20-19(11-15)25-13-22(2,3)29-20/h4-8,11,16,25,28H,9-10,12-13H2,1-3H3,(H,26,27)/t16-,23-/m0/s1 KDMZPLGXEDEZIU-HJPURHCSSA-N 345220 (1S,3S*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3-(1-methyl-1H- benzo[d]imidazol-6- yl)cyclopentanecarboxamide::US9783488, Example 73 Histone deacetylase 4 Homo sapiens 270 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345220 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345220&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86275608 385451283 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681755 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccc2nc([nH]c2c1)C(F)(F)F)C(=O)NO 345221 (1S,3R*)-1-(3-Fluoro-2-methylphenyl)-N-hydroxy-3-(2-(trifluoromethyl)-1H-benzo[d]imidazol-6-yl)cyclopentanecarboxamide::US9783488, Example 74 Histone deacetylase 4 Homo sapiens 74.0 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345221 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345221&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86275607 385451284 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681756 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)c1nc2ccccc2s1)C(=O)NO InChI=1S/C20H19FN2O2S/c1-12-14(5-4-6-15(12)21)20(19(24)23-25)10-9-13(11-20)18-22-16-7-2-3-8-17(16)26-18/h2-8,13,25H,9-11H2,1H3,(H,23,24)/t13-,20-/m0/s1 BBHYQXANTPSPQY-RBZFPXEDSA-N 345222 (1S,3S*)-3- (Benzo[d]thiazol-2-yl)-1- (3-fluoro-2-methylphenyl)- N- hydroxycyclopentanecarboxamide::US9783488, Example 75 Histone deacetylase 4 Homo sapiens 80.0 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345222 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345222&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86275610 385451285 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681757 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1nc2ccccc2s1)C(=O)NO InChI=1S/C20H19FN2O2S/c1-12-14(5-4-6-15(12)21)20(19(24)23-25)10-9-13(11-20)18-22-16-7-2-3-8-17(16)26-18/h2-8,13,25H,9-11H2,1H3,(H,23,24)/t13-,20+/m1/s1 BBHYQXANTPSPQY-XCLFUZPHSA-N 345223 (1S,3R*)-3- (Benzo-[d]thiazol-2-yl)-1- (3-fluoro-2-methylphenyl)- N- hydroxycyclopentanecarboxamide::US9783488, Example 76 Histone deacetylase 4 Homo sapiens 160 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345223 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345223&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86275609 385451286 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681758 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)c1ccc2nc(sc2c1)C1CC1)C(=O)NO InChI=1S/C23H23FN2O2S/c1-13-17(3-2-4-18(13)24)23(22(27)26-28)10-9-16(12-23)15-7-8-19-20(11-15)29-21(25-19)14-5-6-14/h2-4,7-8,11,14,16,28H,5-6,9-10,12H2,1H3,(H,26,27)/t16-,23-/m0/s1 FVSHRAFFHIROGV-HJPURHCSSA-N 345224 (1S,3S*)-3-(2- Cyclopropylbenzo[d]thiazol- 6-yl)-1-(3-fluoro-2- methylphenyl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 77 Histone deacetylase 4 Homo sapiens 310 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345224 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345224&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86272020 385451287 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681759 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccc2nc(sc2c1)C1CC1)C(=O)NO InChI=1S/C23H23FN2O2S/c1-13-17(3-2-4-18(13)24)23(22(27)26-28)10-9-16(12-23)15-7-8-19-20(11-15)29-21(25-19)14-5-6-14/h2-4,7-8,11,14,16,28H,5-6,9-10,12H2,1H3,(H,26,27)/t16-,23+/m1/s1 FVSHRAFFHIROGV-MWTRTKDXSA-N 345225 (1S,3R*)-3-(2- Cyclopropylbenzo[d]thiazol- 6-yl)-1-(3-fluoro-2- methylphenyl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 78 Histone deacetylase 4 Homo sapiens 340 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345225 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345225&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86272022 385451288 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681760 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)c1ccc2sc(nc2c1)C1CC1)C(=O)NO InChI=1S/C23H23FN2O2S/c1-13-17(3-2-4-18(13)24)23(22(27)26-28)10-9-16(12-23)15-7-8-20-19(11-15)25-21(29-20)14-5-6-14/h2-4,7-8,11,14,16,28H,5-6,9-10,12H2,1H3,(H,26,27)/t16-,23-/m0/s1 KABGWNUXYYDTTC-HJPURHCSSA-N 345226 (1S,3S*)-3-(2- Cyclopropylbenzo[d]thiazol- 5-yl)-1-(3-fluoro-2- methylphenyl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 79 Histone deacetylase 4 Homo sapiens 290 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345226 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345226&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86272023 385451289 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681761 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccc2sc(nc2c1)C1CC1)C(=O)NO InChI=1S/C23H23FN2O2S/c1-13-17(3-2-4-18(13)24)23(22(27)26-28)10-9-16(12-23)15-7-8-20-19(11-15)25-21(29-20)14-5-6-14/h2-4,7-8,11,14,16,28H,5-6,9-10,12H2,1H3,(H,26,27)/t16-,23+/m1/s1 KABGWNUXYYDTTC-MWTRTKDXSA-N 345227 (1S,3R*)-3-(2- Cyclopropylbenzo[d]thiazol- 5-yl)-1-(3-fluoro-2- methylphenyl)-N- hydroxycyclopentanecarboxamide::US9783488, Example 80 Histone deacetylase 4 Homo sapiens 330 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345227 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345227&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86272025 385451290 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681762 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1cc2n(C)ncc2cc1F)C(=O)NO InChI=1S/C21H21F2N3O2/c1-12-16(4-3-5-17(12)22)21(20(27)25-28)7-6-13(10-21)15-9-19-14(8-18(15)23)11-24-26(19)2/h3-5,8-9,11,13,28H,6-7,10H2,1-2H3,(H,25,27)/t13-,21+/m1/s1 PXAMEPIPXDXIJJ-ASSNKEHSSA-N 345228 (1S,3R)-3-(5-Fluoro-1-methyl-1H-indazol-6-yl)-1-(3-fluoro-2-methylphenyl)-N-hydroxycyclopentanecarboxamide::US9783488, Example 81 Histone deacetylase 4 Homo sapiens 150 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345228 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345228&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117619015 385451291 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681763 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)c1ccc2cnn(C)c2c1F)C(=O)NO InChI=1S/C21H21F2N3O2/c1-12-16(4-3-5-17(12)22)21(20(27)25-28)9-8-13(10-21)15-7-6-14-11-24-26(2)19(14)18(15)23/h3-7,11,13,28H,8-10H2,1-2H3,(H,25,27)/t13-,21-/m0/s1 CFMBAUBXRNMZPH-ZSEKCTLFSA-N 345229 (1S,3S*)-3-(7-Fluoro-1- methyl-1H-indazol-6-yl)-1- (3-fluoro-2-methylphenyl)- N- hydroxycyclopentanecarboxamide::US9783488, Example 82 Histone deacetylase 4 Homo sapiens 110 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345229 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345229&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118870428 385451292 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681764 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccc2cnn(C)c2c1F)C(=O)NO InChI=1S/C21H21F2N3O2/c1-12-16(4-3-5-17(12)22)21(20(27)25-28)9-8-13(10-21)15-7-6-14-11-24-26(2)19(14)18(15)23/h3-7,11,13,28H,8-10H2,1-2H3,(H,25,27)/t13-,21+/m1/s1 CFMBAUBXRNMZPH-ASSNKEHSSA-N 345230 (1S,3R*)-3-(7-Fluoro-1- methyl-1H-indazol-6-yl)-1- (3-fluoro-2-methylphenyl)- N- hydroxycyclopentanecarboxamide::US9783488, Example 83 Histone deacetylase 4 Homo sapiens 55.0 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345230 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345230&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86272265 385451293 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681765 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)c1ccc2ncccc2c1)C(=O)NO InChI=1S/C22H21FN2O2/c1-14-18(5-2-6-19(14)23)22(21(26)25-27)10-9-17(13-22)15-7-8-20-16(12-15)4-3-11-24-20/h2-8,11-12,17,27H,9-10,13H2,1H3,(H,25,26)/t17-,22-/m0/s1 TXRARWVMRQAKLP-JTSKRJEESA-N 345231 (1S,3S*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3-(quinolin-6- yl)cyclopentanecarboxamide::US9783488, Example 84 Histone deacetylase 4 Homo sapiens 48.0 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345231 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345231&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86272266 385451294 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681766 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)c1ccc2ncccc2c1)C(=O)NO InChI=1S/C22H21FN2O2/c1-14-18(5-2-6-19(14)23)22(21(26)25-27)10-9-17(13-22)15-7-8-20-16(12-15)4-3-11-24-20/h2-8,11-12,17,27H,9-10,13H2,1H3,(H,25,26)/t17-,22+/m1/s1 TXRARWVMRQAKLP-VGSWGCGISA-N 345232 (1S,3R*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3-(quinolin-6- yl)cyclopentanecarboxamide::US9783488, Example 85 Histone deacetylase 4 Homo sapiens 62.0 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345232 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345232&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86272267 385451295 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681767 Cc1c(F)c(F)ccc1[C@@]1(CC[C@H](C1)c1ccc2cnn(C)c2c1)C(=O)NO InChI=1S/C21H21F2N3O2/c1-12-16(5-6-17(22)19(12)23)21(20(27)25-28)8-7-14(10-21)13-3-4-15-11-24-26(2)18(15)9-13/h3-6,9,11,14,28H,7-8,10H2,1-2H3,(H,25,27)/t14-,21+/m1/s1 AAADCKOTKJSVMJ-SZNDQCEHSA-N 345233 (1S,3R*)-1-(3,4-difluoro-2-methylphenyl)-N-hydroxy-3-(1-methyl-1H-indazol-6-yl)cyclopentanecarboxamide::US9783488, Example 86 Histone deacetylase 4 Homo sapiens 90.0 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345233 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345233&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86272268 385451296 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681768 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)N1CCCC1)C(=O)NO InChI=1S/C17H23FN2O2/c1-12-14(5-4-6-15(12)18)17(16(21)19-22)8-7-13(11-17)20-9-2-3-10-20/h4-6,13,22H,2-3,7-11H2,1H3,(H,19,21)/t13-,17+/m1/s1 MGMPDKVTQIXARO-DYVFJYSZSA-N 345234 (1S,3R*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3-(pyrrolidin-1- yl)cyclopentanecarboxamide::US9783488, Example 87 Histone deacetylase 4 Homo sapiens 20000 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345234 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345234&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86272515 385451297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681769 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)N1CCCC1)C(=O)NO InChI=1S/C17H23FN2O2/c1-12-14(5-4-6-15(12)18)17(16(21)19-22)8-7-13(11-17)20-9-2-3-10-20/h4-6,13,22H,2-3,7-11H2,1H3,(H,19,21)/t13-,17-/m0/s1 MGMPDKVTQIXARO-GUYCJALGSA-N 345235 (1S,3S*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3-(pyrrolidin-1- yl)cyclopentanecarboxamide::US9783488, Example 88 Histone deacetylase 4 Homo sapiens >50000 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345235 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345235&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86272514 385451298 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681770 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)N1CCOCC1)C(=O)NO InChI=1S/C17H23FN2O3/c1-12-14(3-2-4-15(12)18)17(16(21)19-22)6-5-13(11-17)20-7-9-23-10-8-20/h2-4,13,22H,5-11H2,1H3,(H,19,21)/t13-,17+/m1/s1 XJEBSWFKAUTCSF-DYVFJYSZSA-N 345236 (1S,3R*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3- morpholinocyclopentanecarboxamide::US9783488, Example 89 Histone deacetylase 4 Homo sapiens 1100 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345236 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345236&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86272271 385451299 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681771 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)N1CCOCC1)C(=O)NO InChI=1S/C17H23FN2O3/c1-12-14(3-2-4-15(12)18)17(16(21)19-22)6-5-13(11-17)20-7-9-23-10-8-20/h2-4,13,22H,5-11H2,1H3,(H,19,21)/t13-,17-/m0/s1 XJEBSWFKAUTCSF-GUYCJALGSA-N 345237 (1S,3S*)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3- morpholinocyclopentanecarboxamide::US9783488, Example 90 Histone deacetylase 4 Homo sapiens 2500 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345237 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345237&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86272513 385451300 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681772 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)Oc1ccc2cnn(C)c2c1)C(=O)NO InChI=1S/C21H22FN3O3/c1-13-17(4-3-5-18(13)22)21(20(26)24-27)9-8-16(11-21)28-15-7-6-14-12-23-25(2)19(14)10-15/h3-7,10,12,16,27H,8-9,11H2,1-2H3,(H,24,26)/t16-,21+/m1/s1 BSDIYYHHDREQCZ-IERDGZPVSA-N 345238 (1S,3R)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3-((1-methyl-1H-indazol- 6- yl)oxy)cyclopentanecarboxamide::US9783488, Example 91 Histone deacetylase 4 Homo sapiens 290 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345238 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345238&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86272270 385451301 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681773 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)Oc1ccc2cnn(C)c2c1)C(=O)NO InChI=1S/C21H22FN3O3/c1-13-17(4-3-5-18(13)22)21(20(26)24-27)9-8-16(11-21)28-15-7-6-14-12-23-25(2)19(14)10-15/h3-7,10,12,16,27H,8-9,11H2,1-2H3,(H,24,26)/t16-,21-/m0/s1 BSDIYYHHDREQCZ-KKSFZXQISA-N 345239 (1S,3S)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3-((1-methyl-1H-indazol- 6- yl)oxy)cyclopentanecarboxamide::US9783488, Example 92 Histone deacetylase 4 Homo sapiens 140 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345239 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345239&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86272269 385451302 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681774 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)Oc1cncc(F)c1)C(=O)NO InChI=1S/C18H18F2N2O3/c1-11-15(3-2-4-16(11)20)18(17(23)22-24)6-5-13(8-18)25-14-7-12(19)9-21-10-14/h2-4,7,9-10,13,24H,5-6,8H2,1H3,(H,22,23)/t13-,18+/m1/s1 PPEPEULACZKSOF-ACJLOTCBSA-N 345240 (1S,3R)-1-(3-Fluoro-2- methylphenyl)-3-((5- fluoropyridin-3-yl)oxy)-N- hydroxycyclopentanecarboxamide::US9783488, Example 93 Histone deacetylase 4 Homo sapiens 200 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345240 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345240&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86272516 385451303 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681775 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)Oc1cncc(F)c1)C(=O)NO InChI=1S/C18H18F2N2O3/c1-11-15(3-2-4-16(11)20)18(17(23)22-24)6-5-13(8-18)25-14-7-12(19)9-21-10-14/h2-4,7,9-10,13,24H,5-6,8H2,1H3,(H,22,23)/t13-,18-/m0/s1 PPEPEULACZKSOF-UGSOOPFHSA-N 345241 (1S,3S)-1-(3-Fluoro-2- methylphenyl)-3-((5- fluoropyridin-3-yl)oxy)-N- hydroxycyclopentanecarboxamide::US9783488, Example 94 Histone deacetylase 4 Homo sapiens 160 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345241 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345241&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86272517 385451304 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681776 Cc1c(F)cccc1[C@@]1(CC[C@H](C1)Oc1ccccc1)C(=O)NO InChI=1S/C19H20FNO3/c1-13-16(8-5-9-17(13)20)19(18(22)21-23)11-10-15(12-19)24-14-6-3-2-4-7-14/h2-9,15,23H,10-12H2,1H3,(H,21,22)/t15-,19+/m1/s1 WVKUWJVGASWANR-BEFAXECRSA-N 345242 (1S,3R)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3- phenoxycyclopentanecarboxamide::US9783488, Example 95 Histone deacetylase 4 Homo sapiens 160 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345242 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345242&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118870480 385451305 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681777 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)Oc1ccccc1)C(=O)NO InChI=1S/C19H20FNO3/c1-13-16(8-5-9-17(13)20)19(18(22)21-23)11-10-15(12-19)24-14-6-3-2-4-7-14/h2-9,15,23H,10-12H2,1H3,(H,21,22)/t15-,19-/m0/s1 WVKUWJVGASWANR-KXBFYZLASA-N 345243 (1S,3S)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 3- phenoxycyclopentanecarboxamide::US9783488, Example 96 Histone deacetylase 4 Homo sapiens 130 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345243 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345243&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86272519 385451306 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681778 Cc1c(F)cccc1[C@@]1(CC[C@@H](C1)OCc1ccc(F)cc1)C(=O)NO InChI=1S/C20H21F2NO3/c1-13-17(3-2-4-18(13)22)20(19(24)23-25)10-9-16(11-20)26-12-14-5-7-15(21)8-6-14/h2-8,16,25H,9-12H2,1H3,(H,23,24)/t16-,20-/m0/s1 XHZFLSUCFDZBFR-JXFKEZNVSA-N 345244 (1S,3S)-1-(3-fluoro-2-methylphenyl)-3-((4-fluorobenzyl)oxy)-N-hydroxycyclopentanecarboxamide::US9783488, Example 97 Histone deacetylase 4 Homo sapiens 240 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345244 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345244&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117618999 385451307 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681779 ONC(=O)C1(CCCCC1)c1ccccc1 InChI=1S/C13H17NO2/c15-12(14-16)13(9-5-2-6-10-13)11-7-3-1-4-8-11/h1,3-4,7-8,16H,2,5-6,9-10H2,(H,14,15) UJHFECOHQHWMCI-UHFFFAOYSA-N 345245 1-phenyl-N-hydroxycyclohexylcarboxamide::US9783488, Example 98 Histone deacetylase 4 Homo sapiens >50000 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345245 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345245&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118870461 385451308 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681780 Cc1c(F)cccc1[C@@]1(CC[C@@H](CC1)c1cncc(F)c1)C(=O)NO InChI=1S/C19H20F2N2O2/c1-12-16(3-2-4-17(12)21)19(18(24)23-25)7-5-13(6-8-19)14-9-15(20)11-22-10-14/h2-4,9-11,13,25H,5-8H2,1H3,(H,23,24)/t13-,19- SEMVOCUFRMPVHZ-HJGJAMNPSA-N 345246 (1r,4r)-1-(3-Fluoro-2- methylphenyl)-4-(5- fluoropyridin-3-yl)-N- hydroxycyclohexanecarboxamide::US9783488, Example 99 Histone deacetylase 4 Homo sapiens 4100 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345246 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345246&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86272518 385451309 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681781 Cc1c(F)cccc1[C@]1(CC[C@@H](CC1)c1cncc(F)c1)C(=O)NO InChI=1S/C19H20F2N2O2/c1-12-16(3-2-4-17(12)21)19(18(24)23-25)7-5-13(6-8-19)14-9-15(20)11-22-10-14/h2-4,9-11,13,25H,5-8H2,1H3,(H,23,24)/t13-,19+ SEMVOCUFRMPVHZ-XVDXERDNSA-N 345247 (1s,4s)-1-(3-Fluoro-2- methylphenyl)-4-(5- fluoropyridin-3-yl)-N- hydroxycyclohexanecarboxamide::US9783488, Example 100 Histone deacetylase 4 Homo sapiens 660 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345247 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345247&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 86272518 385451310 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681782 Cc1c(F)cccc1[C@@]1(CC[C@@H](CC1)Oc1ccccc1)C(=O)NO InChI=1S/C20H22FNO3/c1-14-17(8-5-9-18(14)21)20(19(23)22-24)12-10-16(11-13-20)25-15-6-3-2-4-7-15/h2-9,16,24H,10-13H2,1H3,(H,22,23)/t16-,20- ADVKDBSKBQIPTJ-UKIBZPOASA-N 345248 (1r,4r)-1-(3-fluoro-2-methylphenyl)-N-hydroxy-4-phenoxycyclohexanecarboxamide::US9783488, Example 101 Histone deacetylase 4 Homo sapiens 680 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345248 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345248&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117618936 385451311 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681783 Cc1c(F)cccc1[C@]1(CC[C@@H](CC1)OCc1ccc(F)cc1)C(=O)NO InChI=1S/C21H23F2NO3/c1-14-18(3-2-4-19(14)23)21(20(25)24-26)11-9-17(10-12-21)27-13-15-5-7-16(22)8-6-15/h2-8,17,26H,9-13H2,1H3,(H,24,25)/t17-,21+ JRRTUMLUSQAANQ-UEDWGHLCSA-N 345249 (1s,4s)-1-(3-fluoro-2-methylphenyl)-4-((4-fluorobenzyl)oxy)-N-hydroxycyclohexanecarboxamide::US9783488, Example 102 Histone deacetylase 4 Homo sapiens 14000 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345249 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345249&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117618984 385451312 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681784 Cc1c(F)cccc1[C@]1(CC[C@@H](CC1)c1ccc2cnn(C)c2c1)C(=O)NO InChI=1S/C22H24FN3O2/c1-14-18(4-3-5-19(14)23)22(21(27)25-28)10-8-15(9-11-22)16-6-7-17-13-24-26(2)20(17)12-16/h3-7,12-13,15,28H,8-11H2,1-2H3,(H,25,27)/t15-,22+ WPUFWHGXUIRYPU-FVUUGDKNSA-N 345250 (1s,4s)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 4-(1-methyl-1H-indazol-6- yl)cyclohexanecarboxamide::US9783488, Example 103 Histone deacetylase 4 Homo sapiens 4200 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345250 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345250&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117618989 385451313 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681785 Cc1c(F)cccc1[C@@]1(CC[C@@H](CC1)c1ccc2cnn(C)c2c1)C(=O)NO InChI=1S/C22H24FN3O2/c1-14-18(4-3-5-19(14)23)22(21(27)25-28)10-8-15(9-11-22)16-6-7-17-13-24-26(2)20(17)12-16/h3-7,12-13,15,28H,8-11H2,1-2H3,(H,25,27)/t15-,22- WPUFWHGXUIRYPU-VVONHTQRSA-N 345251 (1r,4r)-1-(3-Fluoro-2- methylphenyl)-N-hydroxy- 4-(1-methyl-1H-indazol-6- yl)cyclohexanecarboxamide::US9783488, Example 104 Histone deacetylase 4 Homo sapiens 950 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345251 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345251&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117618989 385451314 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681786 Cc1c(F)cccc1C1(CCC2(C1)CCOCC2)C(=O)NO InChI=1S/C17H22FNO3/c1-12-13(3-2-4-14(12)18)17(15(20)19-21)6-5-16(11-17)7-9-22-10-8-16/h2-4,21H,5-11H2,1H3,(H,19,20) DACZMYXVALEWIH-UHFFFAOYSA-N 345252 (+-)-2-(3-fluoro-2-methylphenyl)-N-hydroxy-8-oxaspiro[4.5]decane-2-carboxamide::US9783488, Example 105 Histone deacetylase 4 Homo sapiens 1400 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345252 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345252&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117618993 385451315 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681787 ONC(=O)C1(CCCCCC1)c1ccccc1 InChI=1S/C14H19NO2/c16-13(15-17)14(10-6-1-2-7-11-14)12-8-4-3-5-9-12/h3-5,8-9,17H,1-2,6-7,10-11H2,(H,15,16) PXRBQXCZXPMQRW-UHFFFAOYSA-N 345253 N-hydroxy-1-phenylcycloheptanecarboxamide::US9783488, Example 106 Histone deacetylase 4 Homo sapiens 6900 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345253 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345253&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 117618991 385451316 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 681788 Cc1c(F)cccc1C1(CCCCCC1)C(=O)NO InChI=1S/C15H20FNO2/c1-11-12(7-6-8-13(11)16)15(14(18)17-19)9-4-2-3-5-10-15/h6-8,19H,2-5,9-10H2,1H3,(H,17,18) BSBQBYANILGFLN-UHFFFAOYSA-N 345254 1-(3-Fluoro-2-methylphenyl)-N-hydroxycycloheptanecarboxamide::US9783488, Example 107 Histone deacetylase 4 Homo sapiens >50000 US Patent 10.7270/Q2JH3P96 aid1797247 US9783488 Dominguez, C; Munoz-Sanjuan, I; Maillard, M; Raphy, G; Haughan, AF; Luckhurst, CA; Jarvis, RE; Burli, RW; Breccia, P; Wishart, G; Hughes, SJ; Allen, DR; Penrose, SD CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=345254 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=345254&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118870427 385451317 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673463 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1cncnc1)c1ccccc1 InChI=1S/C20H17N3O2/c24-20(23-25)19-17(14-4-2-1-3-5-14)18(19)15-8-6-13(7-9-15)16-10-21-12-22-11-16/h1-12,17-19,25H,(H,23,24)/t17-,18-,19-/m1/s1 RUTKLVXFAATEKA-GUDVDZBRSA-N 340824 US9765054, Compound 50i Histone deacetylase 4 Homo sapiens 100.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340824 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340824&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148736 385211611 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673464 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccccc1Br)c1ccccc1 InChI=1S/C16H14BrNO2/c17-12-9-5-4-8-11(12)14-13(15(14)16(19)18-20)10-6-2-1-3-7-10/h1-9,13-15,20H,(H,18,19)/t13-,14-,15-/m1/s1 JNHOJWIHQGOLJG-RBSFLKMASA-N 340825 US9765054, Compound 16a Histone deacetylase 4 Homo sapiens 620 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340825 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340825&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148622 385211612 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673465 Cc1ccccc1[C@H]1[C@@H]([C@@H]1c1ccccc1)C(=O)NO InChI=1S/C17H17NO2/c1-11-7-5-6-10-13(11)15-14(16(15)17(19)18-20)12-8-3-2-4-9-12/h2-10,14-16,20H,1H3,(H,18,19)/t14-,15-,16-/m1/s1 CJFJOOLGKHRIQZ-BZUAXINKSA-N 340827 US9765054, Compound 18a Histone deacetylase 4 Homo sapiens 1720 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340827 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340827&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148625 385211614 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673466 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1ncccn1)c1ccccc1 InChI=1S/C20H17N3O2/c24-20(23-25)18-16(13-5-2-1-3-6-13)17(18)14-7-9-15(10-8-14)19-21-11-4-12-22-19/h1-12,16-18,25H,(H,23,24)/t16-,17-,18-/m1/s1 OXSICLGZGMRVMF-KZNAEPCWSA-N 340828 US9765054, Compound 50h Histone deacetylase 4 Homo sapiens 60.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340828 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340828&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148735 385211615 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673467 ONC(=O)[C@H]1[C@@H]([C@H]1c1ccccc1F)c1ccccc1 InChI=1S/C16H14FNO2/c17-12-9-5-4-8-11(12)14-13(15(14)16(19)18-20)10-6-2-1-3-7-10/h1-9,13-15,20H,(H,18,19)/t13-,14-,15+/m1/s1 IWUNYKCIMNGBSM-KFWWJZLASA-N 340829 US9765054, Compound 13 Histone deacetylase 4 Homo sapiens 940 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340829 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340829&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148621 385211616 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673468 CC(C)Oc1ccccc1[C@H]1[C@@H]([C@@H]1c1ccccc1)C(=O)NO InChI=1S/C19H21NO3/c1-12(2)23-15-11-7-6-10-14(15)17-16(18(17)19(21)20-22)13-8-4-3-5-9-13/h3-12,16-18,22H,1-2H3,(H,20,21)/t16-,17-,18-/m1/s1 NLHMWTSWRPEZGQ-KZNAEPCWSA-N 340848 US9765054, Compound 11a Histone deacetylase 4 Homo sapiens 20570 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340848 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340848&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148619 385211634 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673469 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccccc1F)c1ccccc1 InChI=1S/C16H14FNO2/c17-12-9-5-4-8-11(12)14-13(15(14)16(19)18-20)10-6-2-1-3-7-10/h1-9,13-15,20H,(H,18,19)/t13-,14-,15-/m1/s1 IWUNYKCIMNGBSM-RBSFLKMASA-N 340849 US9765054, Compound 11b Histone deacetylase 4 Homo sapiens 320 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340849 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340849&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148620 385211635 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673470 ONC(=O)[C@@H]1[C@@H]([C@H]1c1cncnc1)c1ccccc1 InChI=1S/C14H13N3O2/c18-14(17-19)13-11(9-4-2-1-3-5-9)12(13)10-6-15-8-16-7-10/h1-8,11-13,19H,(H,17,18)/t11-,12-,13-/m1/s1 LRIWEJZWXQCFNI-JHJVBQTASA-N 340850 US9765054, Compound 25C Histone deacetylase 4 Homo sapiens 1810 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340850 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340850&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148647 385211636 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673471 ONC(=O)[C@H]1[C@@H]([C@H]1c1ccccc1)C1CCCC1 InChI=1S/C15H19NO2/c17-15(16-18)14-12(10-6-2-1-3-7-10)13(14)11-8-4-5-9-11/h1-3,6-7,11-14,18H,4-5,8-9H2,(H,16,17)/t12-,13-,14-/m1/s1 RWFKGNPIEAZMNM-MGPQQGTHSA-N 340851 US9765054, Compound 25A Histone deacetylase 4 Homo sapiens 8960 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340851 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340851&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148645 385211637 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673472 Cc1cnc(nc1)-c1ccc(cc1)[C@H]1[C@@H]([C@@H]1c1ccccc1)C(=O)NO InChI=1S/C21H19N3O2/c1-13-11-22-20(23-12-13)16-9-7-15(8-10-16)18-17(19(18)21(25)24-26)14-5-3-2-4-6-14/h2-12,17-19,26H,1H3,(H,24,25)/t17-,18-,19-/m1/s1 VEYGHBGGCALTMA-GUDVDZBRSA-N 50155843 CHEMBL3793034::US9765054, Compound 50K Histone deacetylase 4 Homo sapiens 90.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50155843 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50155843&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148738 104043210 CHEMBL3793034 ZINC28461075 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673473 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1nccc(n1)C(F)(F)F)c1ccccc1 InChI=1S/C21H16F3N3O2/c22-21(23,24)15-10-11-25-19(26-15)14-8-6-13(7-9-14)17-16(18(17)20(28)27-29)12-4-2-1-3-5-12/h1-11,16-18,29H,(H,27,28)/t16-,17-,18-/m1/s1 ABWQSANXEMWPFY-KZNAEPCWSA-N 50160875 CHEMBL3794334::US9765054, Compound 50d Histone deacetylase 4 Homo sapiens 210 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50160875 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50160875&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148714 340134789 CHEMBL3794334 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673474 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1ncc(cn1)C1CC1)c1ccccc1 InChI=1S/C23H21N3O2/c27-23(26-28)21-19(15-4-2-1-3-5-15)20(21)16-8-10-17(11-9-16)22-24-12-18(13-25-22)14-6-7-14/h1-5,8-14,19-21,28H,6-7H2,(H,26,27)/t19-,20-,21-/m1/s1 GLQPTJKDIJNVPN-NJDAHSKKSA-N 340856 US9765054, Compound 50C Histone deacetylase 4 Homo sapiens 220 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340856 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340856&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148713 385211642 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673475 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1ncc(F)cn1)c1ccccc1 InChI=1S/C20H16FN3O2/c21-15-10-22-19(23-11-15)14-8-6-13(7-9-14)17-16(18(17)20(25)24-26)12-4-2-1-3-5-12/h1-11,16-18,26H,(H,24,25)/t16-,17-,18-/m1/s1 QHCRWOYXPXJUJS-KZNAEPCWSA-N 50446479 CHEMBL3110015::US9765054, Compound 50A Histone deacetylase 4 Homo sapiens 60.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446479 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446479&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 9F4 4CBT 60148711 194944375 CHEMBL3110015 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673476 ONC(=O)[C@@H]1[C@@H]([C@H]1c1cccc(c1)-c1ncc(F)cn1)c1ccccc1 InChI=1S/C20H16FN3O2/c21-15-10-22-19(23-11-15)14-8-4-7-13(9-14)17-16(18(17)20(25)24-26)12-5-2-1-3-6-12/h1-11,16-18,26H,(H,24,25)/t16-,17-,18-/m1/s1 HTJUXGFUOHWOLU-KZNAEPCWSA-N 50446478 CHEMBL3110016::US9765054, Compound 50B Histone deacetylase 4 Homo sapiens 100.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446478 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446478&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148712 194944374 CHEMBL3110016 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673477 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccnnc1)c1ccccc1 InChI=1S/C14H13N3O2/c18-14(17-19)13-11(9-4-2-1-3-5-9)12(13)10-6-7-15-16-8-10/h1-8,11-13,19H,(H,17,18)/t11-,12-,13-/m1/s1 LEMVZYKUQHTIBM-JHJVBQTASA-N 340859 US9765054, Compound 28A Histone deacetylase 4 Homo sapiens 1090 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340859 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340859&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148666 385211645 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673478 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1cnco1)c1ccccc1 InChI=1S/C19H16N2O3/c22-19(21-23)18-16(13-4-2-1-3-5-13)17(18)14-8-6-12(7-9-14)15-10-20-11-24-15/h1-11,16-18,23H,(H,21,22)/t16-,17-,18-/m1/s1 PYWCXCBMYMFPTR-KZNAEPCWSA-N 50446472 CHEMBL3110021::US9765054, Compound 41B Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446472 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446472&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search KEE 4CBY 60148693 194944368 CHEMBL3110021 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673479 ONC(=O)[C@@H]1[C@@H]([C@H]1c1cccc(c1)-c1cnco1)c1ccccc1 InChI=1S/C19H16N2O3/c22-19(21-23)18-16(12-5-2-1-3-6-12)17(18)14-8-4-7-13(9-14)15-10-20-11-24-15/h1-11,16-18,23H,(H,21,22)/t16-,17-,18-/m1/s1 ZPIKPSAPHYWKKS-KZNAEPCWSA-N 340861 US9765054, Compound 41A Histone deacetylase 4 Homo sapiens 40.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340861 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340861&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148692 385211647 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673480 CC(C)c1nc2ccc(cc2o1)[C@H]1[C@@H]([C@@H]1c1ccccc1)C(=O)NO InChI=1S/C20H20N2O3/c1-11(2)20-21-14-9-8-13(10-15(14)25-20)17-16(18(17)19(23)22-24)12-6-4-3-5-7-12/h3-11,16-18,24H,1-2H3,(H,22,23)/t16-,17-,18-/m1/s1 RYKOEXGARNYITG-KZNAEPCWSA-N 340863 US9765054, Compound 39A Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340863 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340863&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148691 385211649 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673481 ONC(=O)[C@@H]1[C@@H]([C@H]1c1cncc(c1)C(F)(F)F)c1ccccc1 InChI=1S/C16H13F3N2O2/c17-16(18,19)11-6-10(7-20-8-11)13-12(14(13)15(22)21-23)9-4-2-1-3-5-9/h1-8,12-14,23H,(H,21,22)/t12-,13-,14-/m1/s1 KTNCYHBAMISWDO-MGPQQGTHSA-N 340864 US9765054, Compound 68 Histone deacetylase 4 Homo sapiens 230 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340864 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340864&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148809 385211650 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673482 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(nc1)C(F)(F)F)c1ccccc1 InChI=1S/C16H13F3N2O2/c17-16(18,19)11-7-6-10(8-20-11)13-12(14(13)15(22)21-23)9-4-2-1-3-5-9/h1-8,12-14,23H,(H,21,22)/t12-,13-,14-/m1/s1 BWXMGCLNRRSVLZ-MGPQQGTHSA-N 340865 US9765054, Compound 28f Histone deacetylase 4 Homo sapiens 340 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340865 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340865&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148671 385211651 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673483 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccnc(c1)C1CC1)c1ccccc1 InChI=1S/C18H18N2O2/c21-18(20-22)17-15(12-4-2-1-3-5-12)16(17)13-8-9-19-14(10-13)11-6-7-11/h1-5,8-11,15-17,22H,6-7H2,(H,20,21)/t15-,16-,17-/m1/s1 LASRJNMPYOZRDP-BRWVUGGUSA-N 50446476 CHEMBL3109993::US9765054, Compound 28B Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446476 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446476&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148667 194944372 CHEMBL3109993 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673484 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccnc(c1)C1CC1)c1ccc(F)cc1 InChI=1S/C18H17FN2O2/c19-13-5-3-11(4-6-13)15-16(17(15)18(22)21-23)12-7-8-20-14(9-12)10-1-2-10/h3-10,15-17,23H,1-2H2,(H,21,22)/t15-,16-,17-/m1/s1 ZVRAEVJPHJQADI-BRWVUGGUSA-N 340867 US9765054, Compound 25D::US9765054, Compound 28d Histone deacetylase 4 Homo sapiens 30.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340867 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340867&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148669 385211653 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673485 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc2OC(F)(F)Oc2c1)c1ccccc1 InChI=1S/C17H13F2NO4/c18-17(19)23-11-7-6-10(8-12(11)24-17)14-13(15(14)16(21)20-22)9-4-2-1-3-5-9/h1-8,13-15,22H,(H,20,21)/t13-,14-,15-/m1/s1 PEEFWEPTDKHOQN-RBSFLKMASA-N 340869 US9765054, Compound 28E Histone deacetylase 4 Homo sapiens 120 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340869 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340869&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148670 385211655 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673486 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1cnc(o1)C1CC1)c1ccccc1 InChI=1S/C22H20N2O3/c25-21(24-26)20-18(14-4-2-1-3-5-14)19(20)15-8-6-13(7-9-15)17-12-23-22(27-17)16-10-11-16/h1-9,12,16,18-20,26H,10-11H2,(H,24,25)/t18-,19-,20-/m1/s1 VFVVXZLMBWETAN-VAMGGRTRSA-N 50446470 CHEMBL3109985::US9765054, Compound 46 Histone deacetylase 4 Homo sapiens 40.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446470 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446470&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148695 194944366 CHEMBL3109985 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673487 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccnc(c1)C(F)(F)F)c1ccccc1 InChI=1S/C16H13F3N2O2/c17-16(18,19)11-8-10(6-7-20-11)13-12(14(13)15(22)21-23)9-4-2-1-3-5-9/h1-8,12-14,23H,(H,21,22)/t12-,13-,14-/m1/s1 QNOKUAAIIQQOHF-MGPQQGTHSA-N 340871 US9765054, Compound 28G Histone deacetylase 4 Homo sapiens 300 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340871 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340871&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148672 385211657 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673488 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc2C(=O)N(CC(F)(F)F)Cc2c1)c1ccccc1 InChI=1S/C20H17F3N2O3/c21-20(22,23)10-25-9-13-8-12(6-7-14(13)19(25)27)16-15(17(16)18(26)24-28)11-4-2-1-3-5-11/h1-8,15-17,28H,9-10H2,(H,24,26)/t15-,16-,17-/m1/s1 ILEGKQBIIBREPC-BRWVUGGUSA-N 50446473 CHEMBL3109983::US9765054, Compound 33 Histone deacetylase 4 Homo sapiens 30.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446473 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446473&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148690 194944369 CHEMBL3109983 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673489 ONC(=O)[C@H]1[C@@H]([C@H]1c1ccccc1F)c1ccnc(c1)C1CC1 InChI=1S/C18H17FN2O2/c19-13-4-2-1-3-12(13)16-15(17(16)18(22)21-23)11-7-8-20-14(9-11)10-5-6-10/h1-4,7-10,15-17,23H,5-6H2,(H,21,22)/t15-,16-,17+/m1/s1 DKCUOWRDLWZNHB-ZACQAIPSSA-N 340873 US9765054, Compound 28c Histone deacetylase 4 Homo sapiens 40.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340873 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340873&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148668 385211659 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673490 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccnc(c1)C1CC1)c1ccc(F)cc1 InChI=1S/C18H17FN2O2/c19-13-5-3-11(4-6-13)15-16(17(15)18(22)21-23)12-7-8-20-14(9-12)10-1-2-10/h3-10,15-17,23H,1-2H2,(H,21,22)/t15-,16-,17-/m1/s1 ZVRAEVJPHJQADI-BRWVUGGUSA-N 340867 US9765054, Compound 25D::US9765054, Compound 28d Histone deacetylase 4 Homo sapiens 120 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340867 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340867&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148669 385211653 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673491 Cn1cc(cn1)[C@H]1[C@@H]([C@@H]1c1ccccc1)C(=O)NO InChI=1S/C14H15N3O2/c1-17-8-10(7-15-17)12-11(13(12)14(18)16-19)9-5-3-2-4-6-9/h2-8,11-13,19H,1H3,(H,16,18)/t11-,12-,13-/m1/s1 KKEQSTLHUXMHBH-JHJVBQTASA-N 50446477 CHEMBL3110023::US9765054, Compound 25b Histone deacetylase 4 Homo sapiens 540 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446477 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446477&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148646 194944373 CHEMBL3110023 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673492 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1ncc(cn1)C(F)(F)F)c1ccccc1 InChI=1S/C21H16F3N3O2/c22-21(23,24)15-10-25-19(26-11-15)14-8-6-13(7-9-14)17-16(18(17)20(28)27-29)12-4-2-1-3-5-12/h1-11,16-18,29H,(H,27,28)/t16-,17-,18-/m1/s1 SVXRZLLDHWJGOQ-KZNAEPCWSA-N 340877 US9765054, Compound 50e Histone deacetylase 4 Homo sapiens 180 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340877 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340877&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148715 385211662 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673493 ONC(=O)[C@@H]1[C@@H]([C@H]1c1cc(Cl)c2OCCOc2c1)c1ccccc1 InChI=1S/C18H16ClNO4/c19-12-8-11(9-13-17(12)24-7-6-23-13)15-14(16(15)18(21)20-22)10-4-2-1-3-5-10/h1-5,8-9,14-16,22H,6-7H2,(H,20,21)/t14-,15-,16-/m1/s1 MMWFLIBCIOFXBI-BZUAXINKSA-N 50446474 CHEMBL3109980::US9765054, Compound 25e Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446474 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446474&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 57521296 194944370 CHEMBL3109980 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673494 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1cccnn1)c1ccccc1 InChI=1S/C20H17N3O2/c24-20(23-25)19-17(14-5-2-1-3-6-14)18(19)15-10-8-13(9-11-15)16-7-4-12-21-22-16/h1-12,17-19,25H,(H,23,24)/t17-,18-,19-/m1/s1 BHXISYYBPBULKV-GUDVDZBRSA-N 340879 US9765054, Compound 50f Histone deacetylase 4 Homo sapiens 80.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340879 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340879&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148716 385211664 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673495 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1ccnnc1)c1ccccc1 InChI=1S/C20H17N3O2/c24-20(23-25)19-17(14-4-2-1-3-5-14)18(19)15-8-6-13(7-9-15)16-10-11-21-22-12-16/h1-12,17-19,25H,(H,23,24)/t17-,18-,19-/m1/s1 PKRRWXSHMWTUML-GUDVDZBRSA-N 340880 US9765054, Compound 50g Histone deacetylase 4 Homo sapiens 110 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340880 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340880&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148717 385211665 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673496 CN1CCN(CC1)c1ccc(cc1)[C@H]1[C@@H]([C@@H]1c1ccccc1)C(=O)NO InChI=1S/C21H25N3O2/c1-23-11-13-24(14-12-23)17-9-7-16(8-10-17)19-18(20(19)21(25)22-26)15-5-3-2-4-6-15/h2-10,18-20,26H,11-14H2,1H3,(H,22,25)/t18-,19-,20-/m1/s1 AETXLYSOQWBYRW-VAMGGRTRSA-N 340884 US9765054, Compound 56i Histone deacetylase 4 Homo sapiens 140 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340884 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340884&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148787 385211669 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673497 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1ncco1)c1ccccc1 InChI=1S/C19H16N2O3/c22-18(21-23)17-15(12-4-2-1-3-5-12)16(17)13-6-8-14(9-7-13)19-20-10-11-24-19/h1-11,15-17,23H,(H,21,22)/t15-,16-,17-/m1/s1 MGJSXLNXMNGWKC-BRWVUGGUSA-N 340885 US9765054, Compound 58 Histone deacetylase 4 Homo sapiens 50.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340885 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340885&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148788 385211670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673498 Cn1ccnc1-c1ccc(cc1)[C@H]1[C@@H]([C@@H]1c1ccccc1)C(=O)NO InChI=1S/C20H19N3O2/c1-23-12-11-21-19(23)15-9-7-14(8-10-15)17-16(18(17)20(24)22-25)13-5-3-2-4-6-13/h2-12,16-18,25H,1H3,(H,22,24)/t16-,17-,18-/m1/s1 GBGPACXMYDEVFM-KZNAEPCWSA-N 340893 US9765054, Compound 60 Histone deacetylase 4 Homo sapiens 290 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340893 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340893&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148789 385211678 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673499 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-n1cccn1)c1ccccc1 InChI=1S/C19H17N3O2/c23-19(21-24)18-16(13-5-2-1-3-6-13)17(18)14-7-9-15(10-8-14)22-12-4-11-20-22/h1-12,16-18,24H,(H,21,23)/t16-,17-,18-/m1/s1 MOBWOZUJGKGKLV-KZNAEPCWSA-N 340898 US9765054, Compound 65 Histone deacetylase 4 Homo sapiens 90.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340898 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340898&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148808 385211683 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673500 CC1(C)CN(C1)c1ccc(cc1)[C@H]1[C@@H]([C@@H]1c1ccccc1)C(=O)NO InChI=1S/C21H24N2O2/c1-21(2)12-23(13-21)16-10-8-15(9-11-16)18-17(19(18)20(24)22-25)14-6-4-3-5-7-14/h3-11,17-19,25H,12-13H2,1-2H3,(H,22,24)/t17-,18-,19-/m1/s1 YSGJDZUBEJPAQY-GUDVDZBRSA-N 340900 US9765054, Compound 56d Histone deacetylase 4 Homo sapiens 330 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340900 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340900&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148766 385211685 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673501 CC(C)N1CCN(CC1)c1ccc(cc1)[C@H]1[C@@H]([C@@H]1c1ccccc1)C(=O)NO InChI=1S/C23H29N3O2/c1-16(2)25-12-14-26(15-13-25)19-10-8-18(9-11-19)21-20(22(21)23(27)24-28)17-6-4-3-5-7-17/h3-11,16,20-22,28H,12-15H2,1-2H3,(H,24,27)/t20-,21-,22-/m1/s1 LKLUKMPLJVDTJO-YPAWHYETSA-N 340901 US9765054, Compound 56a Histone deacetylase 4 Homo sapiens 90.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340901 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340901&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148763 385211686 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673502 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)N1CCC(F)(F)C1)c1ccccc1 InChI=1S/C20H20F2N2O2/c21-20(22)10-11-24(12-20)15-8-6-14(7-9-15)17-16(18(17)19(25)23-26)13-4-2-1-3-5-13/h1-9,16-18,26H,10-12H2,(H,23,25)/t16-,17-,18-/m1/s1 VJLWXMRFMHLDQI-KZNAEPCWSA-N 340902 US9765054, Compound 56c Histone deacetylase 4 Homo sapiens 150 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340902 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340902&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148765 385211687 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673503 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)N1CC2(COC2)C1)c1ccccc1 InChI=1S/C21H22N2O3/c24-20(22-25)19-17(14-4-2-1-3-5-14)18(19)15-6-8-16(9-7-15)23-10-21(11-23)12-26-13-21/h1-9,17-19,25H,10-13H2,(H,22,24)/t17-,18-,19-/m1/s1 YJQZJJWJCFWGMO-GUDVDZBRSA-N 340903 US9765054, Compound 56e Histone deacetylase 4 Homo sapiens 150 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340903 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340903&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148783 385211688 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673504 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1cccc(OCc2ccccc2)c1)c1ccccc1 InChI=1S/C29H25NO3/c31-29(30-32)28-26(22-10-5-2-6-11-22)27(28)23-16-14-21(15-17-23)24-12-7-13-25(18-24)33-19-20-8-3-1-4-9-20/h1-18,26-28,32H,19H2,(H,30,31)/t26-,27-,28-/m1/s1 LUJCLVLVLHGCKH-JCYYIGJDSA-N 340904 US9765054, Compound 54a Histone deacetylase 4 Homo sapiens 990 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340904 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340904&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 88925095 385211689 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673505 NC(=O)[C@@]1(O)[C@H]([C@@H]1c1ccc(cc1)C1=CCN(Cc2ccccc2)CC1)c1ccccc1 InChI=1S/C28H28N2O2/c29-27(31)28(32)25(23-9-5-2-6-10-23)26(28)24-13-11-21(12-14-24)22-15-17-30(18-16-22)19-20-7-3-1-4-8-20/h1-15,25-26,32H,16-19H2,(H2,29,31)/t25-,26-,28+/m0/s1 QPLXEWNVNXDFCO-UNCTUWKVSA-N 340906 US9765054, Compound 71 Histone deacetylase 4 Homo sapiens 350 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340906 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340906&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 138805962 385211691 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673506 CN1CCOc2cc(ccc12)-c1ccc(cc1)[C@H]1[C@@H]([C@@H]1c1ccccc1)C(=O)NO InChI=1S/C25H24N2O3/c1-27-13-14-30-21-15-19(11-12-20(21)27)16-7-9-18(10-8-16)23-22(24(23)25(28)26-29)17-5-3-2-4-6-17/h2-12,15,22-24,29H,13-14H2,1H3,(H,26,28)/t22-,23-,24-/m1/s1 PNBQXRCVDGVYGN-WXFUMESZSA-N 340907 US9765054, Compound 54c Histone deacetylase 4 Homo sapiens 260 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340907 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340907&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148762 385211692 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673507 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1ccc2CN(Cc2c1)C1CC1)c1ccccc1 InChI=1S/C27H26N2O2/c30-27(28-31)26-24(18-4-2-1-3-5-18)25(26)19-8-6-17(7-9-19)20-10-11-21-15-29(23-12-13-23)16-22(21)14-20/h1-11,14,23-26,31H,12-13,15-16H2,(H,28,30)/t24-,25-,26-/m1/s1 JREWFEAQMZQTEQ-TWJOJJKGSA-N 340908 US9765054, Compound 52 Histone deacetylase 4 Homo sapiens 480 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340908 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340908&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148740 385211693 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673508 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1ccc(cc1)-n1c2ccccc2c2ccccc12)c1ccccc1 InChI=1S/C34H26N2O2/c37-34(35-38)33-31(24-8-2-1-3-9-24)32(33)25-16-14-22(15-17-25)23-18-20-26(21-19-23)36-29-12-6-4-10-27(29)28-11-5-7-13-30(28)36/h1-21,31-33,38H,(H,35,37)/t31-,32-,33-/m1/s1 RKTQKYWUATXSLZ-WRVRXEDSSA-N 340909 US9765054, Compound 54b Histone deacetylase 4 Homo sapiens 5660 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340909 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340909&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148761 385211694 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673509 C[C@]1([C@@H]([C@H]1c1ccc(cc1)-c1ncc(F)cn1)c1ccccc1)C(=O)NO InChI=1S/C21H18FN3O2/c1-21(20(26)25-27)17(13-5-3-2-4-6-13)18(21)14-7-9-15(10-8-14)19-23-11-16(22)12-24-19/h2-12,17-18,27H,1H3,(H,25,26)/t17-,18-,21-/m1/s1 RVHCJKCUHUIJMW-DBXWQHBBSA-N 340910 US9765054, Compound 63 Histone deacetylase 4 Homo sapiens 270 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340910 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340910&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148807 385211695 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673510 CC(C)N1CCN(CC1)c1cccc(c1)[C@H]1[C@@H]([C@@H]1c1ccccc1)C(=O)NO InChI=1S/C23H29N3O2/c1-16(2)25-11-13-26(14-12-25)19-10-6-9-18(15-19)21-20(22(21)23(27)24-28)17-7-4-3-5-8-17/h3-10,15-16,20-22,28H,11-14H2,1-2H3,(H,24,27)/t20-,21-,22-/m1/s1 RUMUGZXUAHCWCB-YPAWHYETSA-N 340911 US9765054, Compound 56b Histone deacetylase 4 Homo sapiens 1430 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340911 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340911&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148764 385211696 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673511 ONC(=O)[C@@H]1[C@@H]([C@H]1c1cccc(c1)N1CCCn2nccc12)c1ccccc1 InChI=1S/C22H22N4O2/c27-22(24-28)21-19(15-6-2-1-3-7-15)20(21)16-8-4-9-17(14-16)25-12-5-13-26-18(25)10-11-23-26/h1-4,6-11,14,19-21,28H,5,12-13H2,(H,24,27)/t19-,20-,21-/m1/s1 KMAGHTJQITVHSQ-NJDAHSKKSA-N 340912 US9765054, Compound 56h Histone deacetylase 4 Homo sapiens 170 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340912 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340912&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148786 385211697 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673512 ONC(=O)[C@@H]1[C@@H]([C@H]1c1cccc(c1)N1CCN2CCCC2C1)c1ccccc1 InChI=1S/C23H27N3O2/c27-23(24-28)22-20(16-6-2-1-3-7-16)21(22)17-8-4-9-18(14-17)26-13-12-25-11-5-10-19(25)15-26/h1-4,6-9,14,19-22,28H,5,10-13,15H2,(H,24,27)/t19?,20-,21-,22-/m1/s1 UJERYDWGADPDAT-QPVBMBBTSA-N 340913 US9765054, Compound 56f Histone deacetylase 4 Homo sapiens 630 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340913 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340913&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148784 385211698 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673513 ONC(=O)[C@@H]1[C@@H]([C@H]1c1cccc(c1)N1CCC(CC1)N1CCCC1)c1ccccc1 InChI=1S/C25H31N3O2/c29-25(26-30)24-22(18-7-2-1-3-8-18)23(24)19-9-6-10-21(17-19)28-15-11-20(12-16-28)27-13-4-5-14-27/h1-3,6-10,17,20,22-24,30H,4-5,11-16H2,(H,26,29)/t22-,23-,24-/m1/s1 ABYADMUFPHKZIY-WXFUMESZSA-N 340914 US9765054, Compound 56g Histone deacetylase 4 Homo sapiens 390 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340914 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340914&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148785 385211699 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673514 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1ncc(Cl)cn1)c1ccccc1 InChI=1S/C20H16ClN3O2/c21-15-10-22-19(23-11-15)14-8-6-13(7-9-14)17-16(18(17)20(25)24-26)12-4-2-1-3-5-12/h1-11,16-18,26H,(H,24,25)/t16-,17-,18-/m1/s1 JLUNPOGVRYFTEO-KZNAEPCWSA-N 50160873 CHEMBL3794544::US9765054, Compound 50j Histone deacetylase 4 Homo sapiens 140 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50160873 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50160873&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148737 340134787 CHEMBL3794544 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673515 Cc1cnc([nH]1)-c1ccc(cc1)[C@H]1[C@@H]([C@@H]1c1ccccc1)C(=O)NO InChI=1S/C20H19N3O2/c1-12-11-21-19(22-12)15-9-7-14(8-10-15)17-16(18(17)20(24)23-25)13-5-3-2-4-6-13/h2-11,16-18,25H,1H3,(H,21,22)(H,23,24)/t16-,17-,18-/m1/s1 WYVIUYWRSQDWCQ-KZNAEPCWSA-N 340916 US9765054, Compound 50l Histone deacetylase 4 Homo sapiens 100.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340916 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340916&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148739 385211701 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673516 ONC(=O)[C@H]1[C@@H]([C@H]1c1ccccc1F)c1cc(Cl)c2OCCOc2c1 InChI=1S/C18H15ClFNO4/c19-11-7-9(8-13-17(11)25-6-5-24-13)14-15(16(14)18(22)21-23)10-3-1-2-4-12(10)20/h1-4,7-8,14-16,23H,5-6H2,(H,21,22)/t14-,15-,16+/m1/s1 NPACLGFXCONGNZ-OAGGEKHMSA-N 340917 US9765054, Compound 25f Histone deacetylase 4 Homo sapiens 30.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340917 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340917&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148649 385211702 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673517 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1cnc(o1)-c1ccccc1)c1ccccc1 InChI=1S/C25H20N2O3/c28-24(27-29)23-21(17-7-3-1-4-8-17)22(23)18-13-11-16(12-14-18)20-15-26-25(30-20)19-9-5-2-6-10-19/h1-15,21-23,29H,(H,27,28)/t21-,22-,23-/m1/s1 PUNLRYFAJRUPBG-DNVJHFABSA-N 340918 US9765054, Compound 48 Histone deacetylase 4 Homo sapiens 280 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340918 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340918&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148696 385211703 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673518 ONC(=O)C1C(C1c1ccccc1)c1ccccc1 InChI=1S/C16H15NO2/c18-16(17-19)15-13(11-7-3-1-4-8-11)14(15)12-9-5-2-6-10-12/h1-10,13-15,19H,(H,17,18) LYQRBPKRGYGRBC-UHFFFAOYSA-N 340920 US9765054, Compound 2 Histone deacetylase 4 Homo sapiens 340 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340920 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340920&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72663680 385211705 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673519 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccccc1)C1CCCCC1 InChI=1S/C16H21NO2/c18-16(17-19)15-13(11-7-3-1-4-8-11)14(15)12-9-5-2-6-10-12/h1,3-4,7-8,12-15,19H,2,5-6,9-10H2,(H,17,18)/t13-,14-,15+/m1/s1 PPDYRBZKMNSKKH-KFWWJZLASA-N 340921 US9765054, Compound 5 Histone deacetylase 4 Homo sapiens 6220 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340921 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340921&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148618 385211706 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673520 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(Br)cc1)c1ccccc1 InChI=1S/C16H14BrNO2/c17-12-8-6-11(7-9-12)14-13(15(14)16(19)18-20)10-4-2-1-3-5-10/h1-9,13-15,20H,(H,18,19)/t13-,14-,15-/m1/s1 DKTCRSTVQZYAKH-RBSFLKMASA-N 340931 US9765054, Compound 16c Histone deacetylase 4 Homo sapiens 370 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340931 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340931&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148624 385211716 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673521 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-n1ccnc1)c1ccccc1 InChI=1S/C19H17N3O2/c23-19(21-24)18-16(13-4-2-1-3-5-13)17(18)14-6-8-15(9-7-14)22-11-10-20-12-22/h1-12,16-18,24H,(H,21,23)/t16-,17-,18-/m1/s1 VXGRIZGEAGUCJY-KZNAEPCWSA-N 340948 US9765054, Compound 42 Histone deacetylase 4 Homo sapiens 200 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340948 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340948&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148694 385211733 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673522 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(NS(=O)(=O)C2CC2)cc1)c1ccccc1 InChI=1S/C19H20N2O4S/c22-19(20-23)18-16(12-4-2-1-3-5-12)17(18)13-6-8-14(9-7-13)21-26(24,25)15-10-11-15/h1-9,15-18,21,23H,10-11H2,(H,20,22)/t16-,17-,18-/m1/s1 JWTODECDZSZASS-KZNAEPCWSA-N 340949 US9765054, Compound 22 Histone deacetylase 4 Homo sapiens 50.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340949 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340949&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148644 385211734 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673523 Cc1ccc(cc1)[C@H]1[C@@H]([C@@H]1c1ccccc1)C(=O)NO InChI=1S/C17H17NO2/c1-11-7-9-13(10-8-11)15-14(16(15)17(19)18-20)12-5-3-2-4-6-12/h2-10,14-16,20H,1H3,(H,18,19)/t14-,15-,16-/m1/s1 LHDFMLMBYBDXCO-BZUAXINKSA-N 340950 US9765054, Compound 18c Histone deacetylase 4 Homo sapiens 150 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340950 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340950&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148643 385211735 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673524 ONC(=O)[C@@H]1[C@@H]([C@H]1c1cccc(Br)c1)c1ccccc1 InChI=1S/C16H14BrNO2/c17-12-8-4-7-11(9-12)14-13(15(14)16(19)18-20)10-5-2-1-3-6-10/h1-9,13-15,20H,(H,18,19)/t13-,14-,15-/m1/s1 ZHHMPPYGXARUCW-RBSFLKMASA-N 340951 US9765054, Compound 16b Histone deacetylase 4 Homo sapiens 70.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340951 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340951&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148623 385211736 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673525 Cc1cccc(c1)[C@H]1[C@@H]([C@@H]1c1ccccc1)C(=O)NO InChI=1S/C17H17NO2/c1-11-6-5-9-13(10-11)15-14(16(15)17(19)18-20)12-7-3-2-4-8-12/h2-10,14-16,20H,1H3,(H,18,19)/t14-,15-,16-/m1/s1 YDQMRNUKOOOYOK-BZUAXINKSA-N 340952 US9765054, Compound 18b Histone deacetylase 4 Homo sapiens 150 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340952 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340952&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148642 385211737 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673526 Cc1ncc(o1)-c1ccc(cc1)[C@H]1[C@@H]([C@@H]1c1ccccc1)C(=O)NO InChI=1S/C20H18N2O3/c1-12-21-11-16(25-12)13-7-9-15(10-8-13)18-17(19(18)20(23)22-24)14-5-3-2-4-6-14/h2-11,17-19,24H,1H3,(H,22,23)/t17-,18-,19-/m1/s1 KYGGGXHFZXXPPY-GUDVDZBRSA-N 50446471 CHEMBL3109984::US9765054, Compound 75a Histone deacetylase 4 Homo sapiens 30.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446471 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446471&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 76310313 194944367 CHEMBL3109984 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673527 Cc1ncc(o1)-c1ccc(cc1)[C@H]1[C@@H]([C@@H]1c1ccccc1F)C(=O)NO InChI=1S/C20H17FN2O3/c1-11-22-10-16(26-11)12-6-8-13(9-7-12)17-18(19(17)20(24)23-25)14-4-2-3-5-15(14)21/h2-10,17-19,25H,1H3,(H,23,24)/t17-,18-,19+/m1/s1 OYIJXJFUDIZMQN-QRVBRYPASA-N 340954 US9765054, Compound 75b Histone deacetylase 4 Homo sapiens 50.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340954 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340954&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148810 385211739 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673528 Cc1cnc(nc1)-c1cccc(c1)[C@H]1[C@@H]([C@@H]1c1ccccc1)C(=O)NO InChI=1S/C21H19N3O2/c1-13-11-22-20(23-12-13)16-9-5-8-15(10-16)18-17(19(18)21(25)24-26)14-6-3-2-4-7-14/h2-12,17-19,26H,1H3,(H,24,25)/t17-,18-,19-/m1/s1 PBOHUUXKBWVPSL-GUDVDZBRSA-N 340955 US9765054, Compound 77 Histone deacetylase 4 Homo sapiens 160 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340955 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340955&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90198497 385211740 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673529 ONC(=O)[C@H]1[C@@H]([C@H]1c1ccccc1F)c1cc(nc(c1)C1CC1)C1CC1 InChI=1S/C21H21FN2O2/c22-15-4-2-1-3-14(15)19-18(20(19)21(25)24-26)13-9-16(11-5-6-11)23-17(10-13)12-7-8-12/h1-4,9-12,18-20,26H,5-8H2,(H,24,25)/t18-,19-,20+/m1/s1 GINQNVLBQSXIKA-AQNXPRMDSA-N 340956 US9765054, Compound 88 Histone deacetylase 4 Homo sapiens 200 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340956 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340956&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90198638 385211741 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673530 Cc1ccn(n1)-c1ccc(cc1)[C@H]1[C@@H]([C@@H]1c1ccccc1)C(=O)NO InChI=1S/C20H19N3O2/c1-13-11-12-23(21-13)16-9-7-15(8-10-16)18-17(19(18)20(24)22-25)14-5-3-2-4-6-14/h2-12,17-19,25H,1H3,(H,22,24)/t17-,18-,19-/m1/s1 JBCDIRLTBJKQNU-GUDVDZBRSA-N 340957 US9765054, Compound 79 Histone deacetylase 4 Homo sapiens 90.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340957 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340957&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 88925102 385211742 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673531 CC(C)N1CCN(CC1)c1ccc(cn1)[C@H]1[C@@H]([C@@H]1c1ccccc1F)C(=O)NO InChI=1S/C22H27FN4O2/c1-14(2)26-9-11-27(12-10-26)18-8-7-15(13-24-18)19-20(21(19)22(28)25-29)16-5-3-4-6-17(16)23/h3-8,13-14,19-21,29H,9-12H2,1-2H3,(H,25,28)/t19-,20-,21+/m1/s1 ACSAICDEWQVODM-NJYVYQBISA-N 340958 US9765054, Compound 83 Histone deacetylase 4 Homo sapiens 120 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340958 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340958&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90198455 385211743 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673532 ONC(=O)[C@H]1[C@@H]([C@H]1c1ccccc1)c1cnn(c1)-c1ccc(cn1)C(F)(F)F InChI=1S/C19H15F3N4O2/c20-19(21,22)13-6-7-14(23-9-13)26-10-12(8-24-26)16-15(17(16)18(27)25-28)11-4-2-1-3-5-11/h1-10,15-17,28H,(H,25,27)/t15-,16-,17-/m1/s1 MELQZDOXFRBRAY-BRWVUGGUSA-N 340959 US9765054, Compound 92b Histone deacetylase 4 Homo sapiens 180 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340959 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340959&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 88925014 385211744 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673533 ONC(=O)[C@H]1[C@@H]([C@H]1c1ccccc1)c1cnc2ccccn12 InChI=1S/C17H15N3O2/c21-17(19-22)16-14(11-6-2-1-3-7-11)15(16)12-10-18-13-8-4-5-9-20(12)13/h1-10,14-16,22H,(H,19,21)/t14-,15-,16-/m1/s1 WEZDLFRIJTYUQW-BZUAXINKSA-N 340960 US9765054, Compound 115 Histone deacetylase 4 Homo sapiens 550 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340960 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340960&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60148887 385211745 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673534 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccn2cc(nc2c1)C(F)(F)F)c1ccccc1 InChI=1S/C18H14F3N3O2/c19-18(20,21)12-9-24-7-6-11(8-13(24)22-12)15-14(16(15)17(25)23-26)10-4-2-1-3-5-10/h1-9,14-16,26H,(H,23,25)/t14-,15-,16-/m1/s1 FYSJOBKTBCKGOQ-BZUAXINKSA-N 340961 US9765054, Compound 109 Histone deacetylase 4 Homo sapiens 230 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340961 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340961&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90198576 385211746 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673535 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccnc(c1)C1CC1)c1cccc(F)c1 InChI=1S/C18H17FN2O2/c19-13-3-1-2-11(8-13)15-16(17(15)18(22)21-23)12-6-7-20-14(9-12)10-4-5-10/h1-3,6-10,15-17,23H,4-5H2,(H,21,22)/t15-,16-,17-/m1/s1 KUHJLMLPBBELFW-BRWVUGGUSA-N 340962 US9765054, Compound 100b Histone deacetylase 4 Homo sapiens 20.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340962 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340962&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 88925169 385211747 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673536 Cc1cnc(s1)-c1ccc(cc1)[C@H]1[C@@H]([C@@H]1c1ccccc1)C(=O)NO InChI=1S/C20H18N2O2S/c1-12-11-21-20(25-12)15-9-7-14(8-10-15)17-16(18(17)19(23)22-24)13-5-3-2-4-6-13/h2-11,16-18,24H,1H3,(H,22,23)/t16-,17-,18-/m1/s1 DAHRPOZTYUIRLT-KZNAEPCWSA-N 340963 US9765054, Compound 102 Histone deacetylase 4 Homo sapiens 40.0 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340963 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340963&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 88925042 385211748 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 673537 ONC(=O)[C@H]1[C@@H]([C@H]1c1ccccc1F)c1ccc(NCC(F)(F)F)nc1 InChI=1S/C17H15F4N3O2/c18-11-4-2-1-3-10(11)14-13(15(14)16(25)24-26)9-5-6-12(22-7-9)23-8-17(19,20)21/h1-7,13-15,26H,8H2,(H,22,23)(H,24,25)/t13-,14-,15+/m1/s1 QALRXRCESNFEEM-KFWWJZLASA-N 340964 US9765054, Compound 106 Histone deacetylase 4 Homo sapiens 170 US Patent 10.7270/Q2XW4MZG aid1797178 US9765054 Burli, RW; Stott, AJ; Breccia, P; Dominguez, C; Munoz-Sanjuan, I; Luckhurst, CA; Hughes, SJ; Haughan, AF CHDI Foundation Inc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=340964 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=340964&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90198413 385211749 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 686553 Oc1ccccc(-c2ccccc2)c1=O InChI=1S/C13H10O2/c14-12-9-5-4-8-11(13(12)15)10-6-2-1-3-7-10/h1-9H,(H,14,15) MUSVYQMQNAIUDU-UHFFFAOYSA-N 347330 MO-OH-PHE::US9790158, 1 Histone deacetylase 4 Homo sapiens 0.080 US Patent 10.7270/Q2QZ2D3V aid1797367 US9790158 Wright, DL; Anderson, AC; Van Heyst, M; Ononye, S University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=347330 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=347330&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 10584105 386049117 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 686555 Oc1ccccc(-c2ccc3ccccc3c2)c1=O InChI=1S/C17H12O2/c18-16-8-4-3-7-15(17(16)19)14-10-9-12-5-1-2-6-13(12)11-14/h1-11H,(H,18,19) ZAJVVUCLCLFUFW-UHFFFAOYSA-N 347451 MO-OH-NAP::US9790158, 2 Histone deacetylase 4 Homo sapiens 0.540 US Patent 10.7270/Q2QZ2D3V aid1797367 US9790158 Wright, DL; Anderson, AC; Van Heyst, M; Ononye, S University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=347451 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=347451&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72163687 386049236 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 686557 COc1ccc(cc1)-c1ccccc(O)c1=O InChI=1S/C14H12O3/c1-17-11-8-6-10(7-9-11)12-4-2-3-5-13(15)14(12)16/h2-9H,1H3,(H,15,16) QQFALFLKEBDAGL-UHFFFAOYSA-N 347452 MO-OH-SM::US9790158, 3 Histone deacetylase 4 Homo sapiens 2.74 US Patent 10.7270/Q2QZ2D3V aid1797367 US9790158 Wright, DL; Anderson, AC; Van Heyst, M; Ononye, S University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=347452 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=347452&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 10728039 386049237 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 686559 COc1ccc(OC)c(c1)-c1ccccc(O)c1=O InChI=1S/C15H14O4/c1-18-10-7-8-14(19-2)12(9-10)11-5-3-4-6-13(16)15(11)17/h3-9H,1-2H3,(H,16,17) FJYSWTJLXWKKCF-UHFFFAOYSA-N 347453 MO-OH-DM::US9790158, 4 Histone deacetylase 4 Homo sapiens 184 US Patent 10.7270/Q2QZ2D3V aid1797367 US9790158 Wright, DL; Anderson, AC; Van Heyst, M; Ononye, S University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=347453 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=347453&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 614947 386049238 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 686561 COc1ccc(c(OC)c1OC)-c1ccccc(O)c1=O InChI=1S/C16H16O5/c1-19-13-9-8-11(15(20-2)16(13)21-3)10-6-4-5-7-12(17)14(10)18/h4-9H,1-3H3,(H,17,18) YTKNXWWUDKLVLK-UHFFFAOYSA-N 347454 MO-OH-TM::US9790158, 5 Histone deacetylase 4 Homo sapiens 59.0 US Patent 10.7270/Q2QZ2D3V aid1797367 US9790158 Wright, DL; Anderson, AC; Van Heyst, M; Ononye, S University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=347454 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=347454&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72163688 386049239 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 686563 Oc1cc(cccc1=O)-c1ccccc1 InChI=1S/C13H10O2/c14-12-8-4-7-11(9-13(12)15)10-5-2-1-3-6-10/h1-9H,(H,14,15) MAAPIYPCXMEMAV-UHFFFAOYSA-N 348883 US9790158, 6 Histone deacetylase 4 Homo sapiens 72.8 US Patent 10.7270/Q2QZ2D3V aid1797367 US9790158 Wright, DL; Anderson, AC; Van Heyst, M; Ononye, S University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=348883 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=348883&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11019840 386050644 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 686565 COc1cccc(c1)-c1cccc(O)c(=O)c1 InChI=1S/C14H12O3/c1-17-12-6-2-4-10(8-12)11-5-3-7-13(15)14(16)9-11/h2-9H,1H3,(H,15,16) AVTLXAUBRVYDGX-UHFFFAOYSA-N 347456 US9790158, 7 Histone deacetylase 4 Homo sapiens 1.70 US Patent 10.7270/Q2QZ2D3V aid1797367 US9790158 Wright, DL; Anderson, AC; Van Heyst, M; Ononye, S University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=347456 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=347456&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 139208364 386049241 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 686567 COc1ccc(OC)c(c1)-c1cccc(O)c(=O)c1 InChI=1S/C15H14O4/c1-18-11-6-7-15(19-2)12(9-11)10-4-3-5-13(16)14(17)8-10/h3-9H,1-2H3,(H,16,17) PRPHVLPFKCLRHC-UHFFFAOYSA-N 347457 US9790158, 8 Histone deacetylase 4 Homo sapiens 541 US Patent 10.7270/Q2QZ2D3V aid1797367 US9790158 Wright, DL; Anderson, AC; Van Heyst, M; Ononye, S University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=347457 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=347457&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71476627 386049242 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 686569 CC(C)c1cccc(O)c(=O)c1 InChI=1S/C10H12O2/c1-7(2)8-4-3-5-9(11)10(12)6-8/h3-7H,1-2H3,(H,11,12) FUWUEFKEXZQKKA-UHFFFAOYSA-N 79632 2-hydroxy-6-isopropyl-cyclohepta-2,4,6-trien-1-one::2-hydroxy-6-propan-2-yl-1-cyclohepta-2,4,6-trienone::2-hydroxy-6-propan-2-ylcyclohepta-2,4,6-trien-1-one::2-oxidanyl-6-propan-2-yl-cyclohepta-2,4,6-trien-1-one::MLS001048906::SMR000387099::US9790158, 9::cid_3611 Histone deacetylase 4 Homo sapiens 3.32 US Patent 10.7270/Q2QZ2D3V aid1797367 US9790158 Wright, DL; Anderson, AC; Van Heyst, M; Ononye, S University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=79632 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=79632&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 3611 252656278 ZINC03872809 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 686571 CC(C)(C)c1cccc(O)c(=O)c1 InChI=1S/C11H14O2/c1-11(2,3)8-5-4-6-9(12)10(13)7-8/h4-7H,1-3H3,(H,12,13) YCJXIOAKVCHNQZ-UHFFFAOYSA-N 348884 US9790158, 10 Histone deacetylase 4 Homo sapiens 489 US Patent 10.7270/Q2QZ2D3V aid1797367 US9790158 Wright, DL; Anderson, AC; Van Heyst, M; Ononye, S University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=348884 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=348884&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 10464879 386050645 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 686573 CCC(C)c1cccc(O)c(=O)c1 InChI=1S/C11H14O2/c1-3-8(2)9-5-4-6-10(12)11(13)7-9/h4-8H,3H2,1-2H3,(H,12,13) QSELYFLDJMFIRZ-UHFFFAOYSA-N 347460 US9790158, 11 Histone deacetylase 4 Homo sapiens 94.5 US Patent 10.7270/Q2QZ2D3V aid1797367 US9790158 Wright, DL; Anderson, AC; Van Heyst, M; Ononye, S University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=347460 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=347460&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71476624 386049244 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 686575 Oc1cccc(cc1=O)C1CCCC1 InChI=1S/C12H14O2/c13-11-7-3-6-10(8-12(11)14)9-4-1-2-5-9/h3,6-9H,1-2,4-5H2,(H,13,14) GWRCCABSMRGDID-UHFFFAOYSA-N 347461 US9790158, 12 Histone deacetylase 4 Homo sapiens 6.64 US Patent 10.7270/Q2QZ2D3V aid1797367 US9790158 Wright, DL; Anderson, AC; Van Heyst, M; Ononye, S University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=347461 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=347461&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71476625 386049245 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725770 ONC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1nc(cs1)-c1ccccc1 InChI=1S/C17H9F12N3O3S/c18-12(19,9(33)31-11-30-8(6-36-11)7-4-2-1-3-5-7)14(22,23)16(26,27)17(28,29)15(24,25)13(20,21)10(34)32-35/h1-6,35H,(H,32,34)(H,30,31,33) NRJBJQJGONXISQ-UHFFFAOYSA-N 50361259 CHEMBL1934901 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361259 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361259&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56951446 136965321 CHEMBL1934901 ZINC73219822 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725829 CC(=O)Nc1ccc(NC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)NO)cc1 InChI=1S/C16H11F12N3O4/c1-6(32)29-7-2-4-8(5-3-7)30-9(33)11(17,18)13(21,22)15(25,26)16(27,28)14(23,24)12(19,20)10(34)31-35/h2-5,35H,1H3,(H,29,32)(H,30,33)(H,31,34) WLACYMKJIFQEMV-UHFFFAOYSA-N 50361251 CHEMBL1934893 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361251 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361251&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 57336556 136965313 CHEMBL1934893 ZINC82158278 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725837 ONC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1ccc(cc1)-c1cnnn1-c1ccccc1 InChI=1S/C22H13F12N5O3/c23-17(24,19(27,28)21(31,32)22(33,34)20(29,30)18(25,26)16(41)37-42)15(40)36-12-8-6-11(7-9-12)14-10-35-38-39(14)13-4-2-1-3-5-13/h1-10,42H,(H,36,40)(H,37,41) DAIFBJJFPUJAIH-UHFFFAOYSA-N 50361260 CHEMBL1934902 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361260 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361260&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 57336565 136965322 CHEMBL1934902 ZINC82164608 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725838 ONC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1cccc(c1)-c1cn(nn1)-c1ccccc1 InChI=1S/C22H13F12N5O3/c23-17(24,19(27,28)21(31,32)22(33,34)20(29,30)18(25,26)16(41)37-42)15(40)35-12-6-4-5-11(9-12)14-10-39(38-36-14)13-7-2-1-3-8-13/h1-10,42H,(H,35,40)(H,37,41) GYLDACZMSVODDY-UHFFFAOYSA-N 50235704 CHEMBL4066343 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50235704 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50235704&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137632251 384991490 CHEMBL4066343 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725842 ONC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1ccc2ccc3cccc4ccc1c2c34 InChI=1S/C24H12F12N2O3/c25-19(26,21(29,30)23(33,34)24(35,36)22(31,32)20(27,28)18(40)38-41)17(39)37-14-9-7-12-5-4-10-2-1-3-11-6-8-13(14)16(12)15(10)11/h1-9,41H,(H,37,39)(H,38,40) GESAHKRRNZDSAD-UHFFFAOYSA-N 50361258 CHEMBL1934900 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361258 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361258&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 57336564 136965320 CHEMBL1934900 ZINC82158497 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725849 FC(F)(C(=O)Nc1ccccc1)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1ccccc1 InChI=1S/C20H12F12N2O2/c21-15(22,13(35)33-11-7-3-1-4-8-11)17(25,26)19(29,30)20(31,32)18(27,28)16(23,24)14(36)34-12-9-5-2-6-10-12/h1-10H,(H,33,35)(H,34,36) MOKUJYDZSIDWRN-UHFFFAOYSA-N 50361268 CHEMBL1934910 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361268 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361268&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 57401090 136965330 CHEMBL1934910 ZINC73220721 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725852 ONC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1ccccc1Cl InChI=1S/C14H7ClF12N2O3/c15-5-3-1-2-4-6(5)28-7(30)9(16,17)11(20,21)13(24,25)14(26,27)12(22,23)10(18,19)8(31)29-32/h1-4,32H,(H,28,30)(H,29,31) XESPWBKPCITCAE-UHFFFAOYSA-N 50235702 CHEMBL4104197 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50235702 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50235702&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137657892 384991488 CHEMBL4104197 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725939 ONC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1ccc(cc1)C#N InChI=1S/C15H7F12N3O3/c16-10(17,8(31)29-7-3-1-6(5-28)2-4-7)12(20,21)14(24,25)15(26,27)13(22,23)11(18,19)9(32)30-33/h1-4,33H,(H,29,31)(H,30,32) JAALGXQNNUUENT-UHFFFAOYSA-N 50361252 CHEMBL1934894 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361252 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361252&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 57336558 136965314 CHEMBL1934894 ZINC82158279 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725940 ONC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1ccc(I)cc1 InChI=1S/C14H7F12IN2O3/c15-9(16,7(30)28-6-3-1-5(27)2-4-6)11(19,20)13(23,24)14(25,26)12(21,22)10(17,18)8(31)29-32/h1-4,32H,(H,28,30)(H,29,31) VQRZUDVUZCFTDO-UHFFFAOYSA-N 50361253 CHEMBL1934895 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361253 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361253&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 57336559 136965315 CHEMBL1934895 ZINC82158280 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725941 ONC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1ccc(F)cc1 InChI=1S/C14H7F13N2O3/c15-5-1-3-6(4-2-5)28-7(30)9(16,17)11(20,21)13(24,25)14(26,27)12(22,23)10(18,19)8(31)29-32/h1-4,32H,(H,28,30)(H,29,31) LNTUQEQVBMRDNL-UHFFFAOYSA-N 50235708 CHEMBL4079958 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50235708 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50235708&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137649646 384991494 CHEMBL4079958 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725942 ONC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1cccc(Cl)c1 InChI=1S/C14H7ClF12N2O3/c15-5-2-1-3-6(4-5)28-7(30)9(16,17)11(20,21)13(24,25)14(26,27)12(22,23)10(18,19)8(31)29-32/h1-4,32H,(H,28,30)(H,29,31) BLMJAZGWDUDKEO-UHFFFAOYSA-N 50235705 CHEMBL4093113 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50235705 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50235705&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137656303 384991491 CHEMBL4093113 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725945 ONC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1cccc(c1)-c1ccccc1 InChI=1S/C20H12F12N2O3/c21-15(22,13(35)33-12-8-4-7-11(9-12)10-5-2-1-3-6-10)17(25,26)19(29,30)20(31,32)18(27,28)16(23,24)14(36)34-37/h1-9,37H,(H,33,35)(H,34,36) RFDGYNNXFQVRFM-UHFFFAOYSA-N 50361262 CHEMBL1934904 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361262 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361262&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 57336567 136965324 CHEMBL1934904 ZINC73224983 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725946 ONC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1ccc(cc1)-c1ccccc1 InChI=1S/C20H12F12N2O3/c21-15(22,13(35)33-12-8-6-11(7-9-12)10-4-2-1-3-5-10)17(25,26)19(29,30)20(31,32)18(27,28)16(23,24)14(36)34-37/h1-9,37H,(H,33,35)(H,34,36) OUDVCJKXBXYAJV-UHFFFAOYSA-N 50361255 CHEMBL1934897 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361255 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361255&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 57336561 136965317 CHEMBL1934897 ZINC82158320 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725947 ONC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1ccc2ccccc2c1 InChI=1S/C18H10F12N2O3/c19-13(20,11(33)31-10-6-5-8-3-1-2-4-9(8)7-10)15(23,24)17(27,28)18(29,30)16(25,26)14(21,22)12(34)32-35/h1-7,35H,(H,31,33)(H,32,34) RRWQSJCXNLQODI-UHFFFAOYSA-N 50361263 CHEMBL1934905 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361263 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361263&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 57336568 136965325 CHEMBL1934905 ZINC73224984 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725948 ONC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1cccc2ccccc12 InChI=1S/C18H10F12N2O3/c19-13(20,11(33)31-10-7-3-5-8-4-1-2-6-9(8)10)15(23,24)17(27,28)18(29,30)16(25,26)14(21,22)12(34)32-35/h1-7,35H,(H,31,33)(H,32,34) CXTGQWXMAKACCU-UHFFFAOYSA-N 50361261 CHEMBL1934903 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361261 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361261&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 57336566 136965323 CHEMBL1934903 ZINC73224745 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725949 CCc1cccc(NC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)NO)c1 InChI=1S/C16H12F12N2O3/c1-2-7-4-3-5-8(6-7)29-9(31)11(17,18)13(21,22)15(25,26)16(27,28)14(23,24)12(19,20)10(32)30-33/h3-6,33H,2H2,1H3,(H,29,31)(H,30,32) BPSRISCSIVKJDI-UHFFFAOYSA-N 50361256 CHEMBL1934898 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361256 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361256&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 57336562 136965318 CHEMBL1934898 ZINC82158495 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725953 ONC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1ccc(Cl)cc1 InChI=1S/C14H7ClF12N2O3/c15-5-1-3-6(4-2-5)28-7(30)9(16,17)11(20,21)13(24,25)14(26,27)12(22,23)10(18,19)8(31)29-32/h1-4,32H,(H,28,30)(H,29,31) VFALVCAGLMEJLW-UHFFFAOYSA-N 50361250 CHEMBL1934892 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361250 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361250&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 57336555 136965312 CHEMBL1934892 ZINC82158277 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725954 Cc1ccccc1NC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)NO InChI=1S/C15H10F12N2O3/c1-6-4-2-3-5-7(6)28-8(30)10(16,17)12(20,21)14(24,25)15(26,27)13(22,23)11(18,19)9(31)29-32/h2-5,32H,1H3,(H,28,30)(H,29,31) DEKQOMXTDGUZBC-UHFFFAOYSA-N 50235706 CHEMBL4080874 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50235706 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50235706&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137647616 384991492 CHEMBL4080874 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725958 ONC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1ccccc1-c1ccccc1 InChI=1S/C20H12F12N2O3/c21-15(22,13(35)33-12-9-5-4-8-11(12)10-6-2-1-3-7-10)17(25,26)19(29,30)20(31,32)18(27,28)16(23,24)14(36)34-37/h1-9,37H,(H,33,35)(H,34,36) AQHUSSNCQKXHOD-UHFFFAOYSA-N 50361264 CHEMBL1934906 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361264 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361264&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 57336569 136965326 CHEMBL1934906 ZINC73224985 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725971 Cc1cccc(NC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)NO)c1 InChI=1S/C15H10F12N2O3/c1-6-3-2-4-7(5-6)28-8(30)10(16,17)12(20,21)14(24,25)15(26,27)13(22,23)11(18,19)9(31)29-32/h2-5,32H,1H3,(H,28,30)(H,29,31) KNFFIUMUAMRWOD-UHFFFAOYSA-N 50235701 CHEMBL4098910 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50235701 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50235701&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137658785 384991487 CHEMBL4098910 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725972 Cc1ccc(NC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)NO)cc1 InChI=1S/C15H10F12N2O3/c1-6-2-4-7(5-3-6)28-8(30)10(16,17)12(20,21)14(24,25)15(26,27)13(22,23)11(18,19)9(31)29-32/h2-5,32H,1H3,(H,28,30)(H,29,31) IFSUDRKRFIOLEE-UHFFFAOYSA-N 50361249 CHEMBL1934891 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361249 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361249&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 57336554 136965311 CHEMBL1934891 ZINC73240866 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725976 Cc1ccc(NC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)NO)cc1C InChI=1S/C16H12F12N2O3/c1-6-3-4-8(5-7(6)2)29-9(31)11(17,18)13(21,22)15(25,26)16(27,28)14(23,24)12(19,20)10(32)30-33/h3-5,33H,1-2H3,(H,29,31)(H,30,32) FDDOLFDMTDIZNX-UHFFFAOYSA-N 50361254 CHEMBL1934896 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361254 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361254&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 57336560 136965316 CHEMBL1934896 ZINC82158281 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725977 ONC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1cc2ccccc2c2ccccc12 InChI=1S/C22H12F12N2O3/c23-17(24,19(27,28)21(31,32)22(33,34)20(29,30)18(25,26)16(38)36-39)15(37)35-14-9-10-5-1-2-6-11(10)12-7-3-4-8-13(12)14/h1-9,39H,(H,35,37)(H,36,38) HJRQSMKNJOBECK-UHFFFAOYSA-N 50361266 CHEMBL1934908 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361266 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361266&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 57336571 136965328 CHEMBL1934908 ZINC73224987 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725978 ONC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1cccc2cc3ccccc3cc12 InChI=1S/C22H12F12N2O3/c23-17(24,19(27,28)21(31,32)22(33,34)20(29,30)18(25,26)16(38)36-39)15(37)35-14-7-3-6-12-8-10-4-1-2-5-11(10)9-13(12)14/h1-9,39H,(H,35,37)(H,36,38) OOPMTJXKNGQOOY-UHFFFAOYSA-N 50361267 CHEMBL1934909 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361267 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361267&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 57336572 136965329 CHEMBL1934909 ZINC73220718 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725979 ONC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1ccc2cc3ccccc3cc2c1 InChI=1S/C22H12F12N2O3/c23-17(24,19(27,28)21(31,32)22(33,34)20(29,30)18(25,26)16(38)36-39)15(37)35-14-6-5-12-7-10-3-1-2-4-11(10)8-13(12)9-14/h1-9,39H,(H,35,37)(H,36,38) JUVWQWOADPQPFM-UHFFFAOYSA-N 50361265 CHEMBL1934907 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361265 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361265&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 57336570 136965327 CHEMBL1934907 ZINC73224986 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725988 ONC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)Nc1ccccc1 InChI=1S/C14H8F12N2O3/c15-9(16,7(29)27-6-4-2-1-3-5-6)11(19,20)13(23,24)14(25,26)12(21,22)10(17,18)8(30)28-31/h1-5,31H,(H,27,29)(H,28,30) PVEUUUJZCFCCIZ-UHFFFAOYSA-N 50361248 CHEMBL1934890 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361248 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361248&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 7H1 5G11,5G1A 56951447 136965310 CHEMBL1934890 ZINC40163586 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50725999 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 14000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50726000 CN(C)c1ccc(NC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)NO)cc1 InChI=1S/C16H13F12N3O3/c1-31(2)8-5-3-7(4-6-8)29-9(32)11(17,18)13(21,22)15(25,26)16(27,28)14(23,24)12(19,20)10(33)30-34/h3-6,34H,1-2H3,(H,29,32)(H,30,33) KKMDVAKOVBBMGZ-UHFFFAOYSA-N 50235703 CHEMBL4066515 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50235703 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50235703&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137631704 384991489 CHEMBL4066515 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50726001 COc1ccc(NC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(=O)NO)cc1 InChI=1S/C15H10F12N2O4/c1-33-7-4-2-6(3-5-7)28-8(30)10(16,17)12(20,21)14(24,25)15(26,27)13(22,23)11(18,19)9(31)29-32/h2-5,32H,1H3,(H,28,30)(H,29,31) FSWRFYJQOQFQCK-UHFFFAOYSA-N 50235707 CHEMBL4095542 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.bmcl.2017.02.050 10.7270/Q2JD502H 28259626 Meyners, C; Wolff, B; Kleinschek, A; Krämer, A; Meyer-Almes, FJ University of Applied Sciences Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50235707 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50235707&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137652670 384991493 CHEMBL4095542 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50758815 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.7b00467 10.7270/Q2VM4FDV 28885834 Dong, G; Chen, W; Wang, X; Yang, X; Xu, T; Wang, P; Zhang, W; Rao, Y; Miao, C; Sheng, C Second Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50758817 Nc1ccccc1NC(=O)c1ccc(Cn2cc(nn2)-c2ccc(cc2)C(=O)NCc2cccnc2)cc1 InChI=1S/C29H25N7O2/c30-25-5-1-2-6-26(25)33-29(38)24-9-7-20(8-10-24)18-36-19-27(34-35-36)22-11-13-23(14-12-22)28(37)32-17-21-4-3-15-31-16-21/h1-16,19H,17-18,30H2,(H,32,37)(H,33,38) LSGNVZAEAAZOEH-UHFFFAOYSA-N 50241438 CHEMBL4065412 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.7b00467 10.7270/Q2VM4FDV 28885834 Dong, G; Chen, W; Wang, X; Yang, X; Xu, T; Wang, P; Zhang, W; Rao, Y; Miao, C; Sheng, C Second Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50241438 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50241438&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137634086 386401839 CHEMBL4065412 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50760542 COc1ccc(cc1)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)NCCCCCC(=O)Nc1cc(ccc1N)-c1cccs1 InChI=1S/C35H37N5O4S/c1-44-26-15-12-23(13-16-26)34(42)40-31(21-25-22-38-29-9-5-4-8-27(25)29)35(43)37-18-6-2-3-11-33(41)39-30-20-24(14-17-28(30)36)32-10-7-19-45-32/h4-5,7-10,12-17,19-20,22,31,38H,2-3,6,11,18,21,36H2,1H3,(H,37,43)(H,39,41)(H,40,42)/t31-/m0/s1 BRWPGVRHKIWLEW-HKBQPEDESA-N 50242038 CHEMBL4065117 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.ejmech.2017.03.069 10.7270/Q2057J3Z 28415009 Li, X; Zhang, Y; Jiang, Y; Wu, J; Inks, ES; Chou, CJ; Gao, S; Hou, J; Ding, Q; Li, J; Wang, X; Huang, Y; Xu, W Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50242038 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50242038&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137633138 386402277 CHEMBL4065117 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50760543 COc1ccc(cc1)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)NCCCCCC(=O)Nc1ccc(F)cc1N InChI=1S/C31H34FN5O4/c1-41-23-13-10-20(11-14-23)30(39)37-28(17-21-19-35-26-8-5-4-7-24(21)26)31(40)34-16-6-2-3-9-29(38)36-27-15-12-22(32)18-25(27)33/h4-5,7-8,10-15,18-19,28,35H,2-3,6,9,16-17,33H2,1H3,(H,34,40)(H,36,38)(H,37,39)/t28-/m0/s1 CTRDRSAJXJQHFW-NDEPHWFRSA-N 50242039 CHEMBL4102988 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.ejmech.2017.03.069 10.7270/Q2057J3Z 28415009 Li, X; Zhang, Y; Jiang, Y; Wu, J; Inks, ES; Chou, CJ; Gao, S; Hou, J; Ding, Q; Li, J; Wang, X; Huang, Y; Xu, W Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50242039 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50242039&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137657586 386402278 CHEMBL4102988 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50765478 CCCNNC(=O)c1ccc(NC(=O)[C@H](Cc2c[nH]c3ccccc23)NC(=O)c2ccc(OC)cc2)cc1 InChI=1S/C29H31N5O4/c1-3-16-31-34-28(36)20-8-12-22(13-9-20)32-29(37)26(17-21-18-30-25-7-5-4-6-24(21)25)33-27(35)19-10-14-23(38-2)15-11-19/h4-15,18,26,30-31H,3,16-17H2,1-2H3,(H,32,37)(H,33,35)(H,34,36)/t26-/m0/s1 JAKZKOACZFIOQD-SANMLTNESA-N 50244779 CHEMBL4063938 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1021/acs.jmedchem.8b00136 10.7270/Q2QJ7KP9 29499113 Li, X; Peterson, YK; Inks, ES; Himes, RA; Li, J; Zhang, Y; Kong, X; Chou, CJ Medical University of South Carolina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50244779 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50244779&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137635119 386403237 CHEMBL4063938 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50800387 Cc1ccc(cc1)C(=O)NCCCCCC(=O)Nc1ccccc1N InChI=1S/C20H25N3O2/c1-15-10-12-16(13-11-15)20(25)22-14-6-2-3-9-19(24)23-18-8-5-4-7-17(18)21/h4-5,7-8,10-13H,2-3,6,9,14,21H2,1H3,(H,22,25)(H,23,24) VOPDXHFYDJAYNS-UHFFFAOYSA-N 207629 US9265734, R01::US9796664, Compound R01 Histone deacetylase 4 Homo sapiens >180000 ChEMBL 10.1021/acs.jmedchem.7b00115 10.7270/Q2FT8PGH 28771357 Bourguet, E; Ozdarska, K; Moroy, G; Jeanblanc, J; Naassila, M Universit£ de Reims Champagne-Ardenne http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=207629 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=207629&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56654642 322058198 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50800395 Nc1ccccc1NC(=O)CCCCCC(=O)Nc1ccccc1 InChI=1S/C19H23N3O2/c20-16-11-7-8-12-17(16)22-19(24)14-6-2-5-13-18(23)21-15-9-3-1-4-10-15/h1,3-4,7-12H,2,5-6,13-14,20H2,(H,21,23)(H,22,24) ZAIULUYKQLVQFH-UHFFFAOYSA-N 50254774 CHEMBL277805 Histone deacetylase 4 Homo sapiens >180000 ChEMBL 10.1021/acs.jmedchem.7b00115 10.7270/Q2FT8PGH 28771357 Bourguet, E; Ozdarska, K; Moroy, G; Jeanblanc, J; Naassila, M Universit£ de Reims Champagne-Ardenne http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50254774 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50254774&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 9543539 402360064 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50800410 C\C=C1/NC(=O)[C@H](CS)NC(=O)[C@H](NC(=O)C[C@H](OC(=O)[C@@H](NC1=O)C(C)C)\C=C\CS)C(C)C InChI=1S/C23H36N4O6S2/c1-6-15-20(29)27-19(13(4)5)23(32)33-14(8-7-9-34)10-17(28)26-18(12(2)3)22(31)25-16(11-35)21(30)24-15/h6-8,12-14,16,18-19,34-35H,9-11H2,1-5H3,(H,24,30)(H,25,31)(H,26,28)(H,27,29)/b8-7+,15-6-/t14-,16+,18-,19+/m1/s1 KEFLLVVROWXXSJ-BOPWYABFSA-N 50254779 CHEMBL4061025 Histone deacetylase 4 Homo sapiens 25 ChEMBL 10.1021/acs.jmedchem.7b00115 10.7270/Q2FT8PGH 28771357 Bourguet, E; Ozdarska, K; Moroy, G; Jeanblanc, J; Naassila, M Universit£ de Reims Champagne-Ardenne http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50254779 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50254779&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137637029 402360067 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50800502 Nc1ccccc1NC(=O)c1ccc(s1)-c1cn(CCc2cccc(c2)[N+]([O-])=O)nn1 InChI=1S/C21H18N6O3S/c22-16-6-1-2-7-17(16)23-21(28)20-9-8-19(31-20)18-13-26(25-24-18)11-10-14-4-3-5-15(12-14)27(29)30/h1-9,12-13H,10-11,22H2,(H,23,28) AXAUXMXVFLCQQK-UHFFFAOYSA-N 50121211 CHEMBL3622375 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.7b00115 10.7270/Q2FT8PGH 28771357 Bourguet, E; Ozdarska, K; Moroy, G; Jeanblanc, J; Naassila, M Universit£ de Reims Champagne-Ardenne http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50121211 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50121211&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71721558 319566163 CHEMBL3622375 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50800619 COc1ccc(\C=C\C(=O)NO)c(c1)-c1ccc(cc1)-c1ccccc1 InChI=1S/C22H19NO3/c1-26-20-13-11-19(12-14-22(24)23-25)21(15-20)18-9-7-17(8-10-18)16-5-3-2-4-6-16/h2-15,25H,1H3,(H,23,24)/b14-12+ ASHPRZYGCOMVHO-WYMLVPIESA-N 50246866 CHEMBL4078458::US11505523, Compound 22d Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.1021/acs.jmedchem.7b00115 10.7270/Q2FT8PGH 28771357 Bourguet, E; Ozdarska, K; Moroy, G; Jeanblanc, J; Naassila, M Universit£ de Reims Champagne-Ardenne http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50246866 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50246866&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 70676597 401960626 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50760229 Cn1ccc2c(CCNS(=O)(=O)c3ccc(\C=C\C(=O)NO)cc3)cccc12 InChI=1S/C20H21N3O4S/c1-23-14-12-18-16(3-2-4-19(18)23)11-13-21-28(26,27)17-8-5-15(6-9-17)7-10-20(24)22-25/h2-10,12,14,21,25H,11,13H2,1H3,(H,22,24)/b10-7+ BESZEUWJRGYGSJ-JXMROGBWSA-N 50241901 CHEMBL4065026 Histone deacetylase 4 Homo sapiens >100 ChEMBL 10.1016/j.ejmech.2017.03.079 10.7270/Q2154K5F 28395150 Mehndiratta, S; Wang, RS; Huang, HL; Su, CJ; Hsu, CM; Wu, YW; Pan, SL; Liou, JP Taipei Medical University (TMU) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50241901 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50241901&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137635575 386402181 CHEMBL4065026 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50760230 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1016/j.ejmech.2017.03.079 10.7270/Q2154K5F 28395150 Mehndiratta, S; Wang, RS; Huang, HL; Su, CJ; Hsu, CM; Wu, YW; Pan, SL; Liou, JP Taipei Medical University (TMU) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50760276 Cl.Cc1[nH]c2ccccc2c1CCNCc1cccc(\C=C\C(=O)NO)c1 InChI=1S/C21H23N3O2/c1-15-18(19-7-2-3-8-20(19)23-15)11-12-22-14-17-6-4-5-16(13-17)9-10-21(25)24-26/h2-10,13,22-23,26H,11-12,14H2,1H3,(H,24,25)/b10-9+ WCSFUXZFWJHMFA-MDZDMXLPSA-N 50241905 CHEMBL4080164 Histone deacetylase 4 Homo sapiens >100 ChEMBL 10.1016/j.ejmech.2017.03.079 10.7270/Q2154K5F 28395150 Mehndiratta, S; Wang, RS; Huang, HL; Su, CJ; Hsu, CM; Wu, YW; Pan, SL; Liou, JP Taipei Medical University (TMU) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50241905 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50241905&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137647813 386402182 CHEMBL4080164 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50760279 Nc1ccccc1NC(=O)c1ccc(CNC(=O)OCc2cccnc2)cc1 InChI=1S/C21H20N4O3/c22-18-5-1-2-6-19(18)25-20(26)17-9-7-15(8-10-17)13-24-21(27)28-14-16-4-3-11-23-12-16/h1-12H,13-14,22H2,(H,24,27)(H,25,26) INVTYAOGFAGBOE-UHFFFAOYSA-N 19410 CHEMBL27759::MS-275::US11377423, MS-275::US11672788, Compound Entinostat::US9265734, MS-275::US9796664, Compound MS-275::benzamide-type inhibitor, 3::pyridin-3-ylmethyl N-({4-[(2-aminophenyl)carbamoyl]phenyl}methyl)carbamate Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2017.03.079 10.7270/Q2154K5F 28395150 Mehndiratta, S; Wang, RS; Huang, HL; Su, CJ; Hsu, CM; Wu, YW; Pan, SL; Liou, JP Taipei Medical University (TMU) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19410 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19410&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4261 46519433 CHEMBL27759 7007 ZINC01488870 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50760310 ONC(=O)\C=C\c1ccc(cc1)S(=O)(=O)NCCc1cccc2[nH]ccc12 InChI=1S/C19H19N3O4S/c23-19(22-24)9-6-14-4-7-16(8-5-14)27(25,26)21-13-10-15-2-1-3-18-17(15)11-12-20-18/h1-9,11-12,20-21,24H,10,13H2,(H,22,23)/b9-6+ DFVAUEUMTWHQIL-RMKNXTFCSA-N 50241906 CHEMBL4069853 Histone deacetylase 4 Homo sapiens >100 ChEMBL 10.1016/j.ejmech.2017.03.079 10.7270/Q2154K5F 28395150 Mehndiratta, S; Wang, RS; Huang, HL; Su, CJ; Hsu, CM; Wu, YW; Pan, SL; Liou, JP Taipei Medical University (TMU) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50241906 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50241906&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137638741 386402183 CHEMBL4069853 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50760314 ONC(=O)\C=C\c1cccc(c1)S(=O)(=O)Nc1ccccc1 InChI=1S/C15H14N2O4S/c18-15(16-19)10-9-12-5-4-8-14(11-12)22(20,21)17-13-6-2-1-3-7-13/h1-11,17,19H,(H,16,18)/b10-9+ NCNRHFGMJRPRSK-MDZDMXLPSA-N 25150 (2E)-N-hydroxy-3-[3-(phenylsulfamoyl)phenyl]prop-2-enamide::Belinosta::Belinostat::PXD-101::PXD101 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1016/j.ejmech.2017.03.079 10.7270/Q2154K5F 28395150 Mehndiratta, S; Wang, RS; Huang, HL; Su, CJ; Hsu, CM; Wu, YW; Pan, SL; Liou, JP Taipei Medical University (TMU) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25150 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25150&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5OG 5EEN 6918638 56374291 61076 ZINC03818726 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50789136 ONC(=O)c1ccc(CN2[C@@H]3CCCC[C@@H]3CS(=O)(=O)c3ccccc23)cc1 InChI=1S/C21H24N2O4S/c24-21(22-25)16-11-9-15(10-12-16)13-23-18-6-2-1-5-17(18)14-28(26,27)20-8-4-3-7-19(20)23/h3-4,7-12,17-18,25H,1-2,5-6,13-14H2,(H,22,24)/t17-,18-/m1/s1 DMIDPYMXHVUIIM-QZTJIDSGSA-N 50252390 CHEMBL4104247 Histone deacetylase 4 Homo sapiens >30000 ChEMBL 10.1016/j.ejmech.2017.04.013 10.7270/Q2G44SQS 28453994 De Vreese, R; D'hooghe, M Ghent University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50252390 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50252390&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137656942 401963027 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50789137 Cc1nc2ccccc2n1Cc1ccc(cc1F)C(=O)NO InChI=1S/C16H14FN3O2/c1-10-18-14-4-2-3-5-15(14)20(10)9-12-7-6-11(8-13(12)17)16(21)19-22/h2-8,22H,9H2,1H3,(H,19,21) MULLJXKFRXICHS-UHFFFAOYSA-N 50252391 CHEMBL4080014 Histone deacetylase 4 Homo sapiens 500 ChEMBL 10.1016/j.ejmech.2017.04.013 10.7270/Q2G44SQS 28453994 De Vreese, R; D'hooghe, M Ghent University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50252391 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50252391&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137652442 401963028 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50789252 CN1C(=O)C2CN(Cc3c2c2ccccc2n3Cc2ccc(cc2)C(=O)NO)C1=O InChI=1S/C22H20N4O4/c1-24-21(28)16-11-25(22(24)29)12-18-19(16)15-4-2-3-5-17(15)26(18)10-13-6-8-14(9-7-13)20(27)23-30/h2-9,16,30H,10-12H2,1H3,(H,23,27) ZCAIUGLOTHAUQX-UHFFFAOYSA-N 50252395 CHEMBL4087616 Histone deacetylase 4 Homo sapiens 3820 ChEMBL 10.1016/j.ejmech.2017.04.013 10.7270/Q2G44SQS 28453994 De Vreese, R; D'hooghe, M Ghent University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50252395 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50252395&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118884610 401963032 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50789268 COc1ccc(cc1)-c1cc(-c2ccoc2)c([nH]1)C(=O)NCc1ccc(cc1)C(=O)NO InChI=1S/C29H24N4O3S/c30-24-3-1-2-4-25(24)33-28(35)20-7-5-18(6-8-20)16-31-29(36)27-23(19-9-11-22(34)12-10-19)15-26(32-27)21-13-14-37-17-21/h1-15,17,32,34H,16,30H2,(H,31,36)(H,33,35) SEYQQVKFMOLZCN-UHFFFAOYSA-N 119703 US8685992, 27 Histone deacetylase 4 Homo sapiens 1080 ChEMBL 10.1016/j.ejmech.2017.04.013 10.7270/Q2G44SQS 28453994 De Vreese, R; D'hooghe, M Ghent University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=119703 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=119703&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 67082776 220230497 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50789369 ONC(=O)c1ccc(Cn2c3CCS(=O)(=O)c3c3ccccc23)cc1 InChI=1S/C18H16N2O4S/c21-18(19-22)13-7-5-12(6-8-13)11-20-15-4-2-1-3-14(15)17-16(20)9-10-25(17,23)24/h1-8,22H,9-11H2,(H,19,21) ZXADRTUZWSITDT-UHFFFAOYSA-N 50252392 CHEMBL4069287 Histone deacetylase 4 Homo sapiens 600 ChEMBL 10.1016/j.ejmech.2017.04.013 10.7270/Q2G44SQS 28453994 De Vreese, R; D'hooghe, M Ghent University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50252392 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50252392&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118656853 401963029 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50752786 ONC(=O)CCCCCONC(=O)Nc1cnc2ccccc2c1 InChI=1S/C16H20N4O4/c21-15(19-23)8-2-1-5-9-24-20-16(22)18-13-10-12-6-3-4-7-14(12)17-11-13/h3-4,6-7,10-11,23H,1-2,5,8-9H2,(H,19,21)(H2,18,20,22) WIIHTSGYTBNRBX-UHFFFAOYSA-N 50239856 CHEMBL2311793 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.6b01538 10.7270/Q2R49SWD 28581289 Stenzel, K; Hamacher, A; Hansen, FK; Gertzen, CGW; Senger, J; Marquardt, V; Marek, L; Marek, M; Romier, C; Remke, M; Jung, M; Gohlke, H; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50239856 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50239856&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11290428 85716265 CHEMBL2311793 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50752787 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NCC1(CCOCC1)c1cnc(s1)-c1ccccc1 InChI=1S/C25H21F3N4O3S/c26-25(27,28)23-31-20(32-35-23)16-6-8-17(9-7-16)21(33)30-15-24(10-12-34-13-11-24)19-14-29-22(36-19)18-4-2-1-3-5-18/h1-9,14H,10-13,15H2,(H,30,33) FMMAEPUXSQUHEM-UHFFFAOYSA-N 50239860 CHEMBL4081343 Histone deacetylase 4 Homo sapiens 447 ChEMBL 10.1021/acs.jmedchem.6b01538 10.7270/Q2R49SWD 28581289 Stenzel, K; Hamacher, A; Hansen, FK; Gertzen, CGW; Senger, J; Marquardt, V; Marek, L; Marek, M; Romier, C; Remke, M; Jung, M; Gohlke, H; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50239860 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50239860&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44450002 85716854 CHEMBL4081343 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50752788 COc1cc(NC(=O)NOCCCCCC(=O)NO)c2nccc(C)c2c1 InChI=1S/C18H24N4O5/c1-12-7-8-19-17-14(12)10-13(26-2)11-15(17)20-18(24)22-27-9-5-3-4-6-16(23)21-25/h7-8,10-11,25H,3-6,9H2,1-2H3,(H,21,23)(H2,20,22,24) PXUBYCVDCQSMFL-UHFFFAOYSA-N 50239859 CHEMBL4088276 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.6b01538 10.7270/Q2R49SWD 28581289 Stenzel, K; Hamacher, A; Hansen, FK; Gertzen, CGW; Senger, J; Marquardt, V; Marek, L; Marek, M; Romier, C; Remke, M; Jung, M; Gohlke, H; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50239859 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50239859&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44449900 85716718 CHEMBL4088276 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50752800 COc1cc(NC(=O)NOCCCCCC(=O)NO)c2ncccc2c1 InChI=1S/C17H22N4O5/c1-25-13-10-12-6-5-8-18-16(12)14(11-13)19-17(23)21-26-9-4-2-3-7-15(22)20-24/h5-6,8,10-11,24H,2-4,7,9H2,1H3,(H,20,22)(H2,19,21,23) CLGDSTJRIXLINL-UHFFFAOYSA-N 50239857 CHEMBL4070745 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.6b01538 10.7270/Q2R49SWD 28581289 Stenzel, K; Hamacher, A; Hansen, FK; Gertzen, CGW; Senger, J; Marquardt, V; Marek, L; Marek, M; Romier, C; Remke, M; Jung, M; Gohlke, H; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50239857 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50239857&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44449600 85716268 CHEMBL4070745 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50752802 COc1cc(NC(=O)NOCCCCCC(=O)NO)c2nc(OC)cc(C)c2c1 InChI=1S/C19H26N4O6/c1-12-9-17(28-3)21-18-14(12)10-13(27-2)11-15(18)20-19(25)23-29-8-6-4-5-7-16(24)22-26/h9-11,26H,4-8H2,1-3H3,(H,22,24)(H2,20,23,25) LQJAALUQLCRUMG-UHFFFAOYSA-N 50239858 CHEMBL4067006 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.6b01538 10.7270/Q2R49SWD 28581289 Stenzel, K; Hamacher, A; Hansen, FK; Gertzen, CGW; Senger, J; Marquardt, V; Marek, L; Marek, M; Romier, C; Remke, M; Jung, M; Gohlke, H; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50239858 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50239858&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44449974 85716815 CHEMBL4067006 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50780437 CC#CCOc1ccc(cc1)C(=O)N[C@H](C(=O)NO)C(C)(C)N InChI=1S/C16H21N3O4/c1-4-5-10-23-12-8-6-11(7-9-12)14(20)18-13(15(21)19-22)16(2,3)17/h6-9,13,22H,10,17H2,1-3H3,(H,18,20)(H,19,21)/t13-/m1/s1 JPCUWLVKAJJSLN-CYBMUJFWSA-N 50249583 CHEMBL4097399 Histone deacetylase 4 Homo sapiens >30000 ChEMBL 10.1021/acs.jmedchem.7b00377 10.7270/Q2FN18MZ 28549219 Piizzi, G; Parker, DT; Peng, Y; Dobler, M; Patnaik, A; Wattanasin, S; Liu, E; Lenoir, F; Nunez, J; Kerrigan, J; McKenney, D; Osborne, C; Yu, D; Lanieri, L; Bojkovic, J; Dzink-Fox, J; Lilly, MD; Sprague, ER; Lu, Y; Wang, H; Ranjitkar, S; Xie, L; Wang, B; Glick, M; Hamann, LG; Tommasi, R; Yang, X; Dean, CR Novartis Institutes for BioMedical Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50249583 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50249583&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 7TD 5U3B 59323957 401961658 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50771238 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1 InChI=1S/C24H27N5O3/c30-22(28-32)15-9-1-2-10-16-25-23(31)19-17-26-24(27-18-19)29(20-11-5-3-6-12-20)21-13-7-4-8-14-21/h3-8,11-14,17-18,32H,1-2,9-10,15-16H2,(H,25,31)(H,28,30) QGZYDVAGYRLSKP-UHFFFAOYSA-N 50439674 RICOLINOSTAT::US10858323, Compound 2::US11207431, Example E::US8609678, 2-(diphenylamino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [26] Histone deacetylase 4 Homo sapiens 7000 ChEMBL 10.1021/acs.jmedchem.7b01404 10.7270/Q2Q81GGB 29304284 Lee, HY; Nepali, K; Huang, FI; Chang, CY; Lai, MJ; Li, YH; Huang, HL; Yang, CR; Liou, JP Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50439674 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50439674&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search AH4 5WGL 53340666 175451991 ZINC89630354 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50771242 ONC(=O)c1ccc(CNc2cccc3ncccc23)cc1 InChI=1S/C17H15N3O2/c21-17(20-22)13-8-6-12(7-9-13)11-19-16-5-1-4-15-14(16)3-2-10-18-15/h1-10,19,22H,11H2,(H,20,21) FBAMZGIGIXSVJK-UHFFFAOYSA-N 50247553 CHEMBL4095667 Histone deacetylase 4 Homo sapiens 4817 ChEMBL 10.1021/acs.jmedchem.7b01404 10.7270/Q2Q81GGB 29304284 Lee, HY; Nepali, K; Huang, FI; Chang, CY; Lai, MJ; Li, YH; Huang, HL; Yang, CR; Liou, JP Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50247553 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50247553&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 132145728 401960995 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50789061 ONC(=O)c1cccc(c1)-c1csc(CSc2ccccc2)n1 InChI=1S/C17H14N2O2S2/c20-17(19-21)13-6-4-5-12(9-13)15-10-23-16(18-15)11-22-14-7-2-1-3-8-14/h1-10,21H,11H2,(H,19,20) KWDXMPXINALNFB-UHFFFAOYSA-N 50252383 CHEMBL4105617 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.ejmech.2017.04.013 10.7270/Q2G44SQS 28453994 De Vreese, R; D'hooghe, M Ghent University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50252383 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50252383&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 76853289 401963024 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50789068 OCCN(C(=O)Cc1ccc(cc1)C(=O)NO)c1ccccc1 InChI=1S/C17H18N2O4/c20-11-10-19(15-4-2-1-3-5-15)16(21)12-13-6-8-14(9-7-13)17(22)18-23/h1-9,20,23H,10-12H2,(H,18,22) RFAZNTABYJYOAR-UHFFFAOYSA-N 198121 HPOB Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2017.04.013 10.7270/Q2G44SQS 28453994 De Vreese, R; D'hooghe, M Ghent University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=198121 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=198121&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5OJ 5EF7 71532921 318489194 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50789069 OCCN(Cc1ccc(cc1)C(=O)NO)C(=O)Cc1ccccc1 InChI=1S/C18H20N2O4/c21-11-10-20(17(22)12-14-4-2-1-3-5-14)13-15-6-8-16(9-7-15)18(23)19-24/h1-9,21,24H,10-13H2,(H,19,23) GTFAUKGKYICUDS-UHFFFAOYSA-N 50252388 CHEMBL4079541 Histone deacetylase 4 Homo sapiens 2200 ChEMBL 10.1016/j.ejmech.2017.04.013 10.7270/Q2G44SQS 28453994 De Vreese, R; D'hooghe, M Ghent University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50252388 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50252388&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search AGJ 5WGK 91810840 401963025 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50789133 CN1CCc2c(C1)c1ccccc1n2Cc1ccc(cc1)C(=O)NO InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::Tubastatin A::US10227295, Compound Tubastatin A::US10456394, Tubastatin A::US11207431, Example D::US8748451, 6::US9249087, Tubacin::US9751832, Tubastatin A::US9956192, Compound Tubastatin-A Histone deacetylase 4 Homo sapiens >30000 ChEMBL 10.1016/j.ejmech.2017.04.013 10.7270/Q2G44SQS 28453994 De Vreese, R; D'hooghe, M Ghent University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 ZINC51951670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50771413 ONC(=O)c1ccc(CNc2cccc3cccnc23)cc1 InChI=1S/C17H15N3O2/c21-17(20-22)14-8-6-12(7-9-14)11-19-15-5-1-3-13-4-2-10-18-16(13)15/h1-10,19,22H,11H2,(H,20,21) BPDQUKCPNSRTTR-UHFFFAOYSA-N 50247556 CHEMBL4104117 Histone deacetylase 4 Homo sapiens 4438 ChEMBL 10.1021/acs.jmedchem.7b01404 10.7270/Q2Q81GGB 29304284 Lee, HY; Nepali, K; Huang, FI; Chang, CY; Lai, MJ; Li, YH; Huang, HL; Yang, CR; Liou, JP Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50247556 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50247556&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 132157820 401960998 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50885675 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.7b00322 10.7270/Q2ZG6VQ5 28368585 Ahmad, M; Aga, MA; Bhat, JA; Kumar, B; Rouf, A; Capalash, N; Mintoo, MJ; Kumar, A; Mahajan, P; Mondhe, DM; Nargotra, A; Sharma, PR; Zargar, MA; Vishwakarma, RA; Shah, BA; Taneja, SC; Hamid, A CSIR-Indian Institute of Integrative Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50885688 ONC(=O)CCCCCCC(=O)Nc1ccccc1CN1CC[C@H](O)C1 InChI=1S/C19H29N3O4/c23-16-11-12-22(14-16)13-15-7-5-6-8-17(15)20-18(24)9-3-1-2-4-10-19(25)21-26/h5-8,16,23,26H,1-4,9-14H2,(H,20,24)(H,21,25)/t16-/m0/s1 PZZNYQXMSCXZEE-INIZCTEOSA-N 50265845 CHEMBL4086093 Histone deacetylase 4 Homo sapiens 7120 ChEMBL 10.1021/acs.jmedchem.7b00322 10.7270/Q2ZG6VQ5 28368585 Ahmad, M; Aga, MA; Bhat, JA; Kumar, B; Rouf, A; Capalash, N; Mintoo, MJ; Kumar, A; Mahajan, P; Mondhe, DM; Nargotra, A; Sharma, PR; Zargar, MA; Vishwakarma, RA; Shah, BA; Taneja, SC; Hamid, A CSIR-Indian Institute of Integrative Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50265845 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50265845&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 132938351 104113466 ZINC53282703 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50826923 FC(F)(F)c1nc(no1)-c1cccc(c1)C(=O)NCC1(CCOCC1)c1nc(cs1)-c1ccccc1 InChI=1S/C25H21F3N4O3S/c26-25(27,28)22-31-20(32-35-22)17-7-4-8-18(13-17)21(33)29-15-24(9-11-34-12-10-24)23-30-19(14-36-23)16-5-2-1-3-6-16/h1-8,13-14H,9-12,15H2,(H,29,33) HORXBWNTEDOVKN-UHFFFAOYSA-N 50446481 CHEMBL3110004::US10011611, TMP269::US10722597, Compound TMP-269 Histone deacetylase 4 Homo sapiens 127 ChEMBL 10.1016/j.ejmech.2016.11.033 10.7270/Q2XD145D 27886544 Lee, HY; Lee, JF; Kumar, S; Wu, YW; HuangFu, WC; Lai, MJ; Li, YH; Huang, HL; Kuo, FC; Hsiao, CJ; Cheng, CC; Yang, CR; Liou, JP Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446481 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446481&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search NU9 3ZNR 53344908 194944377 CHEMBL3110004 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50827031 COc1ccc2c(cn(Cc3ccc(cc3)C(=O)NO)c2c1)C(=O)c1cc(OC)c(OC)c(OC)c1 InChI=1S/C27H26N2O7/c1-33-19-9-10-20-21(25(30)18-11-23(34-2)26(36-4)24(12-18)35-3)15-29(22(20)13-19)14-16-5-7-17(8-6-16)27(31)28-32/h5-13,15,32H,14H2,1-4H3,(H,28,31) VTZNCZMXJPQUPZ-UHFFFAOYSA-N 50259808 CHEMBL4093691 Histone deacetylase 4 Homo sapiens 1980 ChEMBL 10.1016/j.ejmech.2016.11.033 10.7270/Q2XD145D 27886544 Lee, HY; Lee, JF; Kumar, S; Wu, YW; HuangFu, WC; Lai, MJ; Li, YH; Huang, HL; Kuo, FC; Hsiao, CJ; Cheng, CC; Yang, CR; Liou, JP Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50259808 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50259808&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137654946 404339760 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50867720 FC(F)(F)c1nc(no1)-c1cccc(c1)C(=O)NCC1(CCOCC1)c1nc(cs1)-c1ccccc1 InChI=1S/C25H21F3N4O3S/c26-25(27,28)22-31-20(32-35-22)17-7-4-8-18(13-17)21(33)29-15-24(9-11-34-12-10-24)23-30-19(14-36-23)16-5-2-1-3-6-16/h1-8,13-14H,9-12,15H2,(H,29,33) HORXBWNTEDOVKN-UHFFFAOYSA-N 50446481 CHEMBL3110004::US10011611, TMP269::US10722597, Compound TMP-269 Histone deacetylase 4 Homo sapiens 91 ChEMBL 10.1021/acs.jmedchem.7b01593 10.7270/Q24B33S0 29589441 Sellmer, A; Stangl, H; Beyer, M; Grünstein, E; Leonhardt, M; Pongratz, H; Eichhorn, E; Elz, S; Striegl, B; Jenei-Lanzl, Z; Dove, S; Straub, RH; Krämer, OH; Mahboobi, S University of Regensburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446481 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446481&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search NU9 3ZNR 53344908 194944377 CHEMBL3110004 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50867722 CN1C(=O)C2CN(Cc3c2c2ccccc2n3Cc2ccc(cc2)C(=O)NO)C1=O InChI=1S/C22H20N4O4/c1-24-21(28)16-11-25(22(24)29)12-18-19(16)15-4-2-3-5-17(15)26(18)10-13-6-8-14(9-7-13)20(27)23-30/h2-9,16,30H,10-12H2,1H3,(H,23,27) ZCAIUGLOTHAUQX-UHFFFAOYSA-N 50252395 CHEMBL4087616 Histone deacetylase 4 Homo sapiens 1821 ChEMBL 10.1021/acs.jmedchem.7b01593 10.7270/Q24B33S0 29589441 Sellmer, A; Stangl, H; Beyer, M; Grünstein, E; Leonhardt, M; Pongratz, H; Eichhorn, E; Elz, S; Striegl, B; Jenei-Lanzl, Z; Dove, S; Straub, RH; Krämer, OH; Mahboobi, S University of Regensburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50252395 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50252395&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118884610 401963032 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50942825 CC1(C)N(Cc2c1cccc2C(=O)NO)c1cnc(cn1)C(F)(F)F InChI=1S/C16H15F3N4O2/c1-15(2)11-5-3-4-9(14(24)22-25)10(11)8-23(15)13-7-20-12(6-21-13)16(17,18)19/h3-7,25H,8H2,1-2H3,(H,22,24) XCLPBILTRRWOIL-UHFFFAOYSA-N 50273526 CHEMBL4126661::US11535607, Example 22-8 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.bmcl.2018.05.021 10.7270/Q2PR7ZGX 29776742 Martin, MW; Lee, JY; Lancia, DR; Ng, PY; Han, B; Thomason, JR; Lynes, MS; Marshall, CG; Conti, C; Collis, A; Morales, MA; Doshi, K; Rudnitskaya, A; Yao, L; Zheng, X FORMA Therapeutics http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50273526 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50273526&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 134492522 405256605 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50942903 CC1(C)N(Cc2c1cccc2C(N)=O)c1cnc(cn1)C(F)(F)F InChI=1S/C16H15F3N4O/c1-15(2)11-5-3-4-9(14(20)24)10(11)8-23(15)13-7-21-12(6-22-13)16(17,18)19/h3-7H,8H2,1-2H3,(H2,20,24) WTZJBEDUYUCGGN-UHFFFAOYSA-N 50273519 CHEMBL4129930 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.bmcl.2018.05.021 10.7270/Q2PR7ZGX 29776742 Martin, MW; Lee, JY; Lancia, DR; Ng, PY; Han, B; Thomason, JR; Lynes, MS; Marshall, CG; Conti, C; Collis, A; Morales, MA; Doshi, K; Rudnitskaya, A; Yao, L; Zheng, X FORMA Therapeutics http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50273519 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50273519&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 145960971 405256598 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50992870 ONC(=O)c1ccc(CCN2C(=O)c3cccc4c(ccc(C2=O)c34)N2CCOCC2)cc1 InChI=1S/C25H23N3O5/c29-23(26-32)17-6-4-16(5-7-17)10-11-28-24(30)19-3-1-2-18-21(27-12-14-33-15-13-27)9-8-20(22(18)19)25(28)31/h1-9,32H,10-15H2,(H,26,29) CVFBZTABCOVCDI-UHFFFAOYSA-N 50283687 CHEMBL4165684 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.ejmech.2017.10.022 10.7270/Q2028V2K 29102179 Zhang, Y; Yan, J; Yao, TP Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50283687 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50283687&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 145953085 104125344 ZINC26664633 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51030196 COc1cccc(c1)-n1nc(nc1-c1cc(OC)c(OC)c(OC)c1)C(=O)NCCCCCC(=O)NO InChI=1S/C25H31N5O7/c1-34-18-10-8-9-17(15-18)30-24(16-13-19(35-2)22(37-4)20(14-16)36-3)27-23(28-30)25(32)26-12-7-5-6-11-21(31)29-33/h8-10,13-15,33H,5-7,11-12H2,1-4H3,(H,26,32)(H,29,31) KAERXSYXPLNYFJ-UHFFFAOYSA-N 50292331 CHEMBL4168150 Histone deacetylase 4 Homo sapiens 180 ChEMBL 10.1016/j.ejmech.2018.01.021 10.7270/Q2HD7Z6B 29396364 Aboeldahab, AMA; Beshr, EAM; Shoman, ME; Rabea, SM; Aly, OM Minia University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50292331 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50292331&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44445025 104133882 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51030197 ONC(=O)CCCCCCN1C(=O)NC2(CCCc3ccccc23)C1=O InChI=1S/C19H25N3O4/c23-16(21-26)11-3-1-2-6-13-22-17(24)19(20-18(22)25)12-7-9-14-8-4-5-10-15(14)19/h4-5,8,10,26H,1-3,6-7,9,11-13H2,(H,20,25)(H,21,23) KHXZULLQDRTNGQ-UHFFFAOYSA-N 50292317 CHEMBL4172557 Histone deacetylase 4 Homo sapiens 99 ChEMBL 10.1016/j.ejmech.2018.01.021 10.7270/Q2HD7Z6B 29396364 Aboeldahab, AMA; Beshr, EAM; Shoman, ME; Rabea, SM; Aly, OM Minia University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50292317 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50292317&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6169 104133868 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51030198 COc1cccc(c1)-n1nc(nc1-c1cc(OC)c(OC)c(OC)c1)C(=O)NCC(=O)NO InChI=1S/C21H23N5O7/c1-30-14-7-5-6-13(10-14)26-20(23-19(24-26)21(28)22-11-17(27)25-29)12-8-15(31-2)18(33-4)16(9-12)32-3/h5-10,29H,11H2,1-4H3,(H,22,28)(H,25,27) ZNNZLFUKMLGYQJ-UHFFFAOYSA-N 50292318 CHEMBL4174925 Histone deacetylase 4 Homo sapiens 198 ChEMBL 10.1016/j.ejmech.2018.01.021 10.7270/Q2HD7Z6B 29396364 Aboeldahab, AMA; Beshr, EAM; Shoman, ME; Rabea, SM; Aly, OM Minia University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50292318 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50292318&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 45266102 104133869 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51030199 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 91 ChEMBL 10.1016/j.ejmech.2018.01.021 10.7270/Q2HD7Z6B 29396364 Aboeldahab, AMA; Beshr, EAM; Shoman, ME; Rabea, SM; Aly, OM Minia University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51060007 CCCc1nn(C)c2c1nc([nH]c2=O)-c1cc(Cc2ccc(s2)C(=O)NO)ccc1OCC InChI=1S/C23H25N5O4S/c1-4-6-16-19-20(28(3)26-16)23(30)25-21(24-19)15-12-13(7-9-17(15)32-5-2)11-14-8-10-18(33-14)22(29)27-31/h7-10,12,31H,4-6,11H2,1-3H3,(H,27,29)(H,24,25,30) NGFDENLSEDFSFN-UHFFFAOYSA-N 50458479 CHEMBL4212186 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2018.03.005 10.7270/Q2H134MG 29549837 Rabal, O; Sánchez-Arias, JA; Cuadrado-Tejedor, M; de Miguel, I; Pérez-González, M; García-Barroso, C; Ugarte, A; Estella-Hermoso de Mendoza, A; Sáez, E; Espelosin, M; Ursua, S; Haizhong, T; Wei, W; Musheng, X; Garcia-Osta, A; Oyarzabal, J University of Navarra http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50458479 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50458479&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 136645466 433925744 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51053911 Cc1ccc(NC(=O)[C@H](Cc2c[nH]c3ccccc23)NC(=O)c2ccc(cc2)C(=O)NO)cc1 InChI=1S/C26H24N4O4/c1-16-6-12-20(13-7-16)28-26(33)23(14-19-15-27-22-5-3-2-4-21(19)22)29-24(31)17-8-10-18(11-9-17)25(32)30-34/h2-13,15,23,27,34H,14H2,1H3,(H,28,33)(H,29,31)(H,30,32)/t23-/m0/s1 LPHNTVVJNLEGGW-QHCPKHFHSA-N 50458324 CHEMBL4202863 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.ejmech.2018.02.065 10.7270/Q2X92DXX 29505935 Dadashpour, S; Emami, S Mazandaran University of Medical Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50458324 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50458324&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 145968675 433925589 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50993003 CN1CCc2c(C1)c1ccccc1n2Cc1ccc(cc1)C(=O)NO InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::Tubastatin A::US10227295, Compound Tubastatin A::US10456394, Tubastatin A::US11207431, Example D::US8748451, 6::US9249087, Tubacin::US9751832, Tubastatin A::US9956192, Compound Tubastatin-A Histone deacetylase 4 Homo sapiens >30000 ChEMBL 10.1016/j.ejmech.2017.10.022 10.7270/Q2028V2K 29102179 Zhang, Y; Yan, J; Yao, TP Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 ZINC51951670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51131015 CC(Nc1c(NCCCCCC(=O)NO)c(=O)c1=O)C12CC3CC(CC(C3)C1)C2 InChI=1S/C22H33N3O4/c1-13(22-10-14-7-15(11-22)9-16(8-14)12-22)24-19-18(20(27)21(19)28)23-6-4-2-3-5-17(26)25-29/h13-16,23-24,29H,2-12H2,1H3,(H,25,26) XNBWKNWCSWBFRL-UHFFFAOYSA-N 50463738 CHEMBL4244764 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.bmcl.2018.06.029 10.7270/Q2M0484T 30122227 Fournier, JF; Bhurruth-Alcor, Y; Musicki, B; Aubert, J; Aurelly, M; Bouix-Peter, C; Bouquet, K; Chantalat, L; Delorme, M; Drean, B; Duvert, G; Fleury-Bregeot, N; Gauthier, B; Grisendi, K; Harris, CS; Hennequin, LF; Isabet, T; Joly, F; Lafitte, G; Millois, C; Morgentin, R; Pascau, J; Piwnica, D; Rival, Y; Soulet, C; Thoreau, É; Tomas, L Nestle Skin Health R&D http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50463738 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50463738&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 145986208 433931003 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51131016 CC(C)(CCCCC(=O)NO)Nc1c(Nc2ccc(cc2)C(F)(F)F)c(=O)c1=O InChI=1S/C19H22F3N3O4/c1-18(2,10-4-3-5-13(26)25-29)24-15-14(16(27)17(15)28)23-12-8-6-11(7-9-12)19(20,21)22/h6-9,23-24,29H,3-5,10H2,1-2H3,(H,25,26) RHUMXXCHLQENCI-UHFFFAOYSA-N 50463743 CHEMBL4241370 Histone deacetylase 4 Homo sapiens 3400 ChEMBL 10.1016/j.bmcl.2018.06.029 10.7270/Q2M0484T 30122227 Fournier, JF; Bhurruth-Alcor, Y; Musicki, B; Aubert, J; Aurelly, M; Bouix-Peter, C; Bouquet, K; Chantalat, L; Delorme, M; Drean, B; Duvert, G; Fleury-Bregeot, N; Gauthier, B; Grisendi, K; Harris, CS; Hennequin, LF; Isabet, T; Joly, F; Lafitte, G; Millois, C; Morgentin, R; Pascau, J; Piwnica, D; Rival, Y; Soulet, C; Thoreau, É; Tomas, L Nestle Skin Health R&D http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50463743 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50463743&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137701235 433931008 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51131064 COc1ccc(Nc2c(NCCCCCC(=O)NO)c(=O)c2=O)cc1 InChI=1S/C17H21N3O5/c1-25-12-8-6-11(7-9-12)19-15-14(16(22)17(15)23)18-10-4-2-3-5-13(21)20-24/h6-9,18-19,24H,2-5,10H2,1H3,(H,20,21) WOGPSXAJPRAXBA-UHFFFAOYSA-N 50463739 CHEMBL4237803 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.bmcl.2018.06.029 10.7270/Q2M0484T 30122227 Fournier, JF; Bhurruth-Alcor, Y; Musicki, B; Aubert, J; Aurelly, M; Bouix-Peter, C; Bouquet, K; Chantalat, L; Delorme, M; Drean, B; Duvert, G; Fleury-Bregeot, N; Gauthier, B; Grisendi, K; Harris, CS; Hennequin, LF; Isabet, T; Joly, F; Lafitte, G; Millois, C; Morgentin, R; Pascau, J; Piwnica, D; Rival, Y; Soulet, C; Thoreau, É; Tomas, L Nestle Skin Health R&D http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50463739 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50463739&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 145983712 433931004 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51131072 Cc1[nH]c2ccccc2c1CCNCc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C21H23N3O2/c1-15-18(19-4-2-3-5-20(19)23-15)12-13-22-14-17-8-6-16(7-9-17)10-11-21(25)24-26/h2-11,22-23,26H,12-14H2,1H3,(H,24,25)/b11-10+ FPOHNWQLNRZRFC-ZHACJKMWSA-N 29589 Faridak::LBH-589::LBH-589B::Panobinostat::US10722597, Compound Panobinostat Histone deacetylase 4 Homo sapiens 170 ChEMBL 10.1016/j.bmcl.2018.06.029 10.7270/Q2M0484T 30122227 Fournier, JF; Bhurruth-Alcor, Y; Musicki, B; Aubert, J; Aurelly, M; Bouix-Peter, C; Bouquet, K; Chantalat, L; Delorme, M; Drean, B; Duvert, G; Fleury-Bregeot, N; Gauthier, B; Grisendi, K; Harris, CS; Hennequin, LF; Isabet, T; Joly, F; Lafitte, G; Millois, C; Morgentin, R; Pascau, J; Piwnica, D; Rival, Y; Soulet, C; Thoreau, É; Tomas, L Nestle Skin Health R&D http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=29589 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=29589&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search LBH 5EF8 6918837 81055018 ZINC22010649 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51131077 Cn1cc(CNCC2CCN(CC2)c2ncc(cn2)C(=O)NO)c2ccccc12 InChI=1S/C21H26N6O2/c1-26-14-17(18-4-2-3-5-19(18)26)11-22-10-15-6-8-27(9-7-15)21-23-12-16(13-24-21)20(28)25-29/h2-5,12-15,22,29H,6-11H2,1H3,(H,25,28) PAWIYAYFNXQGAP-UHFFFAOYSA-N 50105327 JNJ-26481585::Quisinostat Histone deacetylase 4 Homo sapiens 6.7 ChEMBL 10.1016/j.bmcl.2018.06.029 10.7270/Q2M0484T 30122227 Fournier, JF; Bhurruth-Alcor, Y; Musicki, B; Aubert, J; Aurelly, M; Bouix-Peter, C; Bouquet, K; Chantalat, L; Delorme, M; Drean, B; Duvert, G; Fleury-Bregeot, N; Gauthier, B; Grisendi, K; Harris, CS; Hennequin, LF; Isabet, T; Joly, F; Lafitte, G; Millois, C; Morgentin, R; Pascau, J; Piwnica, D; Rival, Y; Soulet, C; Thoreau, É; Tomas, L Nestle Skin Health R&D http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105327 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105327&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search GOK 7Q1B,6HSK,6HSH 11538455 318590494 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51002711 COc1cc2ccn(CCOc3ccc(NC(=O)CCCCCCC(=O)NO)cc3)c2cc1OC InChI=1S/C26H33N3O6/c1-33-23-17-19-13-14-29(22(19)18-24(23)34-2)15-16-35-21-11-9-20(10-12-21)27-25(30)7-5-3-4-6-8-26(31)28-32/h9-14,17-18,32H,3-8,15-16H2,1-2H3,(H,27,30)(H,28,31) RKKAAKVIUVYFTF-UHFFFAOYSA-N 50285592 CHEMBL4176214 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2017.11.092 10.7270/Q2ZW1PFR 29223096 Chao, SW; Chen, LC; Yu, CC; Liu, CY; Lin, TE; Guh, JH; Wang, CY; Chen, CY; Hsu, KC; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50285592 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50285592&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 145977717 104127163 ZINC01552285 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51003032 COc1cc2ccn(CCOc3cccc(NC(=O)CCCCCCC(=O)NO)c3)c2c(OC)c1OC InChI=1S/C27H35N3O7/c1-34-22-17-19-13-14-30(25(19)27(36-3)26(22)35-2)15-16-37-21-10-8-9-20(18-21)28-23(31)11-6-4-5-7-12-24(32)29-33/h8-10,13-14,17-18,33H,4-7,11-12,15-16H2,1-3H3,(H,28,31)(H,29,32) SFICPVORFVXNPV-UHFFFAOYSA-N 50285591 CHEMBL4162183 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2017.11.092 10.7270/Q2ZW1PFR 29223096 Chao, SW; Chen, LC; Yu, CC; Liu, CY; Lin, TE; Guh, JH; Wang, CY; Chen, CY; Hsu, KC; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50285591 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50285591&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71722010 104127162 ZINC36079863 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51003033 COc1cc2ccn(CCCCOc3cccc(NC(=O)CCCCCCC(=O)NO)c3)c2c(OC)c1OC InChI=1S/C29H39N3O7/c1-36-24-19-21-15-17-32(27(21)29(38-3)28(24)37-2)16-8-9-18-39-23-12-10-11-22(20-23)30-25(33)13-6-4-5-7-14-26(34)31-35/h10-12,15,17,19-20,35H,4-9,13-14,16,18H2,1-3H3,(H,30,33)(H,31,34) TWIPDOQQXDCJOF-UHFFFAOYSA-N 50285590 CHEMBL4172420 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2017.11.092 10.7270/Q2ZW1PFR 29223096 Chao, SW; Chen, LC; Yu, CC; Liu, CY; Lin, TE; Guh, JH; Wang, CY; Chen, CY; Hsu, KC; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50285590 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50285590&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 145951170 104127161 ZINC36079867 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51003034 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2017.11.092 10.7270/Q2ZW1PFR 29223096 Chao, SW; Chen, LC; Yu, CC; Liu, CY; Lin, TE; Guh, JH; Wang, CY; Chen, CY; Hsu, KC; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51003049 COc1ccc2n(CCOc3ccc(NC(=O)CCCCCCC(=O)NO)cc3)ccc2c1 InChI=1S/C25H31N3O5/c1-32-22-12-13-23-19(18-22)14-15-28(23)16-17-33-21-10-8-20(9-11-21)26-24(29)6-4-2-3-5-7-25(30)27-31/h8-15,18,31H,2-7,16-17H2,1H3,(H,26,29)(H,27,30) YBBZZJRLVFMWIZ-UHFFFAOYSA-N 50285589 CHEMBL4159460 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2017.11.092 10.7270/Q2ZW1PFR 29223096 Chao, SW; Chen, LC; Yu, CC; Liu, CY; Lin, TE; Guh, JH; Wang, CY; Chen, CY; Hsu, KC; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50285589 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50285589&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 145959866 104127160 ZINC00837816 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51003095 Cl.NCCCCNCCCCNCCCn1c(=O)c2ccc3c4c(ccc(c24)c1=O)c(=O)n(CCCCCC(=O)NO)c3=O InChI=1S/C31H42N6O6/c32-14-3-4-15-33-16-5-6-17-34-18-8-20-37-30(41)23-12-10-21-26-22(11-13-24(27(23)26)31(37)42)29(40)36(28(21)39)19-7-1-2-9-25(38)35-43/h10-13,33-34,43H,1-9,14-20,32H2,(H,35,38) AKKLHGKRQKYMAM-UHFFFAOYSA-N 50285612 CHEMBL4167599 Histone deacetylase 4 Homo sapiens 117000 ChEMBL 10.1021/acsmedchemlett.7b00289 10.7270/Q22N54T3 29259737 Pasini, A; Marchetti, C; Sissi, C; Cortesi, M; Giordano, E; Minarini, A; Milelli, A Alma Mater Studiorum-University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50285612 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50285612&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 145954785 104127183 ZINC43273972 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51009698 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acsmedchemlett.7b00414 10.7270/Q2CZ39PH 29348808 Chen, W; Dong, G; Wu, Y; Zhang, W; Miao, C; Sheng, C Second Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51009699 CC(C)CCN(CCCCCCC(=O)NO)c1ncc(s1)C(=O)NCCCn1ccnc1 InChI=1S/C22H36N6O3S/c1-18(2)9-14-28(13-6-4-3-5-8-20(29)26-31)22-25-16-19(32-22)21(30)24-10-7-12-27-15-11-23-17-27/h11,15-18,31H,3-10,12-14H2,1-2H3,(H,24,30)(H,26,29) RBVSKBDEAXWXGR-UHFFFAOYSA-N 50286578 CHEMBL4170617 Histone deacetylase 4 Homo sapiens 12000 ChEMBL 10.1021/acsmedchemlett.7b00414 10.7270/Q2CZ39PH 29348808 Chen, W; Dong, G; Wu, Y; Zhang, W; Miao, C; Sheng, C Second Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50286578 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50286578&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 145950884 104128149 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51009717 ONC(=O)CCCCCCN(Cc1ccc(F)cc1)c1ncc(s1)C(=O)NCCCn1ccnc1 InChI=1S/C24H31FN6O3S/c25-20-9-7-19(8-10-20)17-31(14-4-2-1-3-6-22(32)29-34)24-28-16-21(35-24)23(33)27-11-5-13-30-15-12-26-18-30/h7-10,12,15-16,18,34H,1-6,11,13-14,17H2,(H,27,33)(H,29,32) WSTLKKSKCYMNAA-UHFFFAOYSA-N 50286560 CHEMBL4163681 Histone deacetylase 4 Homo sapiens 21000 ChEMBL 10.1021/acsmedchemlett.7b00414 10.7270/Q2CZ39PH 29348808 Chen, W; Dong, G; Wu, Y; Zhang, W; Miao, C; Sheng, C Second Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50286560 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50286560&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 145962694 104128131 ZINC14294186 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51132939 FC(F)(F)c1nc(no1)-c1cccc(c1)C(=O)NCC1(CCOCC1)c1nc(cs1)-c1ccccc1 InChI=1S/C25H21F3N4O3S/c26-25(27,28)22-31-20(32-35-22)17-7-4-8-18(13-17)21(33)29-15-24(9-11-34-12-10-24)23-30-19(14-36-23)16-5-2-1-3-6-16/h1-8,13-14H,9-12,15H2,(H,29,33) HORXBWNTEDOVKN-UHFFFAOYSA-N 50446481 CHEMBL3110004::US10011611, TMP269::US10722597, Compound TMP-269 Histone deacetylase 4 Homo sapiens 353 ChEMBL 10.1016/j.ejmech.2017.11.021 10.7270/Q2PK0JT2 29150335 Cincinelli, R; Musso, L; Artali, R; Guglielmi, M; Bianchino, E; Cardile, F; Colelli, F; Pisano, C; Dallavalle, S Universit£ degli Studi di Milano http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446481 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446481&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search NU9 3ZNR 53344908 194944377 CHEMBL3110004 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51142962 CCCN1CC(=O)N2[C@@H](C)c3c(C[C@@H]2C1=O)c1ccccc1n3Cc1ccc(cc1)C(=O)NO InChI=1S/C26H28N4O4/c1-3-12-28-15-23(31)30-16(2)24-20(13-22(30)26(28)33)19-6-4-5-7-21(19)29(24)14-17-8-10-18(11-9-17)25(32)27-34/h4-11,16,22,34H,3,12-15H2,1-2H3,(H,27,32)/t16-,22+/m0/s1 PNSCXVKMXNVVCY-KSFYIVLOSA-N 50468315 CHEMBL4294514 Histone deacetylase 4 Homo sapiens 1445 ChEMBL 10.1016/j.ejmech.2018.04.046 10.7270/Q2M90CCS 29738953 Leonhardt, M; Sellmer, A; Krämer, OH; Dove, S; Elz, S; Kraus, B; Beyer, M; Mahboobi, S University of Regensburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50468315 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50468315&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 130258911 433935580 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51142964 CN1CCc2c(C1)c1ccccc1n2Cc1ccc(cc1)C(=O)NO InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::Tubastatin A::US10227295, Compound Tubastatin A::US10456394, Tubastatin A::US11207431, Example D::US8748451, 6::US9249087, Tubacin::US9751832, Tubastatin A::US9956192, Compound Tubastatin-A Histone deacetylase 4 Homo sapiens >30000 ChEMBL 10.1016/j.ejmech.2018.04.046 10.7270/Q2M90CCS 29738953 Leonhardt, M; Sellmer, A; Krämer, OH; Dove, S; Elz, S; Kraus, B; Beyer, M; Mahboobi, S University of Regensburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 ZINC51951670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51142978 CCCN1CC(=O)N2Cc3c(CC2C1=O)c1ccccc1n3Cc1ccc(cc1)C(=O)NO InChI=1S/C25H26N4O4/c1-2-11-27-15-23(30)29-14-22-19(12-21(29)25(27)32)18-5-3-4-6-20(18)28(22)13-16-7-9-17(10-8-16)24(31)26-33/h3-10,21,33H,2,11-15H2,1H3,(H,26,31) WKWJMPGMWAQUAL-UHFFFAOYSA-N 50468316 CHEMBL4280893 Histone deacetylase 4 Homo sapiens 20500 ChEMBL 10.1016/j.ejmech.2018.04.046 10.7270/Q2M90CCS 29738953 Leonhardt, M; Sellmer, A; Krämer, OH; Dove, S; Elz, S; Kraus, B; Beyer, M; Mahboobi, S University of Regensburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50468316 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50468316&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118884518 433935581 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 836774 ONC(=O)c1ccc(CN2CCCc3cc(Cl)ccc23)cc1 InChI=1S/C17H17ClN2O2/c18-15-7-8-16-14(10-15)2-1-9-20(16)11-12-3-5-13(6-4-12)17(21)19-22/h3-8,10,22H,1-2,9,11H2,(H,19,21) MNAYBFFSFQRSIT-UHFFFAOYSA-N 417049 4-((6-chloro-3,4-dihydroquinolin-1(2H)-yl)methyl)-N-hydroxybenzamide::US10456394, Example 2 Histone deacetylase 4 Homo sapiens 10950 US Patent 10.7270/Q2Q81GFW aid1803914 US10456394 Kozikowski, A; Shen, S; Bergman, J; Gaisina, I THE BOARD OF TRUSTEES OF THE UNIVERSITY OF ILLINOIS http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=417049 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=417049&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 130345472 433916959 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 836775 CN1CCc2c(C1)c1ccccc1n2Cc1ccc(cc1)C(=O)NO InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::Tubastatin A::US10227295, Compound Tubastatin A::US10456394, Tubastatin A::US11207431, Example D::US8748451, 6::US9249087, Tubacin::US9751832, Tubastatin A::US9956192, Compound Tubastatin-A Histone deacetylase 4 Homo sapiens 3670 US Patent 10.7270/Q2Q81GFW aid1803914 US10456394 Kozikowski, A; Shen, S; Bergman, J; Gaisina, I THE BOARD OF TRUSTEES OF THE UNIVERSITY OF ILLINOIS http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 ZINC51951670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197422 C[C@H](\C=C(/C)\C=C\C(=O)NO)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1 RTKIYFITIVXBLE-QEQCGCAPSA-N 50005711 CHEBI:46024::GNF-Pf-1011::TRICHOSTATIN::Trichostatin A::Trichostatin A (TSA)::US10011611, Trichostatin A::US10722597, Compound Trichostatin::US11535598, Compound Trichostatin A::US9265734, TSA Histone deacetylase 4 Homo sapiens 85 ChEMBL 10.1016/j.bmc.2013.06.009 10.7270/Q2N300XN 23820574 Feng, T; Wang, H; Su, H; Lu, H; Yu, L; Zhang, X; Sun, H; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 444732 242056952 DB04297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197423 Nc1ccccc1NC(=O)c1ccc(CNC(=O)OCc2cccnc2)cc1 InChI=1S/C21H20N4O3/c22-18-5-1-2-6-19(18)25-20(26)17-9-7-15(8-10-17)13-24-21(27)28-14-16-4-3-11-23-12-16/h1-12H,13-14,22H2,(H,24,27)(H,25,26) INVTYAOGFAGBOE-UHFFFAOYSA-N 19410 CHEMBL27759::MS-275::US11377423, MS-275::US11672788, Compound Entinostat::US9265734, MS-275::US9796664, Compound MS-275::benzamide-type inhibitor, 3::pyridin-3-ylmethyl N-({4-[(2-aminophenyl)carbamoyl]phenyl}methyl)carbamate Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmc.2013.06.009 10.7270/Q2N300XN 23820574 Feng, T; Wang, H; Su, H; Lu, H; Yu, L; Zhang, X; Sun, H; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19410 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19410&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4261 46519433 CHEMBL27759 7007 ZINC01488870 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197424 CCN(CCc1ccc2OCOc2c1)Cc1ccc(\C=C\C(=O)NO)o1 InChI=1S/C19H22N2O5/c1-2-21(10-9-14-3-7-17-18(11-14)25-13-24-17)12-16-5-4-15(26-16)6-8-19(22)20-23/h3-8,11,23H,2,9-10,12-13H2,1H3,(H,20,22)/b8-6+ WRFOGRFEKBCHAS-SOFGYWHQSA-N 50492830 CHEMBL2413311 Histone deacetylase 4 Homo sapiens 19950 ChEMBL 10.1016/j.bmc.2013.06.009 10.7270/Q2N300XN 23820574 Feng, T; Wang, H; Su, H; Lu, H; Yu, L; Zhang, X; Sun, H; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50492830 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50492830&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71770439 433960095 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197425 CCN(Cc1ccc(\C=C\C(=O)NO)o1)Cc1ccc(cc1)-c1ccccc1 InChI=1S/C23H24N2O3/c1-2-25(17-22-13-12-21(28-22)14-15-23(26)24-27)16-18-8-10-20(11-9-18)19-6-4-3-5-7-19/h3-15,27H,2,16-17H2,1H3,(H,24,26)/b15-14+ MGVYDSMTJALJHR-CCEZHUSRSA-N 50492831 CHEMBL2413299 Histone deacetylase 4 Homo sapiens 5721 ChEMBL 10.1016/j.bmc.2013.06.009 10.7270/Q2N300XN 23820574 Feng, T; Wang, H; Su, H; Lu, H; Yu, L; Zhang, X; Sun, H; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50492831 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50492831&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71770194 433960096 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197426 Cc1ccc(OCCCCN(Cc2ccc(\C=C\C(=O)NO)o2)Cc2ccccc2)cc1 InChI=1S/C26H30N2O4/c1-21-9-11-23(12-10-21)31-18-6-5-17-28(19-22-7-3-2-4-8-22)20-25-14-13-24(32-25)15-16-26(29)27-30/h2-4,7-16,30H,5-6,17-20H2,1H3,(H,27,29)/b16-15+ CVXPSEOAGUXFLC-FOCLMDBBSA-N 50492832 CHEMBL2413298 Histone deacetylase 4 Homo sapiens 12640 ChEMBL 10.1016/j.bmc.2013.06.009 10.7270/Q2N300XN 23820574 Feng, T; Wang, H; Su, H; Lu, H; Yu, L; Zhang, X; Sun, H; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50492832 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50492832&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71770193 433960097 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197427 ONC(=O)\C=C\c1ccc(CN(CCCOc2ccccc2)Cc2ccccc2)o1 InChI=1S/C24H26N2O4/c27-24(25-28)15-14-22-12-13-23(30-22)19-26(18-20-8-3-1-4-9-20)16-7-17-29-21-10-5-2-6-11-21/h1-6,8-15,28H,7,16-19H2,(H,25,27)/b15-14+ PSAHVPHAZLQMKM-CCEZHUSRSA-N 50492826 CHEMBL2413295 Histone deacetylase 4 Homo sapiens 12290 ChEMBL 10.1016/j.bmc.2013.06.009 10.7270/Q2N300XN 23820574 Feng, T; Wang, H; Su, H; Lu, H; Yu, L; Zhang, X; Sun, H; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50492826 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50492826&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71770060 433960091 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197428 ONC(=O)\C=C\c1ccc(CN(CCOc2ccccc2)Cc2ccccc2)o1 InChI=1S/C23H24N2O4/c26-23(24-27)14-13-21-11-12-22(29-21)18-25(17-19-7-3-1-4-8-19)15-16-28-20-9-5-2-6-10-20/h1-14,27H,15-18H2,(H,24,26)/b14-13+ AHOKJVSRTOKVNK-BUHFOSPRSA-N 50492827 CHEMBL2413293 Histone deacetylase 4 Homo sapiens 50560 ChEMBL 10.1016/j.bmc.2013.06.009 10.7270/Q2N300XN 23820574 Feng, T; Wang, H; Su, H; Lu, H; Yu, L; Zhang, X; Sun, H; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50492827 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50492827&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71770058 433960092 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197429 CCCCN(Cc1ccc(\C=C\C(=O)NO)o1)Cc1ccccc1 InChI=1S/C19H24N2O3/c1-2-3-13-21(14-16-7-5-4-6-8-16)15-18-10-9-17(24-18)11-12-19(22)20-23/h4-12,23H,2-3,13-15H2,1H3,(H,20,22)/b12-11+ NHJCCTCRMXGKKA-VAWYXSNFSA-N 50492833 CHEMBL2413319 Histone deacetylase 4 Homo sapiens 7260 ChEMBL 10.1016/j.bmc.2013.06.009 10.7270/Q2N300XN 23820574 Feng, T; Wang, H; Su, H; Lu, H; Yu, L; Zhang, X; Sun, H; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50492833 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50492833&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71769928 433960098 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197430 CCCN(Cc1ccc(\C=C\C(=O)NO)o1)Cc1ccccc1 InChI=1S/C18H22N2O3/c1-2-12-20(13-15-6-4-3-5-7-15)14-17-9-8-16(23-17)10-11-18(21)19-22/h3-11,22H,2,12-14H2,1H3,(H,19,21)/b11-10+ ZGVKFIQBGUKMJO-ZHACJKMWSA-N 50492834 CHEMBL2413317 Histone deacetylase 4 Homo sapiens 10630 ChEMBL 10.1016/j.bmc.2013.06.009 10.7270/Q2N300XN 23820574 Feng, T; Wang, H; Su, H; Lu, H; Yu, L; Zhang, X; Sun, H; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50492834 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50492834&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71769926 433960099 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197431 CCN(Cc1ccc(\C=C\C(=O)NO)o1)Cc1ccccc1 InChI=1S/C17H20N2O3/c1-2-19(12-14-6-4-3-5-7-14)13-16-9-8-15(22-16)10-11-17(20)18-21/h3-11,21H,2,12-13H2,1H3,(H,18,20)/b11-10+ YSHAULCJPNNZNY-ZHACJKMWSA-N 50492835 CHEMBL2413316 Histone deacetylase 4 Homo sapiens 10730 ChEMBL 10.1016/j.bmc.2013.06.009 10.7270/Q2N300XN 23820574 Feng, T; Wang, H; Su, H; Lu, H; Yu, L; Zhang, X; Sun, H; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50492835 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50492835&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71769925 433960100 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197458 CC(C)N(Cc1ccc(\C=C\C(=O)NO)o1)Cc1ccccc1 InChI=1S/C18H22N2O3/c1-14(2)20(12-15-6-4-3-5-7-15)13-17-9-8-16(23-17)10-11-18(21)19-22/h3-11,14,22H,12-13H2,1-2H3,(H,19,21)/b11-10+ CMYOLJZJCKUTKL-ZHACJKMWSA-N 50492848 CHEMBL2413318 Histone deacetylase 4 Homo sapiens 3960 ChEMBL 10.1016/j.bmc.2013.06.009 10.7270/Q2N300XN 23820574 Feng, T; Wang, H; Su, H; Lu, H; Yu, L; Zhang, X; Sun, H; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50492848 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50492848&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71769927 433960113 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197466 OCCN(Cc1ccc(\C=C\C(=O)NO)o1)Cc1ccccc1 InChI=1S/C17H20N2O4/c20-11-10-19(12-14-4-2-1-3-5-14)13-16-7-6-15(23-16)8-9-17(21)18-22/h1-9,20,22H,10-13H2,(H,18,21)/b9-8+ JMUCKMQNRPOAEH-CMDGGOBGSA-N 50492828 CHEMBL2413292 Histone deacetylase 4 Homo sapiens 11250 ChEMBL 10.1016/j.bmc.2013.06.009 10.7270/Q2N300XN 23820574 Feng, T; Wang, H; Su, H; Lu, H; Yu, L; Zhang, X; Sun, H; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50492828 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50492828&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71770057 433960093 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197475 Cc1ccc(OCCN(Cc2ccc(\C=C\C(=O)NO)o2)Cc2ccccc2)cc1 InChI=1S/C24H26N2O4/c1-19-7-9-21(10-8-19)29-16-15-26(17-20-5-3-2-4-6-20)18-23-12-11-22(30-23)13-14-24(27)25-28/h2-14,28H,15-18H2,1H3,(H,25,27)/b14-13+ IRSNSJQXWLNPKS-BUHFOSPRSA-N 50492836 CHEMBL2413294 Histone deacetylase 4 Homo sapiens 68110 ChEMBL 10.1016/j.bmc.2013.06.009 10.7270/Q2N300XN 23820574 Feng, T; Wang, H; Su, H; Lu, H; Yu, L; Zhang, X; Sun, H; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50492836 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50492836&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71770059 433960101 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197483 Cc1ccc(OCCN(CCc2ccc3OCOc3c2)Cc2ccc(\C=C\C(=O)NO)o2)cc1 InChI=1S/C26H28N2O6/c1-19-2-5-21(6-3-19)31-15-14-28(13-12-20-4-10-24-25(16-20)33-18-32-24)17-23-8-7-22(34-23)9-11-26(29)27-30/h2-11,16,30H,12-15,17-18H2,1H3,(H,27,29)/b11-9+ BOEDISARXAMAME-PKNBQFBNSA-N 50492823 CHEMBL2413289 Histone deacetylase 4 Homo sapiens 52450 ChEMBL 10.1016/j.bmc.2013.06.009 10.7270/Q2N300XN 23820574 Feng, T; Wang, H; Su, H; Lu, H; Yu, L; Zhang, X; Sun, H; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50492823 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50492823&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71770562 433960088 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197484 Cc1ccc(OCCCN(Cc2ccc(\C=C\C(=O)NO)o2)Cc2ccccc2)cc1 InChI=1S/C25H28N2O4/c1-20-8-10-22(11-9-20)30-17-5-16-27(18-21-6-3-2-4-7-21)19-24-13-12-23(31-24)14-15-25(28)26-29/h2-4,6-15,29H,5,16-19H2,1H3,(H,26,28)/b15-14+ CWLTZVKCBLVQKJ-CCEZHUSRSA-N 50492825 CHEMBL2413296 Histone deacetylase 4 Homo sapiens 13220 ChEMBL 10.1016/j.bmc.2013.06.009 10.7270/Q2N300XN 23820574 Feng, T; Wang, H; Su, H; Lu, H; Yu, L; Zhang, X; Sun, H; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50492825 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50492825&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71770191 433960090 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197485 CC(C)CN(Cc1ccc(\C=C\C(=O)NO)o1)Cc1ccccc1 InChI=1S/C19H24N2O3/c1-15(2)12-21(13-16-6-4-3-5-7-16)14-18-9-8-17(24-18)10-11-19(22)20-23/h3-11,15,23H,12-14H2,1-2H3,(H,20,22)/b11-10+ TXXJOSOSWRZWOL-ZHACJKMWSA-N 50492829 CHEMBL2413320 Histone deacetylase 4 Homo sapiens 12320 ChEMBL 10.1016/j.bmc.2013.06.009 10.7270/Q2N300XN 23820574 Feng, T; Wang, H; Su, H; Lu, H; Yu, L; Zhang, X; Sun, H; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50492829 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50492829&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71770054 433960094 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197494 Cc1ccc(OCCN(Cc2ccc(\C=C\C(=O)NO)o2)Cc2ccc(cc2)-c2ccccc2)cc1 InChI=1S/C30H30N2O4/c1-23-7-13-27(14-8-23)35-20-19-32(22-29-16-15-28(36-29)17-18-30(33)31-34)21-24-9-11-26(12-10-24)25-5-3-2-4-6-25/h2-18,34H,19-22H2,1H3,(H,31,33)/b18-17+ HBOMAKTUMCGYJX-ISLYRVAYSA-N 50492824 CHEMBL2413306 Histone deacetylase 4 Homo sapiens 9070 ChEMBL 10.1016/j.bmc.2013.06.009 10.7270/Q2N300XN 23820574 Feng, T; Wang, H; Su, H; Lu, H; Yu, L; Zhang, X; Sun, H; You, Q China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50492824 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50492824&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71770321 433960089 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51202071 CCOC(=O)NCCCC(=O)NCCc1ccccc1 InChI=1S/C15H22N2O3/c1-2-20-15(19)17-11-6-9-14(18)16-12-10-13-7-4-3-5-8-13/h3-5,7-8H,2,6,9-12H2,1H3,(H,16,18)(H,17,19) HTOYBIILVCHURC-UHFFFAOYSA-N 50494415 CHEMBL3086767 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/np400198r 10.7270/Q21J9DQ7 24164245 Pavlik, CM; Wong, CY; Ononye, S; Lopez, DD; Engene, N; McPhail, KL; Gerwick, WH; Balunas, MJ University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50494415 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50494415&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72946782 433961680 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51202074 ONC(=O)CCCC(=O)NCCc1ccccc1 InChI=1S/C13H18N2O3/c16-12(7-4-8-13(17)15-18)14-10-9-11-5-2-1-3-6-11/h1-3,5-6,18H,4,7-10H2,(H,14,16)(H,15,17) MNMBNWINDLRVJD-UHFFFAOYSA-N 50494414 CHEMBL3086768 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/np400198r 10.7270/Q21J9DQ7 24164245 Pavlik, CM; Wong, CY; Ononye, S; Lopez, DD; Engene, N; McPhail, KL; Gerwick, WH; Balunas, MJ University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50494414 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50494414&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72734543 433961679 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51202078 CCOC(=O)NCCCC(=O)NCCc1ccccc1 InChI=1S/C15H22N2O3/c1-2-20-15(19)17-11-6-9-14(18)16-12-10-13-7-4-3-5-8-13/h3-5,7-8H,2,6,9-12H2,1H3,(H,16,18)(H,17,19) HTOYBIILVCHURC-UHFFFAOYSA-N 50494415 CHEMBL3086767 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/np400198r 10.7270/Q21J9DQ7 24164245 Pavlik, CM; Wong, CY; Ononye, S; Lopez, DD; Engene, N; McPhail, KL; Gerwick, WH; Balunas, MJ University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50494415 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50494415&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72946782 433961680 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51196642 CC(C)c1cccc(=O)c(O)c1 InChI=1S/C10H12O2/c1-7(2)8-4-3-5-9(11)10(12)6-8/h3-7H,1-2H3,(H,11,12) FUWUEFKEXZQKKA-UHFFFAOYSA-N 50330794 2-Hydroxy-4-isopropyl-cyclohepta-2,4,6-trienone::2-hydroxy-4-isopropyl-2,4,6-cycloheptatrien-1-one::CHEMBL48310::beta-thujaplicin::hinokitiol Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.1021/ml400158k 10.7270/Q28055HS 24900743 Ononye, SN; VanHeyst, MD; Oblak, EZ; Zhou, W; Ammar, M; Anderson, AC; Wright, DL University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50330794 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50330794&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 3611 123109909 10447 CHEMBL48310 C09904 ZINC95911093 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51196643 Oc1ccccc(-c2ccc3ccccc3c2)c1=O InChI=1S/C17H12O2/c18-16-8-4-3-7-15(17(16)19)14-10-9-12-5-1-2-6-13(12)11-14/h1-11H,(H,18,19) ZAJVVUCLCLFUFW-UHFFFAOYSA-N 347451 MO-OH-NAP::US9790158, 2 Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.1021/ml400158k 10.7270/Q28055HS 24900743 Ononye, SN; VanHeyst, MD; Oblak, EZ; Zhou, W; Ammar, M; Anderson, AC; Wright, DL University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=347451 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=347451&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72163687 386049236 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51196644 Oc1ccccc(-c2ccccc2)c1=O InChI=1S/C13H10O2/c14-12-9-5-4-8-11(13(12)15)10-6-2-1-3-7-10/h1-9H,(H,14,15) MUSVYQMQNAIUDU-UHFFFAOYSA-N 347330 MO-OH-PHE::US9790158, 1 Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.1021/ml400158k 10.7270/Q28055HS 24900743 Ononye, SN; VanHeyst, MD; Oblak, EZ; Zhou, W; Ammar, M; Anderson, AC; Wright, DL University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=347330 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=347330&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 10584105 386049117 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51196652 C[C@H](\C=C(/C)\C=C\C(=O)NO)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1 RTKIYFITIVXBLE-QEQCGCAPSA-N 50005711 CHEBI:46024::GNF-Pf-1011::TRICHOSTATIN::Trichostatin A::Trichostatin A (TSA)::US10011611, Trichostatin A::US10722597, Compound Trichostatin::US11535598, Compound Trichostatin A::US9265734, TSA Histone deacetylase 4 Homo sapiens 14547 ChEMBL 10.1021/ml400158k 10.7270/Q28055HS 24900743 Ononye, SN; VanHeyst, MD; Oblak, EZ; Zhou, W; Ammar, M; Anderson, AC; Wright, DL University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 444732 242056952 DB04297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51196653 COc1ccc(OC)c(c1)-c1cccc(O)c(=O)c1 InChI=1S/C15H14O4/c1-18-11-6-7-15(19-2)12(9-11)10-4-3-5-13(16)14(17)8-10/h3-9H,1-2H3,(H,16,17) PRPHVLPFKCLRHC-UHFFFAOYSA-N 347457 US9790158, 8 Histone deacetylase 4 Homo sapiens 11204 ChEMBL 10.1021/ml400158k 10.7270/Q28055HS 24900743 Ononye, SN; VanHeyst, MD; Oblak, EZ; Zhou, W; Ammar, M; Anderson, AC; Wright, DL University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=347457 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=347457&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71476627 386049242 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51196654 Oc1cccc(cc1=O)C1CCCC1 InChI=1S/C12H14O2/c13-11-7-3-6-10(8-12(11)14)9-4-1-2-5-9/h3,6-9H,1-2,4-5H2,(H,13,14) GWRCCABSMRGDID-UHFFFAOYSA-N 347461 US9790158, 12 Histone deacetylase 4 Homo sapiens 990 ChEMBL 10.1021/ml400158k 10.7270/Q28055HS 24900743 Ononye, SN; VanHeyst, MD; Oblak, EZ; Zhou, W; Ammar, M; Anderson, AC; Wright, DL University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=347461 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=347461&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71476625 386049245 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51196669 COc1ccc(cc1)-c1ccccc(O)c1=O InChI=1S/C14H12O3/c1-17-11-8-6-10(7-9-11)12-4-2-3-5-13(15)14(12)16/h2-9H,1H3,(H,15,16) QQFALFLKEBDAGL-UHFFFAOYSA-N 347452 MO-OH-SM::US9790158, 3 Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.1021/ml400158k 10.7270/Q28055HS 24900743 Ononye, SN; VanHeyst, MD; Oblak, EZ; Zhou, W; Ammar, M; Anderson, AC; Wright, DL University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=347452 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=347452&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 10728039 386049237 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51196671 CC(C)(C)c1cccc(O)c(=O)c1 InChI=1S/C11H14O2/c1-11(2,3)8-5-4-6-9(12)10(13)7-8/h4-7H,1-3H3,(H,12,13) YCJXIOAKVCHNQZ-UHFFFAOYSA-N 348884 US9790158, 10 Histone deacetylase 4 Homo sapiens 806 ChEMBL 10.1021/ml400158k 10.7270/Q28055HS 24900743 Ononye, SN; VanHeyst, MD; Oblak, EZ; Zhou, W; Ammar, M; Anderson, AC; Wright, DL University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=348884 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=348884&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 10464879 386050645 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51196676 COc1ccc(OC)c(c1)-c1ccccc(O)c1=O InChI=1S/C15H14O4/c1-18-10-7-8-14(19-2)12(9-10)11-5-3-4-6-13(16)15(11)17/h3-9H,1-2H3,(H,16,17) FJYSWTJLXWKKCF-UHFFFAOYSA-N 347453 MO-OH-DM::US9790158, 4 Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.1021/ml400158k 10.7270/Q28055HS 24900743 Ononye, SN; VanHeyst, MD; Oblak, EZ; Zhou, W; Ammar, M; Anderson, AC; Wright, DL University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=347453 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=347453&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 614947 386049238 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51196681 COc1ccc(c(OC)c1OC)-c1ccccc(O)c1=O InChI=1S/C16H16O5/c1-19-13-9-8-11(15(20-2)16(13)21-3)10-6-4-5-7-12(17)14(10)18/h4-9H,1-3H3,(H,17,18) YTKNXWWUDKLVLK-UHFFFAOYSA-N 347454 MO-OH-TM::US9790158, 5 Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.1021/ml400158k 10.7270/Q28055HS 24900743 Ononye, SN; VanHeyst, MD; Oblak, EZ; Zhou, W; Ammar, M; Anderson, AC; Wright, DL University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=347454 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=347454&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72163688 386049239 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51196686 COc1cccc(cc1=O)C(C)C InChI=1S/C11H14O2/c1-8(2)9-5-4-6-11(13-3)10(12)7-9/h4-8H,1-3H3 DNORQMNGHAZBGW-UHFFFAOYSA-N 50492542 CHEMBL2408248 Histone deacetylase 4 Homo sapiens 11641 ChEMBL 10.1021/ml400158k 10.7270/Q28055HS 24900743 Ononye, SN; VanHeyst, MD; Oblak, EZ; Zhou, W; Ammar, M; Anderson, AC; Wright, DL University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50492542 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50492542&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 12542182 433959807 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51196687 CCC(C)c1cccc(O)c(=O)c1 InChI=1S/C11H14O2/c1-3-8(2)9-5-4-6-10(12)11(13)7-9/h4-8H,3H2,1-2H3,(H,12,13) QSELYFLDJMFIRZ-UHFFFAOYSA-N 347460 US9790158, 11 Histone deacetylase 4 Homo sapiens 6115 ChEMBL 10.1021/ml400158k 10.7270/Q28055HS 24900743 Ononye, SN; VanHeyst, MD; Oblak, EZ; Zhou, W; Ammar, M; Anderson, AC; Wright, DL University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=347460 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=347460&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71476624 386049244 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51196700 COc1ccc(cc1)-c1cccc(O)c(=O)c1 InChI=1S/C14H12O3/c1-17-12-7-5-10(6-8-12)11-3-2-4-13(15)14(16)9-11/h2-9H,1H3,(H,15,16) ONWOFQLLGGJDEH-UHFFFAOYSA-N 50492540 CHEMBL2408243 Histone deacetylase 4 Homo sapiens 8361 ChEMBL 10.1021/ml400158k 10.7270/Q28055HS 24900743 Ononye, SN; VanHeyst, MD; Oblak, EZ; Zhou, W; Ammar, M; Anderson, AC; Wright, DL University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50492540 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50492540&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71476626 433959805 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51196701 Oc1cccc(cc1=O)-c1ccccc1 InChI=1S/C13H10O2/c14-12-8-4-7-11(9-13(12)15)10-5-2-1-3-6-10/h1-9H,(H,14,15) MAAPIYPCXMEMAV-UHFFFAOYSA-N 50492541 CHEMBL2408242 Histone deacetylase 4 Homo sapiens 10860 ChEMBL 10.1021/ml400158k 10.7270/Q28055HS 24900743 Ononye, SN; VanHeyst, MD; Oblak, EZ; Zhou, W; Ammar, M; Anderson, AC; Wright, DL University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50492541 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50492541&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11019840 433959806 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197166 FC(F)(F)c1nc(no1)-c1cnc(NCc2cccnc2)nc1 InChI=1S/C13H9F3N6O/c14-13(15,16)11-21-10(22-23-11)9-6-19-12(20-7-9)18-5-8-2-1-3-17-4-8/h1-4,6-7H,5H2,(H,18,19,20) ALZUIFJAXCAFHL-UHFFFAOYSA-N 187220 US9670193, 10 N-(pyridin-3-ylmethyl)-5-(5-(trifluoromethyl)-1,2,4-oxadiazol-3-yl)pyrimidin-2-amine Histone deacetylase 4 Homo sapiens 140 ChEMBL 10.1021/ml4002216 10.7270/Q2280BJ9 24900734 Abdel-Magid, AF Therachem Research Medilab (India) Pvt. Ltd. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=187220 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=187220&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71577043 373987627 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197170 C[C@H](CN(C)Cc1ccccc1)NC(=O)c1ccc(nc1)-c1noc(n1)C(F)(F)F InChI=1S/C20H20F3N5O2/c1-13(11-28(2)12-14-6-4-3-5-7-14)25-18(29)15-8-9-16(24-10-15)17-26-19(30-27-17)20(21,22)23/h3-10,13H,11-12H2,1-2H3,(H,25,29)/t13-/m1/s1 LPCZNZVTHJYCCU-CYBMUJFWSA-N 187543 US9670193, 21 (R)—N-(1-(benzyl(methyl)amino)propan-2-yl)-6-(5-(trifluoromethyl)-1,2,4-oxadiazol-3-yl)nicotinamide Histone deacetylase 4 Homo sapiens 18 ChEMBL 10.1021/ml4002216 10.7270/Q2280BJ9 24900734 Abdel-Magid, AF Therachem Research Medilab (India) Pvt. Ltd. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=187543 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=187543&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 73356727 373987682 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51197172 CCN(CC)C[C@@H](C)NC(=O)c1ccc(nc1)-c1noc(n1)C(F)(F)F InChI=1S/C16H20F3N5O2/c1-4-24(5-2)9-10(3)21-14(25)11-6-7-12(20-8-11)13-22-15(26-23-13)16(17,18)19/h6-8,10H,4-5,9H2,1-3H3,(H,21,25)/t10-/m1/s1 VOSBDRADKHZBAZ-SNVBAGLBSA-N 187565 US9670193, 23 (R)—N-(1-(diethylamino)propan-2-yl)-6-(5-(trifluoromethyl)-1,2,4-oxadiazol-3-yl)nicotinamide Histone deacetylase 4 Homo sapiens 28 ChEMBL 10.1021/ml4002216 10.7270/Q2280BJ9 24900734 Abdel-Magid, AF Therachem Research Medilab (India) Pvt. Ltd. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=187565 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=187565&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 73347611 373987696 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51209103 CC[C@H](C)[C@H]1NC(=O)[C@H]2CSSCC\C=C\[C@H](CC(=O)N[C@H](CCSC)C(=O)N2)OC(=O)C[C@@H]1O InChI=1S/C23H37N3O6S3/c1-4-14(2)21-18(27)12-20(29)32-15-7-5-6-9-34-35-13-17(23(31)26-21)25-22(30)16(8-10-33-3)24-19(28)11-15/h5,7,14-18,21,27H,4,6,8-13H2,1-3H3,(H,24,28)(H,25,30)(H,26,31)/b7-5+/t14-,15+,16+,17+,18-,21+/m0/s1 VJXBYUITQBTTQM-DSRNDQRRSA-N 50354088 CHEMBL1836142 Histone deacetylase 4 Homo sapiens 37220 ChEMBL 10.1039/c2md20024d 10.7270/Q21G0Q7K 23997923 Wang, C; Flemming, CJ; Cheng, YQ University of Wisconsin-Milwaukee http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50354088 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50354088&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56602459 136360774 CHEMBL1836142 ZINC72125220 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51209110 CSCC[C@H]1NC(=O)C[C@@H]2OC(=O)C[C@H](O)[C@H](NC(=O)[C@@H](CSSCC\C=C\2)NC1=O)C(C)C InChI=1S/C22H35N3O6S3/c1-13(2)20-17(26)11-19(28)31-14-6-4-5-8-33-34-12-16(22(30)25-20)24-21(29)15(7-9-32-3)23-18(27)10-14/h4,6,13-17,20,26H,5,7-12H2,1-3H3,(H,23,27)(H,24,29)(H,25,30)/b6-4+/t14-,15-,16-,17+,20-/m1/s1 ZRJPMGCEOCZSQC-WMURJLHSSA-N 50449386 CHEMBL3126833 Histone deacetylase 4 Homo sapiens 38040 ChEMBL 10.1039/c2md20024d 10.7270/Q21G0Q7K 23997923 Wang, C; Flemming, CJ; Cheng, YQ University of Wisconsin-Milwaukee http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50449386 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50449386&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 76332759 194947282 CHEMBL3126833 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51209111 CCCC[C@H]1NC(=O)C[C@@H]2OC(=O)C[C@H](O)[C@H](NC(=O)[C@@H](CSSCC\C=C\2)NC1=O)C(C)C InChI=1S/C23H37N3O6S2/c1-4-5-9-16-22(30)25-17-13-34-33-10-7-6-8-15(11-19(28)24-16)32-20(29)12-18(27)21(14(2)3)26-23(17)31/h6,8,14-18,21,27H,4-5,7,9-13H2,1-3H3,(H,24,28)(H,25,30)(H,26,31)/b8-6+/t15-,16-,17-,18+,21-/m1/s1 DLMNFMQRIXCIAK-GFDPPHBOSA-N 50496770 CHEMBL3218562 Histone deacetylase 4 Homo sapiens 46970 ChEMBL 10.1039/c2md20024d 10.7270/Q21G0Q7K 23997923 Wang, C; Flemming, CJ; Cheng, YQ University of Wisconsin-Milwaukee http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50496770 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50496770&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90665809 433964035 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51209112 CCCC[C@H]1NC(=O)C[C@@H]2OC(=O)C[C@H](O)[C@@H](CC(C)C)NC(=O)[C@@H](CSSCC\C=C\2)NC1=O InChI=1S/C24H39N3O6S2/c1-4-5-9-17-23(31)27-19-14-35-34-10-7-6-8-16(12-21(29)25-17)33-22(30)13-20(28)18(11-15(2)3)26-24(19)32/h6,8,15-20,28H,4-5,7,9-14H2,1-3H3,(H,25,29)(H,26,32)(H,27,31)/b8-6+/t16-,17-,18-,19-,20+/m1/s1 BPYUUPVZXFNESA-HXDCCMETSA-N 50496769 CHEMBL3218564 Histone deacetylase 4 Homo sapiens 132500 ChEMBL 10.1039/c2md20024d 10.7270/Q21G0Q7K 23997923 Wang, C; Flemming, CJ; Cheng, YQ University of Wisconsin-Milwaukee http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50496769 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50496769&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90665811 433964034 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51209115 C\C=C1/NC(=O)[C@H]2CSSCC\C=C\[C@H](CC(=O)N[C@H](C(C)C)C(=O)N2)OC(=O)[C@@H](NC1=O)C(C)C InChI=1S/C24H36N4O6S2/c1-6-16-21(30)28-20(14(4)5)24(33)34-15-9-7-8-10-35-36-12-17(22(31)25-16)26-23(32)19(13(2)3)27-18(29)11-15/h6-7,9,13-15,17,19-20H,8,10-12H2,1-5H3,(H,25,31)(H,26,32)(H,27,29)(H,28,30)/b9-7+,16-6-/t15-,17-,19-,20+/m1/s1 OHRURASPPZQGQM-GCCNXGTGSA-N 19151 (1S,4S,7Z,10S,16E,21R)-7-ethylidene-4,21-bis(propan-2-yl)-2-oxa-12,13-dithia-5,8,20,23-tetraazabicyclo[8.7.6]tricos-16-ene-3,6,9,19,22-pentone::Antibiotic FR 901228::CHEMBL343448::Depsipeptide::FK228::Romidepsin Histone deacetylase 4 Homo sapiens 8670 ChEMBL 10.1039/c2md20024d 10.7270/Q21G0Q7K 23997923 Wang, C; Flemming, CJ; Cheng, YQ University of Wisconsin-Milwaukee http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19151 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19151&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5352062 46519185 61080 CHEMBL343448 7006 ZINC03935130 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51209119 CCCC[C@H]1NC(=O)C[C@@H]2OC(=O)C[C@H](O)[C@H](NC(=O)[C@@H](CSSCC\C=C\2)NC1=O)[C@@H](C)CC InChI=1S/C24H39N3O6S2/c1-4-6-10-17-23(31)26-18-14-35-34-11-8-7-9-16(12-20(29)25-17)33-21(30)13-19(28)22(15(3)5-2)27-24(18)32/h7,9,15-19,22,28H,4-6,8,10-14H2,1-3H3,(H,25,29)(H,26,31)(H,27,32)/b9-7+/t15-,16+,17+,18+,19-,22+/m0/s1 MUNWAZFRKGVMPQ-RIRJJDMNSA-N 50354084 CHEMBL1836145 Histone deacetylase 4 Homo sapiens 57440 ChEMBL 10.1039/c2md20024d 10.7270/Q21G0Q7K 23997923 Wang, C; Flemming, CJ; Cheng, YQ University of Wisconsin-Milwaukee http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50354084 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50354084&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56676500 136360770 CHEMBL1836145 ZINC72122972 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51209121 CSCC[C@H]1NC(=O)C[C@@H]2OC(=O)C[C@H](O)[C@@H](CC(C)C)NC(=O)[C@@H](CSSCC\C=C\2)NC1=O InChI=1S/C23H37N3O6S3/c1-14(2)10-17-19(27)12-21(29)32-15-6-4-5-8-34-35-13-18(23(31)25-17)26-22(30)16(7-9-33-3)24-20(28)11-15/h4,6,14-19,27H,5,7-13H2,1-3H3,(H,24,28)(H,25,31)(H,26,30)/b6-4+/t15-,16-,17-,18-,19+/m1/s1 IOHKAMWLDHLUSD-UNAVEXOGSA-N 50496768 CHEMBL3218563 Histone deacetylase 4 Homo sapiens 58880 ChEMBL 10.1039/c2md20024d 10.7270/Q21G0Q7K 23997923 Wang, C; Flemming, CJ; Cheng, YQ University of Wisconsin-Milwaukee http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50496768 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50496768&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90665810 433964033 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 850201 ONC(=O)c1cccc(Nc2nc3cc(Cl)c(Cl)cc3o2)c1 InChI=1S/C14H9Cl2N3O3/c15-9-5-11-12(6-10(9)16)22-14(18-11)17-8-3-1-2-7(4-8)13(20)19-21/h1-6,21H,(H,17,18)(H,19,20) OMJQMYFFOQKXJX-UHFFFAOYSA-N 421500 US10508088, Example 1-1::US10508088, ID HDTK010::US10538496, Compound 1-1 Histone deacetylase 4 Homo sapiens >10000 US Patent 10.7270/Q2280B04 aid1804007 US10508088 Lee, J; Barczak, N; Escobedo, JA; Conti, C; Han, B; Lancia, Jr., DR; Liu, C; Martin, MW; Ng, PY; Rudnitskaya, A; Thomason, JR; Zheng, X FORMA Therapeutics, Inc. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=421500 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=421500&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 134459974 434147362 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 850223 CC1(C)N(Cc2c1cccc2C(=O)NO)c1nc2ccc(cc2[nH]1)C(F)(F)F InChI=1S/C19H17F3N4O2/c1-18(2)13-5-3-4-11(16(27)25-28)12(13)9-26(18)17-23-14-7-6-10(19(20,21)22)8-15(14)24-17/h3-8,28H,9H2,1-2H3,(H,23,24)(H,25,27) ASSXNRYAUYXUGB-UHFFFAOYSA-N 50273553 CHEMBL4127020::US10508088, ID HDTK028::US11535607, Example 17-1 Histone deacetylase 4 Homo sapiens >10000 US Patent 10.7270/Q2280B04 aid1804007 US10508088 Lee, J; Barczak, N; Escobedo, JA; Conti, C; Han, B; Lancia, Jr., DR; Liu, C; Martin, MW; Ng, PY; Rudnitskaya, A; Thomason, JR; Zheng, X FORMA Therapeutics, Inc. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50273553 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50273553&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 134492521 405256618 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51251490 OC(=O)C(F)(F)F.CCCNNC(=O)\C=C\c1ccc(CNCCc2c(C)[nH]c3ccccc23)cc1 InChI=1S/C24H30N4O.C2HF3O2/c1-3-15-26-28-24(29)13-12-19-8-10-20(11-9-19)17-25-16-14-21-18(2)27-23-7-5-4-6-22(21)23;3-2(4,5)1(6)7/h4-13,25-27H,3,14-17H2,1-2H3,(H,28,29);(H,6,7)/b13-12+; YITSGXWXTPWSDD-UEIGIMKUSA-N 50511825 CHEMBL4444219 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.0c00442 10.7270/Q23X89Z5 32321249 Li, X; Jiang, Y; Peterson, YK; Xu, T; Himes, RA; Luo, X; Yin, G; Inks, ES; Dolloff, N; Halene, S; Chan, SSL; Chou, CJ Ocean University of China http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50511825 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50511825&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155517175 440720407 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51251570 Cc1[nH]c2ccccc2c1CCNCc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C21H23N3O2/c1-15-18(19-4-2-3-5-20(19)23-15)12-13-22-14-17-8-6-16(7-9-17)10-11-21(25)24-26/h2-11,22-23,26H,12-14H2,1H3,(H,24,25)/b11-10+ FPOHNWQLNRZRFC-ZHACJKMWSA-N 29589 Faridak::LBH-589::LBH-589B::Panobinostat::US10722597, Compound Panobinostat Histone deacetylase 4 Homo sapiens 203 ChEMBL 10.1021/acs.jmedchem.0c00442 10.7270/Q23X89Z5 32321249 Li, X; Jiang, Y; Peterson, YK; Xu, T; Himes, RA; Luo, X; Yin, G; Inks, ES; Dolloff, N; Halene, S; Chan, SSL; Chou, CJ Ocean University of China http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=29589 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=29589&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search LBH 5EF8 6918837 81055018 ZINC22010649 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51251586 Nc1ccccc1NC(=O)c1ccc(CNC(=O)OCc2cccnc2)cc1 InChI=1S/C21H20N4O3/c22-18-5-1-2-6-19(18)25-20(26)17-9-7-15(8-10-17)13-24-21(27)28-14-16-4-3-11-23-12-16/h1-12H,13-14,22H2,(H,24,27)(H,25,26) INVTYAOGFAGBOE-UHFFFAOYSA-N 19410 CHEMBL27759::MS-275::US11377423, MS-275::US11672788, Compound Entinostat::US9265734, MS-275::US9796664, Compound MS-275::benzamide-type inhibitor, 3::pyridin-3-ylmethyl N-({4-[(2-aminophenyl)carbamoyl]phenyl}methyl)carbamate Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.0c00442 10.7270/Q23X89Z5 32321249 Li, X; Jiang, Y; Peterson, YK; Xu, T; Himes, RA; Luo, X; Yin, G; Inks, ES; Dolloff, N; Halene, S; Chan, SSL; Chou, CJ Ocean University of China http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19410 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19410&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4261 46519433 CHEMBL27759 7007 ZINC01488870 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51263711 CN(Cc1nc(no1)C1CCN(Cc2ccc(C)cc2)CC1)c1ncc(cn1)C(=O)NO InChI=1S/C22H27N7O3/c1-15-3-5-16(6-4-15)13-29-9-7-17(8-10-29)20-25-19(32-27-20)14-28(2)22-23-11-18(12-24-22)21(30)26-31/h3-6,11-12,17,31H,7-10,13-14H2,1-2H3,(H,26,30) DSDPQMCYEOZWTA-UHFFFAOYSA-N 50516203 CHEMBL4517151 Histone deacetylase 4 Homo sapiens 473 ChEMBL 10.1016/j.ejmech.2019.05.089 10.7270/Q2HM5CTP 31177073 Yang, Z; Shen, M; Tang, M; Zhang, W; Cui, X; Zhang, Z; Pei, H; Li, Y; Hu, M; Bai, P; Chen, L Sichuan University and Collaborative Innovation Center of Biotherapy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50516203 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50516203&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 141764754 440724785 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51263722 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2019.05.089 10.7270/Q2HM5CTP 31177073 Yang, Z; Shen, M; Tang, M; Zhang, W; Cui, X; Zhang, Z; Pei, H; Li, Y; Hu, M; Bai, P; Chen, L Sichuan University and Collaborative Innovation Center of Biotherapy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51258812 Cc1[nH]c2ccccc2c1CCNCc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C21H23N3O2/c1-15-18(19-4-2-3-5-20(19)23-15)12-13-22-14-17-8-6-16(7-9-17)10-11-21(25)24-26/h2-11,22-23,26H,12-14H2,1H3,(H,24,25)/b11-10+ FPOHNWQLNRZRFC-ZHACJKMWSA-N 29589 Faridak::LBH-589::LBH-589B::Panobinostat::US10722597, Compound Panobinostat Histone deacetylase 4 Homo sapiens 10390 ChEMBL 10.1021/acs.jmedchem.9b01792 10.7270/Q21839VR 31855601 Zhang, SW; Gong, CJ; Su, MB; Chen, F; He, T; Zhang, YM; Shen, QQ; Su, Y; Ding, J; Li, J; Chen, Y; Nan, FJ Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=29589 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=29589&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search LBH 5EF8 6918837 81055018 ZINC22010649 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51258835 C[C@H](NC(=O)c1nc(sc1C1CC1)-c1ncc(s1)-c1ccccc1)c1ccc(cc1)C(=O)NO InChI=1S/C25H22N4O3S2/c1-14(15-7-11-18(12-8-15)22(30)29-32)27-23(31)20-21(17-9-10-17)34-25(28-20)24-26-13-19(33-24)16-5-3-2-4-6-16/h2-8,11-14,17,32H,9-10H2,1H3,(H,27,31)(H,29,30)/t14-/m0/s1 SELDFFFQCMDDJR-AWEZNQCLSA-N 50514463 CHEMBL4460552 Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.1021/acs.jmedchem.9b01792 10.7270/Q21839VR 31855601 Zhang, SW; Gong, CJ; Su, MB; Chen, F; He, T; Zhang, YM; Shen, QQ; Su, Y; Ding, J; Li, J; Chen, Y; Nan, FJ Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50514463 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50514463&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 139303146 440723045 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51257213 ONC(=O)c1cc(CCNC(=O)c2ccc(Cl)c(Cl)c2)on1 InChI=1S/C13H11Cl2N3O4/c14-9-2-1-7(5-10(9)15)12(19)16-4-3-8-6-11(18-22-8)13(20)17-21/h1-2,5-6,21H,3-4H2,(H,16,19)(H,17,20) JFGOILLZIAIYGA-UHFFFAOYSA-N 50513916 CHEMBL4469488 Histone deacetylase 4 Homo sapiens 19500 ChEMBL 10.1021/acs.jmedchem.9b00946 10.7270/Q2542RXH 31414801 Shen, S; Hadley, M; Ustinova, K; Pavlicek, J; Knox, T; Noonepalle, S; Tavares, MT; Zimprich, CA; Zhang, G; Robers, MB; Bařinka, C; Kozikowski, AP; Villagra, A University of Illinois at Chicago http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50513916 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50513916&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search JNN 6R0K 135348858 440722498 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51257214 ONC(=O)c1ccc(CNC(=O)c2ccc(Cl)c(Cl)c2)cc1 InChI=1S/C15H12Cl2N2O3/c16-12-6-5-11(7-13(12)17)14(20)18-8-9-1-3-10(4-2-9)15(21)19-22/h1-7,22H,8H2,(H,18,20)(H,19,21) ARSRPMMXCDOZIA-UHFFFAOYSA-N 50513915 CHEMBL4447715 Histone deacetylase 4 Homo sapiens 3530 ChEMBL 10.1021/acs.jmedchem.9b00946 10.7270/Q2542RXH 31414801 Shen, S; Hadley, M; Ustinova, K; Pavlicek, J; Knox, T; Noonepalle, S; Tavares, MT; Zimprich, CA; Zhang, G; Robers, MB; Bařinka, C; Kozikowski, AP; Villagra, A University of Illinois at Chicago http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50513915 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50513915&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155519254 440722497 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51257232 CCCCN(Cc1ccc(cc1)C(=O)NO)C(=O)Nc1ccccc1 InChI=1S/C19H23N3O3/c1-2-3-13-22(19(24)20-17-7-5-4-6-8-17)14-15-9-11-16(12-10-15)18(23)21-25/h4-12,25H,2-3,13-14H2,1H3,(H,20,24)(H,21,23) JZWXMCPARMXZQV-UHFFFAOYSA-N 50398716 CHEMBL2179618::US10227295, Compound 5g::US9409858, 5g::US9751832, Compound 5g::US9956192, Compound 5g Histone deacetylase 4 Homo sapiens 14800 ChEMBL 10.1021/acs.jmedchem.9b00946 10.7270/Q2542RXH 31414801 Shen, S; Hadley, M; Ustinova, K; Pavlicek, J; Knox, T; Noonepalle, S; Tavares, MT; Zimprich, CA; Zhang, G; Robers, MB; Bařinka, C; Kozikowski, AP; Villagra, A University of Illinois at Chicago http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50398716 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50398716&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N4R 5G0J,5G0I 71462653 163347740 CHEMBL2179618 ZINC95573398 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51223018 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acsmedchemlett.9b00084 10.7270/Q2DN489R 31413795 Liang, T; Hou, X; Zhou, Y; Yang, X; Fang, H Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51223019 ONC(=O)c1ccc(NC(=O)CCC2N(Cc3ccccc3)C(=O)N(C2=O)c2ccc(Cl)cc2)cc1 InChI=1S/C26H23ClN4O5/c27-19-8-12-21(13-9-19)31-25(34)22(30(26(31)35)16-17-4-2-1-3-5-17)14-15-23(32)28-20-10-6-18(7-11-20)24(33)29-36/h1-13,22,36H,14-16H2,(H,28,32)(H,29,33) DARFUQJSJROALF-UHFFFAOYSA-N 50502570 CHEMBL4450285 Histone deacetylase 4 Homo sapiens 27000 ChEMBL 10.1021/acsmedchemlett.9b00084 10.7270/Q2DN489R 31413795 Liang, T; Hou, X; Zhou, Y; Yang, X; Fang, H Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50502570 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50502570&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155521272 440711155 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51223020 Cc1ccc(CN2C(CCC(=O)Nc3ccc(cc3)C(=O)NO)C(=O)N(C2=O)c2ccc(Cl)cc2)cc1 InChI=1S/C27H25ClN4O5/c1-17-2-4-18(5-3-17)16-31-23(26(35)32(27(31)36)22-12-8-20(28)9-13-22)14-15-24(33)29-21-10-6-19(7-11-21)25(34)30-37/h2-13,23,37H,14-16H2,1H3,(H,29,33)(H,30,34) RSMGBZPONOKBDP-UHFFFAOYSA-N 50502571 CHEMBL4445862 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acsmedchemlett.9b00084 10.7270/Q2DN489R 31413795 Liang, T; Hou, X; Zhou, Y; Yang, X; Fang, H Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50502571 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50502571&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155518106 440711156 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51233325 Nc1ccccc1NC(=O)c1ccc(cc1)-c1cn(CCc2ccsc2)nn1 InChI=1S/C21H19N5OS/c22-18-3-1-2-4-19(18)23-21(27)17-7-5-16(6-8-17)20-13-26(25-24-20)11-9-15-10-12-28-14-15/h1-8,10,12-14H,9,11,22H2,(H,23,27) LBLSLSOENGWIHL-UHFFFAOYSA-N 50121210 CHEMBL3622374 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.9b00359 10.7270/Q2BR8WFX 31050421 Wu, G; Zhao, T; Kang, D; Zhang, J; Song, Y; Namasivayam, V; Kongsted, J; Pannecouque, C; De Clercq, E; Poongavanam, V; Liu, X; Zhan, P Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50121210 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50121210&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71721946 319566162 CHEMBL3622374 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51233350 Nc1ccccc1NC(=O)c1ccc(s1)-c1cn(CCc2cccc(c2)[N+]([O-])=O)nn1 InChI=1S/C21H18N6O3S/c22-16-6-1-2-7-17(16)23-21(28)20-9-8-19(31-20)18-13-26(25-24-18)11-10-14-4-3-5-15(12-14)27(29)30/h1-9,12-13H,10-11,22H2,(H,23,28) AXAUXMXVFLCQQK-UHFFFAOYSA-N 50121211 CHEMBL3622375 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.9b00359 10.7270/Q2BR8WFX 31050421 Wu, G; Zhao, T; Kang, D; Zhang, J; Song, Y; Namasivayam, V; Kongsted, J; Pannecouque, C; De Clercq, E; Poongavanam, V; Liu, X; Zhan, P Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50121211 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50121211&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71721558 319566163 CHEMBL3622375 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51223050 ONC(=O)c1ccc(NC(=O)CCC2N(Cc3ccc(Br)cc3)C(=O)N(C2=O)c2ccc(Cl)cc2)cc1 InChI=1S/C26H22BrClN4O5/c27-18-5-1-16(2-6-18)15-31-22(25(35)32(26(31)36)21-11-7-19(28)8-12-21)13-14-23(33)29-20-9-3-17(4-10-20)24(34)30-37/h1-12,22,37H,13-15H2,(H,29,33)(H,30,34) CDURLFYCCIFYGY-UHFFFAOYSA-N 50502572 CHEMBL4444176 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acsmedchemlett.9b00084 10.7270/Q2DN489R 31413795 Liang, T; Hou, X; Zhou, Y; Yang, X; Fang, H Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50502572 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50502572&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155517086 440711157 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51245668 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 113 ChEMBL 10.1021/acs.jmedchem.8b00189 10.7270/Q27H1NWV 30418766 Luan, Y; Li, J; Bernatchez, JA; Li, R Qingdao University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51245685 Cc1[nH]c2ccccc2c1CCNCc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C21H23N3O2/c1-15-18(19-4-2-3-5-20(19)23-15)12-13-22-14-17-8-6-16(7-9-17)10-11-21(25)24-26/h2-11,22-23,26H,12-14H2,1H3,(H,24,25)/b11-10+ FPOHNWQLNRZRFC-ZHACJKMWSA-N 29589 Faridak::LBH-589::LBH-589B::Panobinostat::US10722597, Compound Panobinostat Histone deacetylase 4 Homo sapiens 27 ChEMBL 10.1021/acs.jmedchem.8b00189 10.7270/Q27H1NWV 30418766 Luan, Y; Li, J; Bernatchez, JA; Li, R Qingdao University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=29589 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=29589&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search LBH 5EF8 6918837 81055018 ZINC22010649 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51245691 COc1ccc(cn1)-c1nc(N2CCOCC2)c2sc(CN(C)c3ncc(cn3)C(=O)NO)cc2n1 InChI=1S/C23H24N8O4S/c1-30(23-25-11-15(12-26-23)22(32)29-33)13-16-9-17-19(36-16)21(31-5-7-35-8-6-31)28-20(27-17)14-3-4-18(34-2)24-10-14/h3-4,9-12,33H,5-8,13H2,1-2H3,(H,29,32) JOWXJLIFIIOYMS-UHFFFAOYSA-N 50188961 CHEMBL3622533 Histone deacetylase 4 Homo sapiens 191 ChEMBL 10.1021/acs.jmedchem.8b00189 10.7270/Q27H1NWV 30418766 Luan, Y; Li, J; Bernatchez, JA; Li, R Qingdao University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50188961 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50188961&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 54575456 104072687 CHEMBL3622533 ZINC13444145 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51239618 ONC(=O)CCCCCN1C(=O)c2cccc3c(NCc4ccccc4)ccc(C1=O)c23 InChI=1S/C25H25N3O4/c29-22(27-32)12-5-2-6-15-28-24(30)19-11-7-10-18-21(14-13-20(23(18)19)25(28)31)26-16-17-8-3-1-4-9-17/h1,3-4,7-11,13-14,26,32H,2,5-6,12,15-16H2,(H,27,29) PFADLOXEKLDOIQ-UHFFFAOYSA-N 50507258 CHEMBL4532304 Histone deacetylase 4 Homo sapiens 5500 ChEMBL 10.1016/j.ejmech.2018.11.020 10.7270/Q2JQ14BB 30448419 Fleming, CL; Natoli, A; Schreuders, J; Devlin, M; Yoganantharajah, P; Gibert, Y; Leslie, KG; New, EJ; Ashton, TD; Pfeffer, FM Deakin University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50507258 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50507258&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155546558 440715843 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51239662 CCCNc1ccc2C(=O)N(CCCCCC(=O)NO)C(=O)c3cccc1c23 InChI=1S/C21H25N3O4/c1-2-12-22-17-11-10-16-19-14(17)7-6-8-15(19)20(26)24(21(16)27)13-5-3-4-9-18(25)23-28/h6-8,10-11,22,28H,2-5,9,12-13H2,1H3,(H,23,25) UODZPFZHXUXNPW-UHFFFAOYSA-N 50507257 CHEMBL4475116 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2018.11.020 10.7270/Q2JQ14BB 30448419 Fleming, CL; Natoli, A; Schreuders, J; Devlin, M; Yoganantharajah, P; Gibert, Y; Leslie, KG; New, EJ; Ashton, TD; Pfeffer, FM Deakin University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50507257 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50507257&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155537473 440715842 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51228014 COc1ccc(cn1)-c1cc(OCCN(C)c2ncc(cn2)C(=O)NO)c2ncnc(C)c2c1 InChI=1S/C23H23N7O4/c1-14-18-8-16(15-4-5-20(33-3)24-10-15)9-19(21(18)28-13-27-14)34-7-6-30(2)23-25-11-17(12-26-23)22(31)29-32/h4-5,8-13,32H,6-7H2,1-3H3,(H,29,31) GVPYBTYCSMGVJF-UHFFFAOYSA-N 50503947 CHEMBL4462577 Histone deacetylase 4 Homo sapiens 972 ChEMBL 10.1021/acs.jmedchem.9b00390 10.7270/Q2RF5Z80 31117517 Zhang, K; Lai, F; Lin, S; Ji, M; Zhang, J; Zhang, Y; Jin, J; Fu, R; Wu, D; Tian, H; Xue, N; Sheng, L; Zou, X; Li, Y; Chen, X; Xu, H TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503947 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503947&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155529247 440712532 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51228025 COc1ncc(cc1F)-c1cc(OCCCCCCC(=O)NO)c2ncnc(C)c2c1 InChI=1S/C22H25FN4O4/c1-14-17-9-15(16-10-18(23)22(30-2)24-12-16)11-19(21(17)26-13-25-14)31-8-6-4-3-5-7-20(28)27-29/h9-13,29H,3-8H2,1-2H3,(H,27,28) BQKQDMVFQZHPJZ-UHFFFAOYSA-N 50503943 CHEMBL4536105 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acs.jmedchem.9b00390 10.7270/Q2RF5Z80 31117517 Zhang, K; Lai, F; Lin, S; Ji, M; Zhang, J; Zhang, Y; Jin, J; Fu, R; Wu, D; Tian, H; Xue, N; Sheng, L; Zou, X; Li, Y; Chen, X; Xu, H TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503943 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503943&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 138454792 440712528 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51228045 COc1ccc(cn1)-c1nc(N2CCOCC2)c2sc(CN(C)c3ncc(cn3)C(=O)NO)cc2n1 InChI=1S/C23H24N8O4S/c1-30(23-25-11-15(12-26-23)22(32)29-33)13-16-9-17-19(36-16)21(31-5-7-35-8-6-31)28-20(27-17)14-3-4-18(34-2)24-10-14/h3-4,9-12,33H,5-8,13H2,1-2H3,(H,29,32) JOWXJLIFIIOYMS-UHFFFAOYSA-N 50188961 CHEMBL3622533 Histone deacetylase 4 Homo sapiens 445 ChEMBL 10.1021/acs.jmedchem.9b00390 10.7270/Q2RF5Z80 31117517 Zhang, K; Lai, F; Lin, S; Ji, M; Zhang, J; Zhang, Y; Jin, J; Fu, R; Wu, D; Tian, H; Xue, N; Sheng, L; Zou, X; Li, Y; Chen, X; Xu, H TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50188961 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50188961&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 54575456 104072687 CHEMBL3622533 ZINC13444145 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51244969 Cc1cc(C)cc(c1)C(=O)N(CCCCCC(=O)Nc1cc(ccc1N)-c1ccccc1)CC(=O)NCc1ccccc1 InChI=1S/C36H40N4O3/c1-26-20-27(2)22-31(21-26)36(43)40(25-35(42)38-24-28-12-6-3-7-13-28)19-11-5-10-16-34(41)39-33-23-30(17-18-32(33)37)29-14-8-4-9-15-29/h3-4,6-9,12-15,17-18,20-23H,5,10-11,16,19,24-25,37H2,1-2H3,(H,38,42)(H,39,41) ZZDRCLUTJPDPHV-UHFFFAOYSA-N 50509442 CHEMBL4564332 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.9b01489 10.7270/Q2JW8J5F 31762274 Krieger, V; Hamacher, A; Cao, F; Stenzel, K; Gertzen, CGW; Schäker-Hübner, L; Kurz, T; Gohlke, H; Dekker, FJ; Kassack, MU; Hansen, FK Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50509442 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50509442&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155559872 440718027 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51244994 Cc1cc(C)cc(c1)C(=O)N(CC(=O)NCc1ccccc1)Cc1ccc(cc1)C(=O)Nc1cc(ccc1N)-c1ccccc1 InChI=1S/C38H36N4O3/c1-26-19-27(2)21-33(20-26)38(45)42(25-36(43)40-23-28-9-5-3-6-10-28)24-29-13-15-31(16-14-29)37(44)41-35-22-32(17-18-34(35)39)30-11-7-4-8-12-30/h3-22H,23-25,39H2,1-2H3,(H,40,43)(H,41,44) WAFVXFIYLRQEBZ-UHFFFAOYSA-N 50509443 CHEMBL4587363 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.9b01489 10.7270/Q2JW8J5F 31762274 Krieger, V; Hamacher, A; Cao, F; Stenzel, K; Gertzen, CGW; Schäker-Hübner, L; Kurz, T; Gohlke, H; Dekker, FJ; Kassack, MU; Hansen, FK Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50509443 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50509443&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155566644 440718028 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51228064 CCCCN(Cc1ccc(cc1)C(=O)NO)C(=O)Nc1ccc(OCCCCCn2cc(CNc3cccc4C(=O)N(C5CCC(=O)NC5=O)C(=O)c34)nn2)cc1 InChI=1S/C40H45N9O8/c1-2-3-20-47(24-26-10-12-27(13-11-26)36(51)45-56)40(55)42-28-14-16-30(17-15-28)57-22-6-4-5-21-48-25-29(44-46-48)23-41-32-9-7-8-31-35(32)39(54)49(38(31)53)33-18-19-34(50)43-37(33)52/h7-17,25,33,41,56H,2-6,18-24H2,1H3,(H,42,55)(H,45,51)(H,43,50,52) DQGQXFRCIYCGOE-UHFFFAOYSA-N 50503977 CHEMBL4465902 Histone deacetylase 4 Homo sapiens >300 ChEMBL 10.1021/acs.jmedchem.9b00516 10.7270/Q2MP56H6 31271281 Wu, H; Yang, K; Zhang, Z; Leisten, ED; Li, Z; Xie, H; Liu, J; Smith, KA; Novakova, Z; Barinka, C; Tang, W Institute of Biotechnology of the Czech Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503977 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503977&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 150076000 440712562 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51245044 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 42200 ChEMBL 10.1021/acs.jmedchem.9b01489 10.7270/Q2JW8J5F 31762274 Krieger, V; Hamacher, A; Cao, F; Stenzel, K; Gertzen, CGW; Schäker-Hübner, L; Kurz, T; Gohlke, H; Dekker, FJ; Kassack, MU; Hansen, FK Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51245084 CN(C)c1ccc(cc1)C(=O)N(CC(=O)NCc1ccccc1)Cc1ccc(cc1)C(=O)Nc1ccccc1N InChI=1S/C32H33N5O3/c1-36(2)27-18-16-26(17-19-27)32(40)37(22-30(38)34-20-23-8-4-3-5-9-23)21-24-12-14-25(15-13-24)31(39)35-29-11-7-6-10-28(29)33/h3-19H,20-22,33H2,1-2H3,(H,34,38)(H,35,39) SIRNCVDOMIOFAK-UHFFFAOYSA-N 50509450 CHEMBL4474656 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.9b01489 10.7270/Q2JW8J5F 31762274 Krieger, V; Hamacher, A; Cao, F; Stenzel, K; Gertzen, CGW; Schäker-Hübner, L; Kurz, T; Gohlke, H; Dekker, FJ; Kassack, MU; Hansen, FK Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50509450 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50509450&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155537112 440718035 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51249869 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.9b02178 10.7270/Q27W6GHJ 32153186 Pan, Z; Li, X; Wang, Y; Jiang, Q; Jiang, L; Zhang, M; Zhang, N; Wu, F; Liu, B; He, G Sichuan University and Collaborative Innovation Center of Biotherapy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51249942 CN1CCc2c(C1)sc1nc([nH]c(=O)c21)-c1cc(C)c(OCCCCCC(=O)NO)c(C)c1 InChI=1S/C24H30N4O4S/c1-14-11-16(12-15(2)21(14)32-10-6-4-5-7-19(29)27-31)22-25-23(30)20-17-8-9-28(3)13-18(17)33-24(20)26-22/h11-12,31H,4-10,13H2,1-3H3,(H,27,29)(H,25,26,30) BBFKONWWIAFKEJ-UHFFFAOYSA-N 50511231 CHEMBL4514808 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.9b02178 10.7270/Q27W6GHJ 32153186 Pan, Z; Li, X; Wang, Y; Jiang, Q; Jiang, L; Zhang, M; Zhang, N; Wu, F; Liu, B; He, G Sichuan University and Collaborative Innovation Center of Biotherapy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50511231 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50511231&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 153534005 440719813 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51251084 CC(C)C[C@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)c1ccc(cc1)C(=O)Nc1ccccc1N)B1O[C@@H]2[C@@H]3C[C@H](C[C@]2(C)O1)C3(C)C InChI=1S/C38H47BN4O5/c1-23(2)19-32(39-47-33-28-21-27(37(28,3)4)22-38(33,5)48-39)43-36(46)31(20-24-11-7-6-8-12-24)42-35(45)26-17-15-25(16-18-26)34(44)41-30-14-10-9-13-29(30)40/h6-18,23,27-28,31-33H,19-22,40H2,1-5H3,(H,41,44)(H,42,45)(H,43,46)/t27-,28+,31+,32+,33-,38+/m1/s1 CADXOGZMLIVVAM-HGHHWUKJSA-N 50511593 CHEMBL4456886 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.9b02161 10.7270/Q2J67M8B 32267687 Zhou, Y; Liu, X; Xue, J; Liu, L; Liang, T; Li, W; Yang, X; Hou, X; Fang, H Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50511593 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50511593&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155525782 440720175 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51251085 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 74000 ChEMBL 10.1021/acs.jmedchem.9b02161 10.7270/Q2J67M8B 32267687 Zhou, Y; Liu, X; Xue, J; Liu, L; Liang, T; Li, W; Yang, X; Hou, X; Fang, H Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51251105 CC(C)C[C@H](NC(=O)CNC(=O)c1cccc(\C=C\C(=O)NO)c1)B1O[C@@H]2[C@@H]3C[C@H](C[C@]2(C)O1)C3(C)C InChI=1S/C27H38BN3O6/c1-16(2)11-21(28-36-24-20-13-19(26(20,3)4)14-27(24,5)37-28)30-23(33)15-29-25(34)18-8-6-7-17(12-18)9-10-22(32)31-35/h6-10,12,16,19-21,24,35H,11,13-15H2,1-5H3,(H,29,34)(H,30,33)(H,31,32)/b10-9+/t19-,20+,21+,24-,27+/m1/s1 WAKGJPYDEKJAKC-PAUPOJMRSA-N 50511599 CHEMBL4576202 Histone deacetylase 4 Homo sapiens 11100 ChEMBL 10.1021/acs.jmedchem.9b02161 10.7270/Q2J67M8B 32267687 Zhou, Y; Liu, X; Xue, J; Liu, L; Liang, T; Li, W; Yang, X; Hou, X; Fang, H Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50511599 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50511599&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155552130 440720181 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51238159 ONC(=O)\C=C\c1ccc(NC(=O)Cc2cccc3ccccc23)cn1 InChI=1S/C20H17N3O3/c24-19(23-26)11-10-16-8-9-17(13-21-16)22-20(25)12-15-6-3-5-14-4-1-2-7-18(14)15/h1-11,13,26H,12H2,(H,22,25)(H,23,24)/b11-10+ DTNVLAIWDVXDJR-ZHACJKMWSA-N 50506780 CHEMBL4550522 Histone deacetylase 4 Homo sapiens 2700 ChEMBL 10.1016/j.ejmech.2018.10.041 10.7270/Q21V5J76 30366254 Bouchut, A; Rotili, D; Pierrot, C; Valente, S; Lafitte, S; Schultz, J; Hoglund, U; Mazzone, R; Lucidi, A; Fabrizi, G; Pechalrieu, D; Arimondo, PB; Skinner-Adams, TS; Chua, MJ; Andrews, KT; Mai, A; Khalife, J Universit£ de Lille http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50506780 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50506780&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155555345 440715365 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51238160 ONC(=O)CCCCCSc1nc(cc(=O)[nH]1)-c1ccc(cc1)-c1ccccc1 InChI=1S/C22H23N3O3S/c26-20(25-28)9-5-2-6-14-29-22-23-19(15-21(27)24-22)18-12-10-17(11-13-18)16-7-3-1-4-8-16/h1,3-4,7-8,10-13,15,28H,2,5-6,9,14H2,(H,25,26)(H,23,24,27) KGFPPHGIBSDRGO-UHFFFAOYSA-N 50506775 CHEMBL4593437 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2018.10.041 10.7270/Q21V5J76 30366254 Bouchut, A; Rotili, D; Pierrot, C; Valente, S; Lafitte, S; Schultz, J; Hoglund, U; Mazzone, R; Lucidi, A; Fabrizi, G; Pechalrieu, D; Arimondo, PB; Skinner-Adams, TS; Chua, MJ; Andrews, KT; Mai, A; Khalife, J Universit£ de Lille http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50506775 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50506775&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 136173094 440715360 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51238161 ONC(=O)c1ccc(NC(=O)Cc2ccccc2)cn1 InChI=1S/C14H13N3O3/c18-13(8-10-4-2-1-3-5-10)16-11-6-7-12(15-9-11)14(19)17-20/h1-7,9,20H,8H2,(H,16,18)(H,17,19) KHCGDOSZEMWAGW-UHFFFAOYSA-N 50506781 CHEMBL4435005 Histone deacetylase 4 Homo sapiens 11000 ChEMBL 10.1016/j.ejmech.2018.10.041 10.7270/Q21V5J76 30366254 Bouchut, A; Rotili, D; Pierrot, C; Valente, S; Lafitte, S; Schultz, J; Hoglund, U; Mazzone, R; Lucidi, A; Fabrizi, G; Pechalrieu, D; Arimondo, PB; Skinner-Adams, TS; Chua, MJ; Andrews, KT; Mai, A; Khalife, J Universit£ de Lille http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50506781 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50506781&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155510915 440715366 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51238162 FC(F)(F)c1nc(no1)-c1cccc(c1)C(=O)NCC1(CCOCC1)c1nc(cs1)-c1ccccc1 InChI=1S/C25H21F3N4O3S/c26-25(27,28)22-31-20(32-35-22)17-7-4-8-18(13-17)21(33)29-15-24(9-11-34-12-10-24)23-30-19(14-36-23)16-5-2-1-3-6-16/h1-8,13-14H,9-12,15H2,(H,29,33) HORXBWNTEDOVKN-UHFFFAOYSA-N 50446481 CHEMBL3110004::US10011611, TMP269::US10722597, Compound TMP-269 Histone deacetylase 4 Homo sapiens 300 ChEMBL 10.1016/j.ejmech.2018.10.041 10.7270/Q21V5J76 30366254 Bouchut, A; Rotili, D; Pierrot, C; Valente, S; Lafitte, S; Schultz, J; Hoglund, U; Mazzone, R; Lucidi, A; Fabrizi, G; Pechalrieu, D; Arimondo, PB; Skinner-Adams, TS; Chua, MJ; Andrews, KT; Mai, A; Khalife, J Universit£ de Lille http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446481 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446481&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search NU9 3ZNR 53344908 194944377 CHEMBL3110004 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51238179 ONC(=O)CCCCCSc1nc(cc(=O)[nH]1)-c1ccc2ccccc2c1 InChI=1S/C20H21N3O3S/c24-18(23-26)8-2-1-5-11-27-20-21-17(13-19(25)22-20)16-10-9-14-6-3-4-7-15(14)12-16/h3-4,6-7,9-10,12-13,26H,1-2,5,8,11H2,(H,23,24)(H,21,22,25) IQFOLJQYULLTTM-UHFFFAOYSA-N 50506778 CHEMBL4469596 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2018.10.041 10.7270/Q21V5J76 30366254 Bouchut, A; Rotili, D; Pierrot, C; Valente, S; Lafitte, S; Schultz, J; Hoglund, U; Mazzone, R; Lucidi, A; Fabrizi, G; Pechalrieu, D; Arimondo, PB; Skinner-Adams, TS; Chua, MJ; Andrews, KT; Mai, A; Khalife, J Universit£ de Lille http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50506778 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50506778&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155534005 440715363 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51238183 C[C@H](\C=C(/C)\C=C\C(=O)NO)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1 RTKIYFITIVXBLE-QEQCGCAPSA-N 50005711 CHEBI:46024::GNF-Pf-1011::TRICHOSTATIN::Trichostatin A::Trichostatin A (TSA)::US10011611, Trichostatin A::US10722597, Compound Trichostatin::US11535598, Compound Trichostatin A::US9265734, TSA Histone deacetylase 4 Homo sapiens 3800 ChEMBL 10.1016/j.ejmech.2018.10.041 10.7270/Q21V5J76 30366254 Bouchut, A; Rotili, D; Pierrot, C; Valente, S; Lafitte, S; Schultz, J; Hoglund, U; Mazzone, R; Lucidi, A; Fabrizi, G; Pechalrieu, D; Arimondo, PB; Skinner-Adams, TS; Chua, MJ; Andrews, KT; Mai, A; Khalife, J Universit£ de Lille http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 444732 242056952 DB04297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51238185 ONC(=O)c1ccc(NC(=O)Cc2cccc3ccccc23)cn1 InChI=1S/C18H15N3O3/c22-17(20-14-8-9-16(19-11-14)18(23)21-24)10-13-6-3-5-12-4-1-2-7-15(12)13/h1-9,11,24H,10H2,(H,20,22)(H,21,23) JLCBQKQIFFSMTN-UHFFFAOYSA-N 50506779 CHEMBL4521590 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2018.10.041 10.7270/Q21V5J76 30366254 Bouchut, A; Rotili, D; Pierrot, C; Valente, S; Lafitte, S; Schultz, J; Hoglund, U; Mazzone, R; Lucidi, A; Fabrizi, G; Pechalrieu, D; Arimondo, PB; Skinner-Adams, TS; Chua, MJ; Andrews, KT; Mai, A; Khalife, J Universit£ de Lille http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50506779 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50506779&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155542755 440715364 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51238191 ONC(=O)CCCCSc1nc(cc(=O)[nH]1)-c1ccc2ccccc2c1 InChI=1S/C19H19N3O3S/c23-17(22-25)7-3-4-10-26-19-20-16(12-18(24)21-19)15-9-8-13-5-1-2-6-14(13)11-15/h1-2,5-6,8-9,11-12,25H,3-4,7,10H2,(H,22,23)(H,20,21,24) TVGKKFWZZRSYCE-UHFFFAOYSA-N 50506777 CHEMBL4476057 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2018.10.041 10.7270/Q21V5J76 30366254 Bouchut, A; Rotili, D; Pierrot, C; Valente, S; Lafitte, S; Schultz, J; Hoglund, U; Mazzone, R; Lucidi, A; Fabrizi, G; Pechalrieu, D; Arimondo, PB; Skinner-Adams, TS; Chua, MJ; Andrews, KT; Mai, A; Khalife, J Universit£ de Lille http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50506777 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50506777&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155538087 440715362 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226536 ONC(=O)C(c1ccc(cc1)-c1cnccn1)c1ccccc1F InChI=1S/C18H14FN3O2/c19-15-4-2-1-3-14(15)17(18(23)22-24)13-7-5-12(6-8-13)16-11-20-9-10-21-16/h1-11,17,24H,(H,22,23) XNKNHMFYODNSOB-UHFFFAOYSA-N 50503689 CHEMBL4577004 Histone deacetylase 4 Homo sapiens 40 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503689 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503689&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155554004 440712274 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226539 Cc1cnc(nc1)-c1ccc(cc1)C(C(=O)NO)c1ccccc1F InChI=1S/C19H16FN3O2/c1-12-10-21-18(22-11-12)14-8-6-13(7-9-14)17(19(24)23-25)15-4-2-3-5-16(15)20/h2-11,17,25H,1H3,(H,23,24) XRYDRNDHGYJSIH-UHFFFAOYSA-N 50503691 CHEMBL4533107 Histone deacetylase 4 Homo sapiens 17 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503691 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503691&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118681924 440712276 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226544 ONC(=O)C(c1ccc(cc1)-c1ncc(cn1)C(F)(F)F)c1ccccc1F InChI=1S/C19H13F4N3O2/c20-15-4-2-1-3-14(15)16(18(27)26-28)11-5-7-12(8-6-11)17-24-9-13(10-25-17)19(21,22)23/h1-10,16,28H,(H,26,27) LMGDHGQJJLEAPQ-UHFFFAOYSA-N 50503690 CHEMBL4456445 Histone deacetylase 4 Homo sapiens 112 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503690 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503690&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 81689842 440712275 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226560 ONC(=O)C(c1ccc(cc1)-c1ncc(cn1)C(F)(F)F)c1ccccc1F InChI=1S/C19H13F4N3O2/c20-15-4-2-1-3-14(15)16(18(27)26-28)11-5-7-12(8-6-11)17-24-9-13(10-25-17)19(21,22)23/h1-10,16,28H,(H,26,27) LMGDHGQJJLEAPQ-UHFFFAOYSA-N 50503690 CHEMBL4456445 Histone deacetylase 4 Homo sapiens 54 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503690 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503690&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 81689842 440712275 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226561 ONC(=O)C(c1ccc(cc1)-c1ncccn1)c1ccccc1F InChI=1S/C18H14FN3O2/c19-15-5-2-1-4-14(15)16(18(23)22-24)12-6-8-13(9-7-12)17-20-10-3-11-21-17/h1-11,16,24H,(H,22,23) YSZMJCICKWAAGT-UHFFFAOYSA-N 50503693 CHEMBL4581271 Histone deacetylase 4 Homo sapiens 25 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503693 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503693&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155561731 440712278 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226562 Cc1ncncc1-c1ccc(cc1)C(C(=O)NO)c1ccccc1F InChI=1S/C19H16FN3O2/c1-12-16(10-21-11-22-12)13-6-8-14(9-7-13)18(19(24)23-25)15-4-2-3-5-17(15)20/h2-11,18,25H,1H3,(H,23,24) FWBWKCSAAOHVRU-UHFFFAOYSA-N 50503694 CHEMBL4572214 Histone deacetylase 4 Homo sapiens 49 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503694 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503694&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155563135 440712279 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226563 ONC(=O)C(c1ccc(cc1)-c1cncnc1)c1ccccc1F InChI=1S/C18H14FN3O2/c19-16-4-2-1-3-15(16)17(18(23)22-24)13-7-5-12(6-8-13)14-9-20-11-21-10-14/h1-11,17,24H,(H,22,23) INVRWIZGQPIKEM-UHFFFAOYSA-N 50503695 CHEMBL4558414 Histone deacetylase 4 Homo sapiens 57 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503695 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503695&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155557724 440712280 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226564 ONC(=O)C(c1ccc(cc1)-c1cnco1)c1ccccc1F InChI=1S/C17H13FN2O3/c18-14-4-2-1-3-13(14)16(17(21)20-22)12-7-5-11(6-8-12)15-9-19-10-23-15/h1-10,16,22H,(H,20,21) ZGKWDJXPFDUIKR-UHFFFAOYSA-N 50503696 CHEMBL4546422 Histone deacetylase 4 Homo sapiens 25 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503696 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503696&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155552531 440712281 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226565 ONC(=O)C(c1ccc(cc1)-c1ccnnc1)c1ccccc1F InChI=1S/C18H14FN3O2/c19-16-4-2-1-3-15(16)17(18(23)22-24)13-7-5-12(6-8-13)14-9-10-20-21-11-14/h1-11,17,24H,(H,22,23) BIXITDNUBODVDA-UHFFFAOYSA-N 50503697 CHEMBL4438812 Histone deacetylase 4 Homo sapiens 31 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503697 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503697&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155513435 440712282 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226566 ONC(=O)C(c1ccc(cc1)-c1cccnn1)c1ccccc1F InChI=1S/C18H14FN3O2/c19-15-5-2-1-4-14(15)17(18(23)22-24)13-9-7-12(8-10-13)16-6-3-11-20-21-16/h1-11,17,24H,(H,22,23) HLCWFJFIXVBAMD-UHFFFAOYSA-N 50503698 CHEMBL4447877 Histone deacetylase 4 Homo sapiens 33 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503698 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503698&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155519955 440712283 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226567 ONC(=O)C(c1ccc(NS(=O)(=O)c2ccccc2)cc1)c1ccccc1F InChI=1S/C20H17FN2O4S/c21-18-9-5-4-8-17(18)19(20(24)22-25)14-10-12-15(13-11-14)23-28(26,27)16-6-2-1-3-7-16/h1-13,19,23,25H,(H,22,24) UWWUDJZGZJLYJJ-UHFFFAOYSA-N 50503699 CHEMBL4461062 Histone deacetylase 4 Homo sapiens 22 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503699 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503699&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155528228 440712284 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226571 ONC(=O)C1c2ccccc2-c2ccccc12 InChI=1S/C14H11NO2/c16-14(15-17)13-11-7-3-1-5-9(11)10-6-2-4-8-12(10)13/h1-8,13,17H,(H,15,16) LEYJMVDNPXDXSO-UHFFFAOYSA-N 50446482 CHEMBL3110003 Histone deacetylase 4 Homo sapiens 330 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446482 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446482&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 54030066 194944378 CHEMBL3110003 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226572 ONC(=O)C(c1ccc(cc1)-c1nccc(n1)C(F)(F)F)c1ccccc1F InChI=1S/C19H13F4N3O2/c20-14-4-2-1-3-13(14)16(18(27)26-28)11-5-7-12(8-6-11)17-24-10-9-15(25-17)19(21,22)23/h1-10,16,28H,(H,26,27) ZYHYJFQONYHPBX-UHFFFAOYSA-N 50503700 CHEMBL4469204 Histone deacetylase 4 Homo sapiens 119 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503700 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503700&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155533604 440712285 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226573 Cc1ncc(cn1)-c1ccc(cc1)C(C(=O)NO)c1ccccc1F InChI=1S/C19H16FN3O2/c1-12-21-10-15(11-22-12)13-6-8-14(9-7-13)18(19(24)23-25)16-4-2-3-5-17(16)20/h2-11,18,25H,1H3,(H,23,24) SFXMVIQZYOMYOF-UHFFFAOYSA-N 50503692 CHEMBL4437833 Histone deacetylase 4 Homo sapiens 36 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503692 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503692&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search EBE 6FYZ 86302836 440712277 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226574 ONC(=O)C(c1ccc(cc1)-c1ccncn1)c1ccccc1F InChI=1S/C18H14FN3O2/c19-15-4-2-1-3-14(15)17(18(23)22-24)13-7-5-12(6-8-13)16-9-10-20-11-21-16/h1-11,17,24H,(H,22,23) ADGLKPIWGPUPAW-UHFFFAOYSA-N 50503701 CHEMBL4457713 Histone deacetylase 4 Homo sapiens 22 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503701 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503701&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155525509 440712286 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226575 ONC(=O)C(c1ccc(cc1)-c1ccncc1)c1ccccc1F InChI=1S/C19H15FN2O2/c20-17-4-2-1-3-16(17)18(19(23)22-24)15-7-5-13(6-8-15)14-9-11-21-12-10-14/h1-12,18,24H,(H,22,23) QRPYNZCZDKZUNW-UHFFFAOYSA-N 50503702 CHEMBL4452941 Histone deacetylase 4 Homo sapiens 103 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503702 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503702&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155523278 440712287 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226580 Cn1ccnc1-c1ccc(cc1)C(C(=O)NO)c1ccccc1F InChI=1S/C18H16FN3O2/c1-22-11-10-20-17(22)13-8-6-12(7-9-13)16(18(23)21-24)14-4-2-3-5-15(14)19/h2-11,16,24H,1H3,(H,21,23) OGZUTLOAJZJYEZ-UHFFFAOYSA-N 50503703 CHEMBL4535902 Histone deacetylase 4 Homo sapiens 30 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503703 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503703&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155547936 440712288 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226581 ONC(=O)C(c1ccc(cc1)-c1cncs1)c1ccccc1F InChI=1S/C17H13FN2O2S/c18-14-4-2-1-3-13(14)16(17(21)20-22)12-7-5-11(6-8-12)15-9-19-10-23-15/h1-10,16,22H,(H,20,21) VTFWSYNPGGAWQB-UHFFFAOYSA-N 50503704 CHEMBL4472392 Histone deacetylase 4 Homo sapiens 22 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503704 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503704&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155535427 440712289 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226585 ONC(=O)C(c1ccc(cc1)-c1cnc(nc1)C1CC1)c1ccccc1F InChI=1S/C21H18FN3O2/c22-18-4-2-1-3-17(18)19(21(26)25-27)14-7-5-13(6-8-14)16-11-23-20(24-12-16)15-9-10-15/h1-8,11-12,15,19,27H,9-10H2,(H,25,26) PNPXZSIZLIBULX-UHFFFAOYSA-N 50503705 CHEMBL4531880 Histone deacetylase 4 Homo sapiens 55 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503705 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503705&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155546580 440712290 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226586 ONC(=O)C(c1ccccc1)c1ccccc1 InChI=1S/C14H13NO2/c16-14(15-17)13(11-7-3-1-4-8-11)12-9-5-2-6-10-12/h1-10,13,17H,(H,15,16) OFSBBVCLWMCGNY-UHFFFAOYSA-N 50207561 CHEMBL396097::Class IIa HDAC inhibitor, Compound 6::N-hydroxy-2,2-diphenylacetamide Histone deacetylase 4 Homo sapiens 250 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50207561 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50207561&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 239512 104084972 CHEMBL396097 ZINC04522248 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226588 Cc1ncc(cn1)-c1ccc(cc1)C(C(=O)NO)c1ccccc1F InChI=1S/C19H16FN3O2/c1-12-21-10-15(11-22-12)13-6-8-14(9-7-13)18(19(24)23-25)16-4-2-3-5-17(16)20/h2-11,18,25H,1H3,(H,23,24) SFXMVIQZYOMYOF-UHFFFAOYSA-N 50503692 CHEMBL4437833 Histone deacetylase 4 Homo sapiens 80 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503692 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503692&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search EBE 6FYZ 86302836 440712277 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51226589 ONC(=O)C(c1ccc(cc1)-c1ncc(F)cn1)c1ccccc1F InChI=1S/C18H13F2N3O2/c19-13-9-21-17(22-10-13)12-7-5-11(6-8-12)16(18(24)23-25)14-3-1-2-4-15(14)20/h1-10,16,25H,(H,23,24) CQFFHVHAWUZJLV-UHFFFAOYSA-N 50503706 CHEMBL4454327 Histone deacetylase 4 Homo sapiens 25 ChEMBL 10.1016/j.bmcl.2018.11.009 10.7270/Q2G44TJZ 30463802 Luckhurst, CA; Aziz, O; Beaumont, V; Bürli, RW; Breccia, P; Maillard, MC; Haughan, AF; Lamers, M; Leonard, P; Matthews, KL; Raphy, G; Stott, AJ; Munoz-Sanjuan, I; Thomas, B; Wall, M; Wishart, G; Yates, D; Dominguez, C Charles River Discovery (previously BioFocus) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503706 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503706&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155523903 440712291 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51266398 CN1CCC(CNC(=O)c2cccc(c2)C(=O)NO)(CC1)c1nc(cs1)-c1ccccc1 InChI=1S/C24H26N4O3S/c1-28-12-10-24(11-13-28,23-26-20(15-32-23)17-6-3-2-4-7-17)16-25-21(29)18-8-5-9-19(14-18)22(30)27-31/h2-9,14-15,31H,10-13,16H2,1H3,(H,25,29)(H,27,30) KVCVQVLJDBCJRE-UHFFFAOYSA-N 50517219 CHEMBL4456269 Histone deacetylase 4 Homo sapiens 23800 ChEMBL 10.1016/j.bmc.2019.115087 10.7270/Q2VM4GMZ 31561937 Asfaha, Y; Schrenk, C; Alves Avelar, LA; Hamacher, A; Pflieger, M; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50517219 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50517219&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 70789579 440725801 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51266401 CN1CCC(CNC(=O)c2cccc(c2)-c2noc(n2)C(F)(F)F)(CC1)c1nc(cs1)-c1ccccc1 InChI=1S/C26H24F3N5O2S/c1-34-12-10-25(11-13-34,24-31-20(15-37-24)17-6-3-2-4-7-17)16-30-22(35)19-9-5-8-18(14-19)21-32-23(36-33-21)26(27,28)29/h2-9,14-15H,10-13,16H2,1H3,(H,30,35) BQFISAUAZNJOEG-UHFFFAOYSA-N 50517218 CHEMBL4525406 Histone deacetylase 4 Homo sapiens 75 ChEMBL 10.1016/j.bmc.2019.115087 10.7270/Q2VM4GMZ 31561937 Asfaha, Y; Schrenk, C; Alves Avelar, LA; Hamacher, A; Pflieger, M; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50517218 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50517218&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search NU7 3ZNS 69950064 440725800 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51266412 CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(cc1)C(=O)NC(CCP(O)(O)=O)P(O)(O)=O InChI=1S/C18H24N8O7P2/c1-26(9-11-8-21-16-14(22-11)15(19)24-18(20)25-16)12-4-2-10(3-5-12)17(27)23-13(35(31,32)33)6-7-34(28,29)30/h2-5,8,13H,6-7,9H2,1H3,(H,23,27)(H2,28,29,30)(H2,31,32,33)(H4,19,20,21,24,25) IYHDGYOJXJQQRF-UHFFFAOYSA-N 50517220 CHEMBL4576281 Histone deacetylase 4 Homo sapiens 4160 ChEMBL 10.1016/j.bmc.2019.115087 10.7270/Q2VM4GMZ 31561937 Asfaha, Y; Schrenk, C; Alves Avelar, LA; Hamacher, A; Pflieger, M; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50517220 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50517220&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 338818 440725802 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51266415 CN(Cc1cnc2nc(N)nc(N)c2n1)c1ccc(cc1)C(=O)NC(CCP(O)(O)=O)P(O)(O)=O InChI=1S/C18H24N8O7P2/c1-26(9-11-8-21-16-14(22-11)15(19)24-18(20)25-16)12-4-2-10(3-5-12)17(27)23-13(35(31,32)33)6-7-34(28,29)30/h2-5,8,13H,6-7,9H2,1H3,(H,23,27)(H2,28,29,30)(H2,31,32,33)(H4,19,20,21,24,25) IYHDGYOJXJQQRF-UHFFFAOYSA-N 50517220 CHEMBL4576281 Histone deacetylase 4 Homo sapiens >40000 ChEMBL 10.1016/j.bmc.2019.115087 10.7270/Q2VM4GMZ 31561937 Asfaha, Y; Schrenk, C; Alves Avelar, LA; Hamacher, A; Pflieger, M; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50517220 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50517220&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 338818 440725802 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51271968 Cn1cc(CNCC2CCN(CC2)c2ncc(cn2)C(=O)NO)c2ccccc12 InChI=1S/C21H26N6O2/c1-26-14-17(18-4-2-3-5-19(18)26)11-22-10-15-6-8-27(9-7-15)21-23-12-16(13-24-21)20(28)25-29/h2-5,12-15,22,29H,6-11H2,1H3,(H,25,28) PAWIYAYFNXQGAP-UHFFFAOYSA-N 50105327 JNJ-26481585::Quisinostat Histone deacetylase 4 Homo sapiens 4.6 ChEMBL 10.1021/acsmedchemlett.9b00471 10.7270/Q26976Z8 31938464 Shouksmith, AE; Gawel, JM; Nawar, N; Sina, D; Raouf, YS; Bukhari, S; He, L; Johns, AE; Manaswiyoungkul, P; Olaoye, OO; Cabral, AD; Sedighi, A; de Araujo, ED; Gunning, PT University of Toronto Mississauga http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105327 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105327&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search GOK 7Q1B,6HSK,6HSH 11538455 318590494 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51272005 CC(C)(C)c1ccc(cc1)C(=O)Nc1ccc(cc1)C(=O)NO InChI=1S/C18H20N2O3/c1-18(2,3)14-8-4-12(5-9-14)16(21)19-15-10-6-13(7-11-15)17(22)20-23/h4-11,23H,1-3H3,(H,19,21)(H,20,22) FMOQHLZNJFXULZ-UHFFFAOYSA-N 50519457 CHEMBL4452620 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acsmedchemlett.9b00471 10.7270/Q26976Z8 31938464 Shouksmith, AE; Gawel, JM; Nawar, N; Sina, D; Raouf, YS; Bukhari, S; He, L; Johns, AE; Manaswiyoungkul, P; Olaoye, OO; Cabral, AD; Sedighi, A; de Araujo, ED; Gunning, PT University of Toronto Mississauga http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50519457 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50519457&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11688197 440728039 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51272006 Nc1ccccc1NC(=O)c1ccc(CNC(=O)OCc2cccnc2)cc1 InChI=1S/C21H20N4O3/c22-18-5-1-2-6-19(18)25-20(26)17-9-7-15(8-10-17)13-24-21(27)28-14-16-4-3-11-23-12-16/h1-12H,13-14,22H2,(H,24,27)(H,25,26) INVTYAOGFAGBOE-UHFFFAOYSA-N 19410 CHEMBL27759::MS-275::US11377423, MS-275::US11672788, Compound Entinostat::US9265734, MS-275::US9796664, Compound MS-275::benzamide-type inhibitor, 3::pyridin-3-ylmethyl N-({4-[(2-aminophenyl)carbamoyl]phenyl}methyl)carbamate Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acsmedchemlett.9b00471 10.7270/Q26976Z8 31938464 Shouksmith, AE; Gawel, JM; Nawar, N; Sina, D; Raouf, YS; Bukhari, S; He, L; Johns, AE; Manaswiyoungkul, P; Olaoye, OO; Cabral, AD; Sedighi, A; de Araujo, ED; Gunning, PT University of Toronto Mississauga http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19410 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19410&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4261 46519433 CHEMBL27759 7007 ZINC01488870 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51272007 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1Cl InChI=1S/C24H26ClN5O3/c25-20-12-7-8-13-21(20)30(19-10-4-3-5-11-19)24-27-16-18(17-28-24)23(32)26-15-9-2-1-6-14-22(31)29-33/h3-5,7-8,10-13,16-17,33H,1-2,6,9,14-15H2,(H,26,32)(H,29,31) VLIUIBXPEDFJRF-UHFFFAOYSA-N 110036 US8609678, 2-((2-chlorophenyl)(phenyl)amino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [89] Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acsmedchemlett.9b00471 10.7270/Q26976Z8 31938464 Shouksmith, AE; Gawel, JM; Nawar, N; Sina, D; Raouf, YS; Bukhari, S; He, L; Johns, AE; Manaswiyoungkul, P; Olaoye, OO; Cabral, AD; Sedighi, A; de Araujo, ED; Gunning, PT University of Toronto Mississauga http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=110036 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=110036&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 53340426 186526906 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51272031 C[C@H](\C=C(/C)\C=C\C(=O)NO)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1 RTKIYFITIVXBLE-QEQCGCAPSA-N 50005711 CHEBI:46024::GNF-Pf-1011::TRICHOSTATIN::Trichostatin A::Trichostatin A (TSA)::US10011611, Trichostatin A::US10722597, Compound Trichostatin::US11535598, Compound Trichostatin A::US9265734, TSA Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acsmedchemlett.9b00471 10.7270/Q26976Z8 31938464 Shouksmith, AE; Gawel, JM; Nawar, N; Sina, D; Raouf, YS; Bukhari, S; He, L; Johns, AE; Manaswiyoungkul, P; Olaoye, OO; Cabral, AD; Sedighi, A; de Araujo, ED; Gunning, PT University of Toronto Mississauga http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 444732 242056952 DB04297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51272049 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1 InChI=1S/C24H27N5O3/c30-22(28-32)15-9-1-2-10-16-25-23(31)19-17-26-24(27-18-19)29(20-11-5-3-6-12-20)21-13-7-4-8-14-21/h3-8,11-14,17-18,32H,1-2,9-10,15-16H2,(H,25,31)(H,28,30) QGZYDVAGYRLSKP-UHFFFAOYSA-N 50439674 RICOLINOSTAT::US10858323, Compound 2::US11207431, Example E::US8609678, 2-(diphenylamino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [26] Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acsmedchemlett.9b00471 10.7270/Q26976Z8 31938464 Shouksmith, AE; Gawel, JM; Nawar, N; Sina, D; Raouf, YS; Bukhari, S; He, L; Johns, AE; Manaswiyoungkul, P; Olaoye, OO; Cabral, AD; Sedighi, A; de Araujo, ED; Gunning, PT University of Toronto Mississauga http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50439674 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50439674&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search AH4 5WGL 53340666 175451991 ZINC89630354 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51271798 CC(C)c1cc(C(=O)N(C)c2ccc(NC(=O)CCCCCCCC(=O)NO)cc2)c(O)cc1O InChI=1S/C26H35N3O6/c1-17(2)20-15-21(23(31)16-22(20)30)26(34)29(3)19-13-11-18(12-14-19)27-24(32)9-7-5-4-6-8-10-25(33)28-35/h11-17,30-31,35H,4-10H2,1-3H3,(H,27,32)(H,28,33) BPYXZYFZLYBSIO-UHFFFAOYSA-N 50519398 CHEMBL4448385 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2019.111725 10.7270/Q2V1286G 31655430 Mehndiratta, S; Lin, MH; Wu, YW; Chen, CH; Wu, TY; Chuang, KH; Chao, MW; Chen, YY; Pan, SL; Chen, MC; Liou, JP Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50519398 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50519398&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155519645 440727980 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51271825 CC(C)c1cc(C(=O)N(C)c2ccc(NC(=O)CCCCCCC(=O)NO)cc2)c(O)cc1O InChI=1S/C25H33N3O6/c1-16(2)19-14-20(22(30)15-21(19)29)25(33)28(3)18-12-10-17(11-13-18)26-23(31)8-6-4-5-7-9-24(32)27-34/h10-16,29-30,34H,4-9H2,1-3H3,(H,26,31)(H,27,32) NRTQVEBKTMOYBI-UHFFFAOYSA-N 50519391 CHEMBL4514330 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2019.111725 10.7270/Q2V1286G 31655430 Mehndiratta, S; Lin, MH; Wu, YW; Chen, CH; Wu, TY; Chuang, KH; Chao, MW; Chen, YY; Pan, SL; Chen, MC; Liou, JP Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50519391 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50519391&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155539311 440727973 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309124 C[C@H](\C=C(/C)\C=C\C(=O)NO)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1 RTKIYFITIVXBLE-QEQCGCAPSA-N 50005711 CHEBI:46024::GNF-Pf-1011::TRICHOSTATIN::Trichostatin A::Trichostatin A (TSA)::US10011611, Trichostatin A::US10722597, Compound Trichostatin::US11535598, Compound Trichostatin A::US9265734, TSA Histone deacetylase 4 Homo sapiens 34 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 444732 242056952 DB04297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309129 ONC(=O)\C=C\c1cccn(CCc2ccc3ccccc3c2)c1=O InChI=1S/C20H18N2O3/c23-19(21-25)10-9-17-6-3-12-22(20(17)24)13-11-15-7-8-16-4-1-2-5-18(16)14-15/h1-10,12,14,25H,11,13H2,(H,21,23)/b10-9+ XQXZIMLBLPDARP-MDZDMXLPSA-N 50531333 CHEMBL4577107 Histone deacetylase 4 Homo sapiens 14625 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531333 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531333&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 49846123 440739915 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309136 C\C=C1/NC(=O)[C@H]2CSSCC\C=C\[C@@H](CC(=O)N[C@H](C(C)C)C(=O)N2)OC(=O)[C@@H](NC1=O)C(C)C InChI=1S/C24H36N4O6S2/c1-6-16-21(30)28-20(14(4)5)24(33)34-15-9-7-8-10-35-36-12-17(22(31)25-16)26-23(32)19(13(2)3)27-18(29)11-15/h6-7,9,13-15,17,19-20H,8,10-12H2,1-5H3,(H,25,31)(H,26,32)(H,27,29)(H,28,30)/b9-7+,16-6-/t15-,17+,19+,20-/m0/s1 OHRURASPPZQGQM-QSVHVVLASA-N 50048864 CHEMBL3310505 Histone deacetylase 4 Homo sapiens 510 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50048864 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50048864&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11947684 103979245 CHEMBL3310505 ZINC13745305 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309150 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 1600 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309173 ONC(=O)c1ccc(Cn2c3CCS(=O)(=O)Cc3c3ccccc23)cc1 InChI=1S/C19H18N2O4S/c22-19(20-23)14-7-5-13(6-8-14)11-21-17-4-2-1-3-15(17)16-12-26(24,25)10-9-18(16)21/h1-8,23H,9-12H2,(H,20,22) JTWSNIOCMRULQH-UHFFFAOYSA-N 50531339 CHEMBL4577299 Histone deacetylase 4 Homo sapiens 1600 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531339 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531339&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71583103 440739921 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309174 ONC(=O)c1ccc(Cn2c3CCS(=O)(=O)Cc3c3cc(F)ccc23)cc1 InChI=1S/C19H17FN2O4S/c20-14-5-6-17-15(9-14)16-11-27(25,26)8-7-18(16)22(17)10-12-1-3-13(4-2-12)19(23)21-24/h1-6,9,24H,7-8,10-11H2,(H,21,23) UFLTXBAQOUWVFZ-UHFFFAOYSA-N 50531341 CHEMBL4531108 Histone deacetylase 4 Homo sapiens 1900 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531341 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531341&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71583105 440739923 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309175 ONC(=O)c1ccc(Cn2c3CC[S+]([O-])Cc3c3cc(F)ccc23)cc1 InChI=1S/C19H17FN2O3S/c20-14-5-6-17-15(9-14)16-11-26(25)8-7-18(16)22(17)10-12-1-3-13(4-2-12)19(23)21-24/h1-6,9,24H,7-8,10-11H2,(H,21,23) SHZDDDMVFPGXKW-UHFFFAOYSA-N 50531342 CHEMBL4283105 Histone deacetylase 4 Homo sapiens 1200 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531342 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531342&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118656852 440739924 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309176 ONC(=O)c1ccc(CN2[C@@H]3CCCC[C@H]3Cc3ccccc23)cc1 InChI=1S/C21H24N2O2/c24-21(22-25)16-11-9-15(10-12-16)14-23-19-7-3-1-5-17(19)13-18-6-2-4-8-20(18)23/h1,3,5,7,9-12,18,20,25H,2,4,6,8,13-14H2,(H,22,24)/t18-,20+/m0/s1 CRDNJGOSRIVAFU-AZUAARDMSA-N 50531340 CHEMBL4471619 Histone deacetylase 4 Homo sapiens >30000 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531340 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531340&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155535084 440739922 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309177 ONC(=O)c1ccc(CN2[C@@H]3CCCCC[C@H]3Cc3ccccc23)cc1 InChI=1S/C22H26N2O2/c25-22(23-26)17-12-10-16(11-13-17)15-24-20-8-3-1-2-6-18(20)14-19-7-4-5-9-21(19)24/h4-5,7,9-13,18,20,26H,1-3,6,8,14-15H2,(H,23,25)/t18-,20+/m0/s1 FGMWOTOTJBZLHH-AZUAARDMSA-N 50531343 CHEMBL4579366 Histone deacetylase 4 Homo sapiens >30000 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531343 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531343&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155565491 440739925 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309257 ONC(=O)CCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@@H]2CCCCCCCCCCC[C@@H](NC1=O)C(=O)N2 InChI=1S/C28H47N5O6/c34-24(32-39)18-12-8-11-15-21-25(35)29-20-14-9-6-4-2-1-3-5-7-10-16-22(31-26(20)36)28(38)33-19-13-17-23(33)27(37)30-21/h20-23,39H,1-19H2,(H,29,35)(H,30,37)(H,31,36)(H,32,34)/t20-,21+,22+,23-/m1/s1 TVNZWPOEHUTSFV-WZYRSQIMSA-N 50309931 6-((1S,7R,10S,13R)-2,8,11,26-Tetraoxo-3,9,12,25-tetraaza-tricyclo[11.11.2.0*3,7*]hexacos-10-yl)-hexanoic acid hydroxyamide::CHEMBL589311 Histone deacetylase 4 Homo sapiens 4.5 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50309931 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50309931&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 46216760 104164292 CHEMBL589311 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309258 OB(O)CCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@@H]2CCCCCCCCCCC[C@@H](NC1=O)C(=O)N2 InChI=1S/C27H47BN4O6/c33-24-21(15-11-8-12-18-28(37)38)30-26(35)23-17-13-19-32(23)27(36)22-16-10-7-5-3-1-2-4-6-9-14-20(29-24)25(34)31-22/h20-23,37-38H,1-19H2,(H,29,33)(H,30,35)(H,31,34)/t20-,21+,22+,23-/m1/s1 YBAFTIVPWJJYBI-WZYRSQIMSA-N 50531364 CHEMBL4524515 Histone deacetylase 4 Homo sapiens 9400 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531364 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531364&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155520119 440739946 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309259 CC1CCCCC11NC(=O)[C@H](CCCCCC(=O)NO)NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC1=O InChI=1S/C30H43N5O6/c1-20-11-8-9-17-30(20)29(40)32-23(19-21-12-4-2-5-13-21)28(39)35-18-10-15-24(35)27(38)31-22(26(37)33-30)14-6-3-7-16-25(36)34-41/h2,4-5,12-13,20,22-24,41H,3,6-11,14-19H2,1H3,(H,31,38)(H,32,40)(H,33,37)(H,34,36)/t20?,22-,23-,24+,30?/m0/s1 SZZPNZMUSIGRPA-XQMXURKASA-N 50531330 CHEMBL4467160 Histone deacetylase 4 Homo sapiens 6.0 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531330 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531330&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155531979 440739912 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309270 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 340 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309271 CC(=O)SCCCCCC(NC(=O)OCc1ccccc1)C(=O)Nc1cccc2cccnc12 InChI=1S/C26H29N3O4S/c1-19(30)34-17-7-3-6-14-23(29-26(32)33-18-20-10-4-2-5-11-20)25(31)28-22-15-8-12-21-13-9-16-27-24(21)22/h2,4-5,8-13,15-16,23H,3,6-7,14,17-18H2,1H3,(H,28,31)(H,29,32) UJKGYYPNUCRQFO-UHFFFAOYSA-N 50531368 CHEMBL4551751 Histone deacetylase 4 Homo sapiens 18 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531368 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531368&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155555900 440739950 C04334 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309272 O=C(NC(CCCCCSSCCCCCC(NC(=O)OCc1ccccc1)C(=O)Nc1cccc2cccnc12)C(=O)Nc1cccc2cccnc12)OCc1ccccc1 InChI=1S/C48H52N6O6S2/c55-45(51-39-27-13-21-37-23-15-29-49-43(37)39)41(53-47(57)59-33-35-17-5-1-6-18-35)25-9-3-11-31-61-62-32-12-4-10-26-42(54-48(58)60-34-36-19-7-2-8-20-36)46(56)52-40-28-14-22-38-24-16-30-50-44(38)40/h1-2,5-8,13-24,27-30,41-42H,3-4,9-12,25-26,31-34H2,(H,51,55)(H,52,56)(H,53,57)(H,54,58) XQPDEMOFEZWKBH-UHFFFAOYSA-N 50531366 CHEMBL4543038 Histone deacetylase 4 Homo sapiens 3.4 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531366 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531366&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155551891 440739948 C15496 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309273 CCCCCCCC(=O)SCC\C=C\[C@@H]1CC(=O)NCc2nc(cs2)C2=N[C@@](C)(CS2)C(=O)C[C@@H](C(C)C)C(=O)C1 InChI=1S/C31H45N3O4S3/c1-5-6-7-8-9-13-29(38)39-14-11-10-12-22-15-25(35)23(21(2)3)17-26(36)31(4)20-41-30(34-31)24-19-40-28(33-24)18-32-27(37)16-22/h10,12,19,21-23H,5-9,11,13-18,20H2,1-4H3,(H,32,37)/b12-10+/t22-,23-,31-/m0/s1 NPICYKHOEXQJGW-UNTWLVQOSA-N 50531367 CHEMBL4452333 Histone deacetylase 4 Homo sapiens 3000 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531367 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531367&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155523130 440739949 C05752 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309314 ONC(=O)\C=C\c1cccn(CCCc2ccc3ccccc3c2)c1=O InChI=1S/C21H20N2O3/c24-20(22-26)12-11-18-8-4-14-23(21(18)25)13-3-5-16-9-10-17-6-1-2-7-19(17)15-16/h1-2,4,6-12,14-15,26H,3,5,13H2,(H,22,24)/b12-11+ KYXMKYJAKNUUDF-VAWYXSNFSA-N 50531329 CHEMBL4082995 Histone deacetylase 4 Homo sapiens 5730 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531329 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531329&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 49847150 440739911 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309326 COCCOCC(=O)SCCCCCC(NC(=O)OCc1ccccc1)C(=O)Nc1cccc2cccnc12 InChI=1S/C29H35N3O6S/c1-36-17-18-37-21-26(33)39-19-7-3-6-14-25(32-29(35)38-20-22-10-4-2-5-11-22)28(34)31-24-15-8-12-23-13-9-16-30-27(23)24/h2,4-5,8-13,15-16,25H,3,6-7,14,17-21H2,1H3,(H,31,34)(H,32,35) ADSFNXXUDGBABJ-UHFFFAOYSA-N 50531381 CHEMBL4593341 Histone deacetylase 4 Homo sapiens 18 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531381 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531381&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155568884 440739963 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309343 ONC(=O)c1ccc(Cn2c3CCSCc3c3cc(F)ccc23)cc1 InChI=1S/C19H17FN2O2S/c20-14-5-6-17-15(9-14)16-11-25-8-7-18(16)22(17)10-12-1-3-13(4-2-12)19(23)21-24/h1-6,9,24H,7-8,10-11H2,(H,21,23) LOFPHNPTVBYXBB-UHFFFAOYSA-N 50531323 CHEMBL4537561 Histone deacetylase 4 Homo sapiens 1500 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531323 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531323&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71583101 440739905 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309344 ONC(=O)c1ccc(CN2[C@@H]3CCCC[C@H]3CCCc3ccccc23)cc1 InChI=1S/C23H28N2O2/c26-23(24-27)20-14-12-17(13-15-20)16-25-21-10-3-1-6-18(21)8-5-9-19-7-2-4-11-22(19)25/h1,3,6,10,12-15,19,22,27H,2,4-5,7-9,11,16H2,(H,24,26)/t19-,22+/m0/s1 GCFYEXIGUMACTD-SIKLNZKXSA-N 50531318 CHEMBL4557665 Histone deacetylase 4 Homo sapiens >30000 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531318 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531318&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155554360 440739900 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309356 CC1CCCC2(C1)NC(=O)[C@H](CCCCCC(=O)NO)NC(=O)[C@H]1CCCN1C(=O)[C@H](Cc1ccccc1)NC2=O InChI=1S/C30H43N5O6/c1-20-10-8-16-30(19-20)29(40)32-23(18-21-11-4-2-5-12-21)28(39)35-17-9-14-24(35)27(38)31-22(26(37)33-30)13-6-3-7-15-25(36)34-41/h2,4-5,11-12,20,22-24,41H,3,6-10,13-19H2,1H3,(H,31,38)(H,32,40)(H,33,37)(H,34,36)/t20?,22-,23-,24+,30?/m0/s1 RYFHRSBVYHHCEC-XQMXURKASA-N 50531363 CHEMBL4567942 Histone deacetylase 4 Homo sapiens 14 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531363 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531363&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 76853285 440739945 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309358 C[C@H](\C=C(/C)\C=C\C(=O)NO)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1 RTKIYFITIVXBLE-QEQCGCAPSA-N 50005711 CHEBI:46024::GNF-Pf-1011::TRICHOSTATIN::Trichostatin A::Trichostatin A (TSA)::US10011611, Trichostatin A::US10722597, Compound Trichostatin::US11535598, Compound Trichostatin A::US9265734, TSA Histone deacetylase 4 Homo sapiens 1400 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 444732 242056952 DB04297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309368 ONC(=O)c1ccc(CN2[C@@H]3CCCC[C@H]3CCc3ccccc23)cc1 InChI=1S/C22H26N2O2/c25-22(23-26)19-11-9-16(10-12-19)15-24-20-7-3-1-5-17(20)13-14-18-6-2-4-8-21(18)24/h1,3,5,7,9-12,18,21,26H,2,4,6,8,13-15H2,(H,23,25)/t18-,21+/m0/s1 UOEQVYQBYSGXBR-GHTZIAJQSA-N 50531320 CHEMBL4469098 Histone deacetylase 4 Homo sapiens >30000 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531320 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531320&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155533876 440739902 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309397 C[C@H](\C=C(/C)\C=C\C(=O)NO)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1 RTKIYFITIVXBLE-QEQCGCAPSA-N 50005711 CHEBI:46024::GNF-Pf-1011::TRICHOSTATIN::Trichostatin A::Trichostatin A (TSA)::US10011611, Trichostatin A::US10722597, Compound Trichostatin::US11535598, Compound Trichostatin A::US9265734, TSA Histone deacetylase 4 Homo sapiens 6600 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 444732 242056952 DB04297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309402 OCCN(C(=O)Cc1ccc(cc1)C(=O)NO)c1ccccc1 InChI=1S/C17H18N2O4/c20-11-10-19(15-4-2-1-3-5-15)16(21)12-13-6-8-14(9-7-13)17(22)18-23/h1-9,20,23H,10-12H2,(H,18,22) RFAZNTABYJYOAR-UHFFFAOYSA-N 198121 HPOB Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=198121 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=198121&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5OJ 5EF7 71532921 318489194 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309411 ONC(=O)c1ccc(CN2C3CCS(=O)(=O)C3c3ccccc23)cc1 InChI=1S/C18H18N2O4S/c21-18(19-22)13-7-5-12(6-8-13)11-20-15-4-2-1-3-14(15)17-16(20)9-10-25(17,23)24/h1-8,16-17,22H,9-11H2,(H,19,21) XYQDILWULREMBI-UHFFFAOYSA-N 50531317 CHEMBL4445312 Histone deacetylase 4 Homo sapiens 600 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531317 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531317&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155518062 440739899 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309429 COCC(=O)CCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@@H]2CCCCCCCCCCC[C@@H](NC1=O)C(=O)N2 InChI=1S/C30H50N4O6/c1-40-21-22(35)15-10-9-13-17-24-27(36)31-23-16-11-7-5-3-2-4-6-8-12-18-25(33-28(23)37)30(39)34-20-14-19-26(34)29(38)32-24/h23-26H,2-21H2,1H3,(H,31,36)(H,32,38)(H,33,37)/t23-,24+,25+,26-/m1/s1 HTSRJCYFMOFFNE-KEVKATSASA-N 50531380 CHEMBL4557234 Histone deacetylase 4 Homo sapiens 26 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531380 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531380&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155554383 440739962 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51309434 OCCSSCCCCCC(NC(=O)OCc1ccccc1)C(=O)Nc1cccc2cccnc12 InChI=1S/C26H31N3O4S2/c30-16-18-35-34-17-6-2-5-13-23(29-26(32)33-19-20-9-3-1-4-10-20)25(31)28-22-14-7-11-21-12-8-15-27-24(21)22/h1,3-4,7-12,14-15,23,30H,2,5-6,13,16-19H2,(H,28,31)(H,29,32) OMEMORTXMDILLA-UHFFFAOYSA-N 50531365 CHEMBL4438404 Histone deacetylase 4 Homo sapiens 2.0 ChEMBL 10.1016/j.ejmech.2018.08.073 10.7270/Q2HT2STK 30245394 Sangwan, R; Rajan, R; Mandal, PK Indian CSIR-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531365 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531365&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155513281 440739947 C15496 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51310003 ONC(=O)\C=C\c1ccc2C(=O)c3ccccc3C(=O)c2c1 InChI=1S/C17H11NO4/c19-15(18-22)8-6-10-5-7-13-14(9-10)17(21)12-4-2-1-3-11(12)16(13)20/h1-9,22H,(H,18,19)/b8-6+ YQEOLWSMXGNTKB-SOFGYWHQSA-N 50531608 CHEMBL4556817 Histone deacetylase 4 Homo sapiens 16180 ChEMBL 10.1016/j.ejmech.2018.12.056 10.7270/Q279485Z 30597327 Song, Y; Lim, J; Seo, YH Keimyung University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531608 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531608&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 149405396 440740190 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51310014 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 37090 ChEMBL 10.1016/j.ejmech.2018.12.056 10.7270/Q279485Z 30597327 Song, Y; Lim, J; Seo, YH Keimyung University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51310017 ONC(=O)c1ccc2C(=O)c3ccccc3C(=O)c2c1 InChI=1S/C15H9NO4/c17-13-9-3-1-2-4-10(9)14(18)12-7-8(15(19)16-20)5-6-11(12)13/h1-7,20H,(H,16,19) CNGWNOQUKFLVKK-UHFFFAOYSA-N 50531609 CHEMBL4437432 Histone deacetylase 4 Homo sapiens 5611 ChEMBL 10.1016/j.ejmech.2018.12.056 10.7270/Q279485Z 30597327 Song, Y; Lim, J; Seo, YH Keimyung University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531609 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531609&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 147254231 440740191 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51320645 ONC(=O)[C@H](Cc1ccccc1)n1nnc(c1C#CC1CC1)-c1ccccc1 InChI=1S/C22H20N4O2/c27-22(24-28)20(15-17-7-3-1-4-8-17)26-19(14-13-16-11-12-16)21(23-25-26)18-9-5-2-6-10-18/h1-10,16,20,28H,11-12,15H2,(H,24,27)/t20-/m0/s1 WQUMCIJBZDIUPT-FQEVSTJZSA-N 50534338 CHEMBL4534486 Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.1021/acsmedchemlett.6b00239 10.7270/Q2QC0718 27774131 Ingham, OJ; Paranal, RM; Smith, WB; Escobar, RA; Yueh, H; Snyder, T; Porco, JA; Bradner, JE; Beeler, AB Boston University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50534338 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50534338&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 76853213 440742920 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51319538 ONC(=O)CCCC(=O)NCCc1ccccc1 InChI=1S/C13H18N2O3/c16-12(7-4-8-13(17)15-18)14-10-9-11-5-2-1-3-6-11/h1-3,5-6,18H,4,7-10H2,(H,14,16)(H,15,17) MNMBNWINDLRVJD-UHFFFAOYSA-N 50494414 CHEMBL3086768 Histone deacetylase 4 Homo sapiens 5000 ChEMBL 10.1016/j.bmc.2016.08.040 10.7270/Q29C71WX 27614919 Gromek, SM; deMayo, JA; Maxwell, AT; West, AM; Pavlik, CM; Zhao, Z; Li, J; Wiemer, AJ; Zweifach, A; Balunas, MJ University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50494414 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50494414&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72734543 433961679 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51319546 CCOC(=O)NCCCC(=O)NCCc1ccccc1 InChI=1S/C15H22N2O3/c1-2-20-15(19)17-11-6-9-14(18)16-12-10-13-7-4-3-5-8-13/h3-5,7-8H,2,6,9-12H2,1H3,(H,16,18)(H,17,19) HTOYBIILVCHURC-UHFFFAOYSA-N 50494415 CHEMBL3086767 Histone deacetylase 4 Homo sapiens 5000 ChEMBL 10.1016/j.bmc.2016.08.040 10.7270/Q29C71WX 27614919 Gromek, SM; deMayo, JA; Maxwell, AT; West, AM; Pavlik, CM; Zhao, Z; Li, J; Wiemer, AJ; Zweifach, A; Balunas, MJ University of Connecticut http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50494415 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50494415&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72946782 433961680 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51320635 ONC(=O)[C@H](Cc1ccccc1)n1nnc(c1C#Cc1ccccc1)-c1ccccc1 InChI=1S/C25H20N4O2/c30-25(27-31)23(18-20-12-6-2-7-13-20)29-22(17-16-19-10-4-1-5-11-19)24(26-28-29)21-14-8-3-9-15-21/h1-15,23,31H,18H2,(H,27,30)/t23-/m0/s1 JMEPDOCHFSIAAG-QHCPKHFHSA-N 50534339 CHEMBL4593948 Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.1021/acsmedchemlett.6b00239 10.7270/Q2QC0718 27774131 Ingham, OJ; Paranal, RM; Smith, WB; Escobar, RA; Yueh, H; Snyder, T; Porco, JA; Bradner, JE; Beeler, AB Boston University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50534339 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50534339&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 78324068 440742921 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51290675 Nc1ccccc1NC(=O)c1ccc(CN2CC(=C)c3ccccc3C2=O)cc1 InChI=1S/C24H21N3O2/c1-16-14-27(24(29)20-7-3-2-6-19(16)20)15-17-10-12-18(13-11-17)23(28)26-22-9-5-4-8-21(22)25/h2-13H,1,14-15,25H2,(H,26,28) GTLTXEIKQVWSRF-UHFFFAOYSA-N 50470576 CHEMBL4294949 Histone deacetylase 4 Homo sapiens 5000 ChEMBL 10.1016/j.ejmech.2019.01.077 10.7270/Q2K93BZT 30735902 Amin, SA; Adhikari, N; Kotagiri, S; Jha, T; Ghosh, B Jadavpur University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50470576 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50470576&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 56965342 433937841 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51294237 CC[C@H](Nc1ncnc2[nH]cnc12)c1nc(CCCCCC(=O)NO)c2ccccc2n1 InChI=1S/C22H26N8O2/c1-2-15(27-22-19-21(24-12-23-19)25-13-26-22)20-28-16(9-4-3-5-11-18(31)30-32)14-8-6-7-10-17(14)29-20/h6-8,10,12-13,15,32H,2-5,9,11H2,1H3,(H,30,31)(H2,23,24,25,26,27)/t15-/m0/s1 XQCPGFJFDSSKBD-HNNXBMFYSA-N 50527618 CHEMBL4539040 Histone deacetylase 4 Homo sapiens 100000 ChEMBL 10.1021/acs.jmedchem.0c00193 10.7270/Q2KS6W0V 32212730 Thakur, A; Tawa, GJ; Henderson, MJ; Danchik, C; Liu, S; Shah, P; Wang, AQ; Dunn, G; Kabir, M; Padilha, EC; Xu, X; Simeonov, A; Kharbanda, S; Stone, R; Grewal, G National Center for Advancing Translational Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50527618 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50527618&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 142505968 440736200 C02860 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51294238 CC[C@H](Nc1ncnc2[nH]cnc12)c1nc2cccc(NCc3ccc(cn3)C(=O)NO)c2c(=O)n1-c1ccccc1 InChI=1S/C29H26N10O3/c1-2-20(36-26-24-25(33-15-32-24)34-16-35-26)27-37-22-10-6-9-21(23(22)29(41)39(27)19-7-4-3-5-8-19)31-14-18-12-11-17(13-30-18)28(40)38-42/h3-13,15-16,20,31,42H,2,14H2,1H3,(H,38,40)(H2,32,33,34,35,36)/t20-/m0/s1 NNCNCNUUHFTRQN-FQEVSTJZSA-N 50527607 CHEMBL4443548 Histone deacetylase 4 Homo sapiens 381 ChEMBL 10.1021/acs.jmedchem.0c00193 10.7270/Q2KS6W0V 32212730 Thakur, A; Tawa, GJ; Henderson, MJ; Danchik, C; Liu, S; Shah, P; Wang, AQ; Dunn, G; Kabir, M; Padilha, EC; Xu, X; Simeonov, A; Kharbanda, S; Stone, R; Grewal, G National Center for Advancing Translational Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50527607 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50527607&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 146585718 440736189 C02860 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51294268 CC[C@H](Nc1ncnc2[nH]cnc12)c1nc(NCCCC(=O)NO)c2ccccc2n1 InChI=1S/C20H23N9O2/c1-2-13(26-20-16-19(23-10-22-16)24-11-25-20)18-27-14-7-4-3-6-12(14)17(28-18)21-9-5-8-15(30)29-31/h3-4,6-7,10-11,13,31H,2,5,8-9H2,1H3,(H,29,30)(H,21,27,28)(H2,22,23,24,25,26)/t13-/m0/s1 OQBTZSPSRKQWJQ-ZDUSSCGKSA-N 50527612 CHEMBL4439820 Histone deacetylase 4 Homo sapiens 100000 ChEMBL 10.1021/acs.jmedchem.0c00193 10.7270/Q2KS6W0V 32212730 Thakur, A; Tawa, GJ; Henderson, MJ; Danchik, C; Liu, S; Shah, P; Wang, AQ; Dunn, G; Kabir, M; Padilha, EC; Xu, X; Simeonov, A; Kharbanda, S; Stone, R; Grewal, G National Center for Advancing Translational Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50527612 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50527612&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 142506170 440736194 C02860 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298215 O=C1Sc2ccccc2C2=NCCCN12 InChI=1S/C11H10N2OS/c14-11-13-7-3-6-12-10(13)8-4-1-2-5-9(8)15-11/h1-2,4-5H,3,6-7H2 YDKBMIFGWFISIE-UHFFFAOYSA-N 50529148 CHEMBL4582224 Histone deacetylase 4 Homo sapiens 5900 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529148 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529148&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60200243 440737730 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298216 Fc1cc(Br)cc2SC(=S)N3CCN=C3c12 InChI=1S/C10H6BrFN2S2/c11-5-3-6(12)8-7(4-5)16-10(15)14-2-1-13-9(8)14/h3-4H,1-2H2 VVPDIYAALCJMRK-UHFFFAOYSA-N 50529138 CHEMBL4580307 Histone deacetylase 4 Homo sapiens 4100 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529138 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529138&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155565674 440737720 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298217 Fc1ccc2SC(=S)N3CCCN=C3c2c1 InChI=1S/C11H9FN2S2/c12-7-2-3-9-8(6-7)10-13-4-1-5-14(10)11(15)16-9/h2-3,6H,1,4-5H2 ONKSFHXYNMMECZ-UHFFFAOYSA-N 50529136 CHEMBL4463244 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529136 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529136&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 129104227 440737718 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298222 COc1ccc2C3=NCCN3C(=S)Sc2c1 InChI=1S/C11H10N2OS2/c1-14-7-2-3-8-9(6-7)16-11(15)13-5-4-12-10(8)13/h2-3,6H,4-5H2,1H3 BYIFHHTYFILUMK-UHFFFAOYSA-N 50529152 CHEMBL4514367 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529152 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529152&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155539319 440737734 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298223 Clc1cccc2SC(=S)N3CCCN=C3c12 InChI=1S/C11H9ClN2S2/c12-7-3-1-4-8-9(7)10-13-5-2-6-14(10)11(15)16-8/h1,3-4H,2,5-6H2 XOTIQYGBONSIAZ-UHFFFAOYSA-N 50529134 CHEMBL4516558 Histone deacetylase 4 Homo sapiens 1400 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529134 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529134&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155540189 440737716 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51301854 C[C@@H]1CN(CCO1)C(=O)Nc1ccc(cc1)-c1nc(N2CCOCC2)c2cnn(CCCCCCC(=O)NO)c2n1 InChI=1S/C28H38N8O5/c1-20-19-35(14-17-41-20)28(38)30-22-9-7-21(8-10-22)25-31-26(34-12-15-40-16-13-34)23-18-29-36(27(23)32-25)11-5-3-2-4-6-24(37)33-39/h7-10,18,20,39H,2-6,11-17,19H2,1H3,(H,30,38)(H,33,37)/t20-/m1/s1 YPXRCUVTZDXVHY-HXUWFJFHSA-N 50530002 CHEMBL4532398 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acs.jmedchem.8b01825 10.7270/Q20868S8 30629434 Chen, Y; Yuan, X; Zhang, W; Tang, M; Zheng, L; Wang, F; Yan, W; Yang, S; Wei, Y; He, J; Chen, L TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50530002 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50530002&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137628684 440738584 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298310 S=C1Sc2cc(ccc2C2=NCCN12)C#N InChI=1S/C11H7N3S2/c12-6-7-1-2-8-9(5-7)16-11(15)14-4-3-13-10(8)14/h1-2,5H,3-4H2 KOBXGDPSXGREFC-UHFFFAOYSA-N 50529137 CHEMBL4583466 Histone deacetylase 4 Homo sapiens 6800 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529137 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529137&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155562249 440737719 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298311 Brc1ccc2SC(=S)N3CCN=C3c2c1 InChI=1S/C10H7BrN2S2/c11-6-1-2-8-7(5-6)9-12-3-4-13(9)10(14)15-8/h1-2,5H,3-4H2 KZIZEDNFZLTFGR-UHFFFAOYSA-N 50529149 CHEMBL4475077 Histone deacetylase 4 Homo sapiens 17000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155537573 440737731 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298312 Brc1cccc2SC(=S)N3CCN=C3c12 InChI=1S/C10H7BrN2S2/c11-6-2-1-3-7-8(6)9-12-4-5-13(9)10(14)15-7/h1-3H,4-5H2 QSRDMFWIKLRMOW-UHFFFAOYSA-N 50529161 CHEMBL4527868 Histone deacetylase 4 Homo sapiens 5100 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529161 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529161&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155544459 440737743 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298313 Brc1ccc2C3=NCCN3C(=S)Sc2c1 InChI=1S/C10H7BrN2S2/c11-6-1-2-7-8(5-6)15-10(14)13-4-3-12-9(7)13/h1-2,5H,3-4H2 KJYDOYMIBGLEAG-UHFFFAOYSA-N 50529130 CHEMBL4462619 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529130 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529130&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155529137 440737712 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298314 Ic1ccc2SC(=S)N3CCN=C3c2c1 InChI=1S/C10H7IN2S2/c11-6-1-2-8-7(5-6)9-12-3-4-13(9)10(14)15-8/h1-2,5H,3-4H2 MZNARERCSNMRFL-UHFFFAOYSA-N 50529162 CHEMBL4531463 Histone deacetylase 4 Homo sapiens 20000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529162 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529162&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155546632 440737744 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298315 Cc1ccc2SC(=S)N3CCN=C3c2c1 InChI=1S/C11H10N2S2/c1-7-2-3-9-8(6-7)10-12-4-5-13(10)11(14)15-9/h2-3,6H,4-5H2,1H3 NOYKRSRQTIQQCU-UHFFFAOYSA-N 50529144 CHEMBL4578368 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529144 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529144&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155564750 440737726 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298316 Clc1ccc2C3=NCCN3C(=S)Sc2c1 InChI=1S/C10H7ClN2S2/c11-6-1-2-7-8(5-6)15-10(14)13-4-3-12-9(7)13/h1-2,5H,3-4H2 OIJOGIXKKXNSED-UHFFFAOYSA-N 50529163 CHEMBL4440904 Histone deacetylase 4 Homo sapiens 11000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529163 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529163&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155514603 440737745 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298317 Ic1cccc2SC(=S)N3CCN=C3c12 InChI=1S/C10H7IN2S2/c11-6-2-1-3-7-8(6)9-12-4-5-13(9)10(14)15-7/h1-3H,4-5H2 SOAMZCWXCKKAIA-UHFFFAOYSA-N 50529132 CHEMBL4583053 Histone deacetylase 4 Homo sapiens 20000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529132 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529132&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155566122 440737714 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298318 Fc1cccc2C3=NCCN3C(=S)Sc12 InChI=1S/C10H7FN2S2/c11-7-3-1-2-6-8(7)15-10(14)13-5-4-12-9(6)13/h1-3H,4-5H2 VKRUXLIIQYTIAA-UHFFFAOYSA-N 50529131 CHEMBL4467248 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529131 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529131&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 129104402 440737713 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298319 CN(C)c1ccc2C3=NCCN3C(=S)Sc2c1 InChI=1S/C12H13N3S2/c1-14(2)8-3-4-9-10(7-8)17-12(16)15-6-5-13-11(9)15/h3-4,7H,5-6H2,1-2H3 HRRBQSDXCUZKKT-UHFFFAOYSA-N 50529164 CHEMBL4556055 Histone deacetylase 4 Homo sapiens 32000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529164 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529164&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155550827 440737746 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298320 Fc1cccc2SC(=S)N3CCN=C3c12 InChI=1S/C10H7FN2S2/c11-6-2-1-3-7-8(6)9-12-4-5-13(9)10(14)15-7/h1-3H,4-5H2 JUBLKPGWZRDUPQ-UHFFFAOYSA-N 50529154 CHEMBL4438437 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529154 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529154&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155513471 440737736 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298321 Cc1ccc2C3=NCCN3C(=S)Sc2c1 InChI=1S/C11H10N2S2/c1-7-2-3-8-9(6-7)15-11(14)13-5-4-12-10(8)13/h2-3,6H,4-5H2,1H3 GMZLHKSEGJIFAH-UHFFFAOYSA-N 50529165 CHEMBL4587389 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529165 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529165&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155566461 440737747 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298322 Cc1cccc2C3=NCCN3C(=S)Sc12 InChI=1S/C11H10N2S2/c1-7-3-2-4-8-9(7)15-11(14)13-6-5-12-10(8)13/h2-4H,5-6H2,1H3 JCHNUJLNFOMCKL-UHFFFAOYSA-N 50529133 CHEMBL4462363 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529133 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529133&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155529066 440737715 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298323 Ic1cccc2SC(=S)N3CCCN=C3c12 InChI=1S/C11H9IN2S2/c12-7-3-1-4-8-9(7)10-13-5-2-6-14(10)11(15)16-8/h1,3-4H,2,5-6H2 STEYNPOIAMHHEV-UHFFFAOYSA-N 50529167 CHEMBL4442562 Histone deacetylase 4 Homo sapiens 2200 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529167 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529167&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155515864 440737749 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298324 Cc1cccc2SC(=S)N3CCCN=C3c12 InChI=1S/C12H12N2S2/c1-8-4-2-5-9-10(8)11-13-6-3-7-14(11)12(15)16-9/h2,4-5H,3,6-7H2,1H3 DTQBFVCDRLUECE-UHFFFAOYSA-N 50529155 CHEMBL4553969 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529155 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529155&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 129104138 440737737 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51301871 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acs.jmedchem.8b01825 10.7270/Q20868S8 30629434 Chen, Y; Yuan, X; Zhang, W; Tang, M; Zheng, L; Wang, F; Yan, W; Yang, S; Wei, Y; He, J; Chen, L TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51301887 C[C@@H]1CN(CCO1)C(=O)Nc1ccc(cc1)-c1nc(N2CCOCC2)c2cnn(CCCCCCC(=O)NO)c2n1 InChI=1S/C28H38N8O5/c1-20-19-35(14-17-41-20)28(38)30-22-9-7-21(8-10-22)25-31-26(34-12-15-40-16-13-34)23-18-29-36(27(23)32-25)11-5-3-2-4-6-24(37)33-39/h7-10,18,20,39H,2-6,11-17,19H2,1H3,(H,30,38)(H,33,37)/t20-/m1/s1 YPXRCUVTZDXVHY-HXUWFJFHSA-N 50530002 CHEMBL4532398 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acs.jmedchem.8b01825 10.7270/Q20868S8 30629434 Chen, Y; Yuan, X; Zhang, W; Tang, M; Zheng, L; Wang, F; Yan, W; Yang, S; Wei, Y; He, J; Chen, L TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50530002 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50530002&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137628684 440738584 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51301893 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acs.jmedchem.8b01825 10.7270/Q20868S8 30629434 Chen, Y; Yuan, X; Zhang, W; Tang, M; Zheng, L; Wang, F; Yan, W; Yang, S; Wei, Y; He, J; Chen, L TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298325 Clc1ccc2SC(=S)N3CCCN=C3c2c1 InChI=1S/C11H9ClN2S2/c12-7-2-3-9-8(6-7)10-13-4-1-5-14(10)11(15)16-9/h2-3,6H,1,4-5H2 ZRBHOXHGCHVHRQ-UHFFFAOYSA-N 50529156 CHEMBL4552300 Histone deacetylase 4 Homo sapiens 29000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529156 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529156&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 129104426 440737738 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298326 FC(F)(F)c1ccc2SC(=S)N3CCCN=C3c2c1 InChI=1S/C12H9F3N2S2/c13-12(14,15)7-2-3-9-8(6-7)10-16-4-1-5-17(10)11(18)19-9/h2-3,6H,1,4-5H2 SRNBQQLYBCYORW-UHFFFAOYSA-N 50529171 CHEMBL4579494 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529171 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529171&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 121279020 440737753 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298327 Ic1ccc2SC(=S)N3CCCN=C3c2c1 InChI=1S/C11H9IN2S2/c12-7-2-3-9-8(6-7)10-13-4-1-5-14(10)11(15)16-9/h2-3,6H,1,4-5H2 BZAVJMMRSZOANQ-UHFFFAOYSA-N 50529158 CHEMBL4437805 Histone deacetylase 4 Homo sapiens 8100 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529158 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529158&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155512551 440737740 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298328 Brc1ccc2C3=NCCCN3C(=S)Sc2c1 InChI=1S/C11H9BrN2S2/c12-7-2-3-8-9(6-7)16-11(15)14-5-1-4-13-10(8)14/h2-3,6H,1,4-5H2 CMXWNQQNLFMQSM-UHFFFAOYSA-N 50529145 CHEMBL4457853 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529145 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529145&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 129104183 440737727 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298329 Brc1ccc2SC(=S)N3CCCN=C3c2c1 InChI=1S/C11H9BrN2S2/c12-7-2-3-9-8(6-7)10-13-4-1-5-14(10)11(15)16-9/h2-3,6H,1,4-5H2 OIPZIHODGKWSSX-UHFFFAOYSA-N 50529168 CHEMBL4588346 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529168 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529168&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155567444 440737750 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298330 Brc1cccc2SC(=S)N3CCCN=C3c12 InChI=1S/C11H9BrN2S2/c12-7-3-1-4-8-9(7)10-13-5-2-6-14(10)11(15)16-8/h1,3-4H,2,5-6H2 KUZCOHXDCNJHHJ-UHFFFAOYSA-N 50529135 CHEMBL4464526 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529135 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529135&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 135367138 440737717 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298331 Clc1ccc2C3=NCCCN3C(=S)Sc2c1 InChI=1S/C11H9ClN2S2/c12-7-2-3-8-9(6-7)16-11(15)14-5-1-4-13-10(8)14/h2-3,6H,1,4-5H2 HFTPEFGKDFCIRR-UHFFFAOYSA-N 50529159 CHEMBL4465980 Histone deacetylase 4 Homo sapiens 21000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529159 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529159&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155531452 440737741 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298332 Cc1cccc2C3=NCCCN3C(=S)Sc12 InChI=1S/C12H12N2S2/c1-8-4-2-5-9-10(8)16-12(15)14-7-3-6-13-11(9)14/h2,4-5H,3,6-7H2,1H3 BCZROZPMQANTPH-UHFFFAOYSA-N 50529147 CHEMBL4534843 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529147 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529147&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155549087 440737729 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298333 S=C1Sc2ccccc2C2=NCCCN12 InChI=1S/C11H10N2S2/c14-11-13-7-3-6-12-10(13)8-4-1-2-5-9(8)15-11/h1-2,4-5H,3,6-7H2 NPBNYYVWCOBLJR-UHFFFAOYSA-N 50529172 CHEMBL4589752 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529172 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529172&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44623002 440737754 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298399 COc1ccc2SC(=S)N3CCN=C3c2c1 InChI=1S/C11H10N2OS2/c1-14-7-2-3-9-8(6-7)10-12-4-5-13(10)11(15)16-9/h2-3,6H,4-5H2,1H3 MURRZIYBHPBMJM-UHFFFAOYSA-N 50529150 CHEMBL4529006 Histone deacetylase 4 Homo sapiens 16000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529150 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529150&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155545078 440737732 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298412 Fc1ccc2C3=NCCCN3C(=S)Sc2c1 InChI=1S/C11H9FN2S2/c12-7-2-3-8-9(6-7)16-11(15)14-5-1-4-13-10(8)14/h2-3,6H,1,4-5H2 XDJQLZOPVNEPPF-UHFFFAOYSA-N 50529153 CHEMBL4557077 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529153 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529153&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44623153 440737735 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298437 S=C1Oc2ccccc2C2=NCCCN12 InChI=1S/C11H10N2OS/c15-11-13-7-3-6-12-10(13)8-4-1-2-5-9(8)14-11/h1-2,4-5H,3,6-7H2 HKDJCRDJEKJPFA-UHFFFAOYSA-N 50529174 CHEMBL4525499 Histone deacetylase 4 Homo sapiens 13000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529174 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529174&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 12397856 440737756 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298438 Cc1cccc2SC(=S)N3CCN=C3c12 InChI=1S/C11H10N2S2/c1-7-3-2-4-8-9(7)10-12-5-6-13(10)11(14)15-8/h2-4H,5-6H2,1H3 LBRKPADINYILOC-UHFFFAOYSA-N 50529151 CHEMBL4591317 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529151 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529151&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155568350 440737733 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298439 Cc1ccc2SC(=S)N3CCCN=C3c2c1 InChI=1S/C12H12N2S2/c1-8-3-4-10-9(7-8)11-13-5-2-6-14(11)12(15)16-10/h3-4,7H,2,5-6H2,1H3 VEXIKOBXIPCAHQ-UHFFFAOYSA-N 50529166 CHEMBL4557047 Histone deacetylase 4 Homo sapiens 1900 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529166 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529166&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 121278998 440737748 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298440 Fc1cccc2SC(=S)N3CCCN=C3c12 InChI=1S/C11H9FN2S2/c12-7-3-1-4-8-9(7)10-13-5-2-6-14(10)11(15)16-8/h1,3-4H,2,5-6H2 BTPDQXGJSLTUTC-UHFFFAOYSA-N 50529142 CHEMBL4532057 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529142 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529142&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155546325 440737724 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298454 Clc1cccc2SC(=S)N3CCN=C3c12 InChI=1S/C10H7ClN2S2/c11-6-2-1-3-7-8(6)9-12-4-5-13(9)10(14)15-7/h1-3H,4-5H2 YFMDQWAZZYJLKU-UHFFFAOYSA-N 50529143 CHEMBL4442168 Histone deacetylase 4 Homo sapiens 14000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529143 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529143&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155515284 440737725 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298455 Fc1ccc2SC(=S)N3CCN=C3c2c1 InChI=1S/C10H7FN2S2/c11-6-1-2-8-7(5-6)9-12-3-4-13(9)10(14)15-8/h1-2,5H,3-4H2 DRSAJGBPIBDTMY-UHFFFAOYSA-N 50529169 CHEMBL4442089 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529169 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529169&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155515602 440737751 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298456 Clc1cccc2C3=NCCN3C(=S)Sc12 InChI=1S/C10H7ClN2S2/c11-7-3-1-2-6-8(7)15-10(14)13-5-4-12-9(6)13/h1-3H,4-5H2 CBFKYLOJWRAAHT-UHFFFAOYSA-N 50529170 CHEMBL4469327 Histone deacetylase 4 Homo sapiens 16000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529170 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529170&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 14113325 440737752 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298457 Clc1ccc2SC(=S)N3CCN=C3c2c1 InChI=1S/C10H7ClN2S2/c11-6-1-2-8-7(5-6)9-12-3-4-13(9)10(14)15-8/h1-2,5H,3-4H2 QTUPZKLWJSUPTJ-UHFFFAOYSA-N 50529139 CHEMBL4476731 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529139 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529139&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 129104349 440737721 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298458 S=C1Sc2ccccc2C2=NCCN12 InChI=1S/C10H8N2S2/c13-10-12-6-5-11-9(12)7-3-1-2-4-8(7)14-10/h1-4H,5-6H2 RBWKPQSLRCNQCK-UHFFFAOYSA-N 50529141 CHEMBL4547343 Histone deacetylase 4 Homo sapiens 19000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529141 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529141&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 14113324 440737723 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298459 S=C1Sc2cc(ccc2C2=NCCCN12)C#N InChI=1S/C12H9N3S2/c13-7-8-2-3-9-10(6-8)17-12(16)15-5-1-4-14-11(9)15/h2-3,6H,1,4-5H2 LDZQWDKVBOEJTR-UHFFFAOYSA-N 50529140 CHEMBL4466529 Histone deacetylase 4 Homo sapiens 3800 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529140 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529140&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155531957 440737722 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298460 Cc1ccc2C3=NCCCN3C(=S)Sc2c1 InChI=1S/C12H12N2S2/c1-8-3-4-9-10(7-8)16-12(15)14-6-2-5-13-11(9)14/h3-4,7H,2,5-6H2,1H3 UZLFDAINHMGSAJ-UHFFFAOYSA-N 50529157 CHEMBL4461819 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529157 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529157&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44623152 440737739 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298461 CN(C)c1ccc2C3=NCCCN3C(=S)Sc2c1 InChI=1S/C13H15N3S2/c1-15(2)9-4-5-10-11(8-9)18-13(17)16-7-3-6-14-12(10)16/h4-5,8H,3,6-7H2,1-2H3 UUFSKZQZJPVOEO-UHFFFAOYSA-N 50529173 CHEMBL4576116 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529173 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529173&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 135367789 440737755 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298462 Fc1cccc2C3=NCCCN3C(=S)Sc12 InChI=1S/C11H9FN2S2/c12-8-4-1-3-7-9(8)16-11(15)14-6-2-5-13-10(7)14/h1,3-4H,2,5-6H2 QJICPVISGOAFSU-UHFFFAOYSA-N 50529160 CHEMBL4443377 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529160 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529160&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 129104374 440737742 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51298506 Clc1cccc2C3=NCCCN3C(=S)Sc12 InChI=1S/C11H9ClN2S2/c12-8-4-1-3-7-9(8)16-11(15)14-6-2-5-13-10(7)14/h1,3-4H,2,5-6H2 PINZXEWOUXSNTN-UHFFFAOYSA-N 50529146 CHEMBL4552915 Histone deacetylase 4 Homo sapiens 8800 ChEMBL 10.1016/j.ejmech.2019.111756 10.7270/Q2S185ZR 31630054 Wolff, B; Jänsch, N; Sugiarto, WO; Frühschulz, S; Lang, M; Altintas, R; Oehme, I; Meyer-Almes, FJ University of Applied Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50529146 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50529146&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155555957 440737728 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51288848 C[C@@H](\C=C(/C)\C=C\C(=O)NO)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m0/s1 RTKIYFITIVXBLE-LEJRBOCMSA-N 50525406 CHEMBL164868 Histone deacetylase 4 Homo sapiens 2500 ChEMBL 10.1021/acsmedchemlett.8b00440 10.7270/Q23J3HDS 31223439 Bouchet, S; Linot, C; Ruzic, D; Agbaba, D; Fouchaq, B; Roche, J; Nikolic, K; Blanquart, C; Bertrand, P UMR CNRS 7285 http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50525406 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50525406&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search E1Z 5G0H 13507024 440733988 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51294148 CC[C@H](Nc1ncnc2[nH]cnc12)c1nc2cccc(CNc3ncc(cn3)C(=O)NO)c2c(=O)n1-c1ccccc1 InChI=1S/C28H25N11O3/c1-2-19(36-24-22-23(33-14-32-22)34-15-35-24)25-37-20-10-6-7-16(11-29-28-30-12-17(13-31-28)26(40)38-42)21(20)27(41)39(25)18-8-4-3-5-9-18/h3-10,12-15,19,42H,2,11H2,1H3,(H,38,40)(H,29,30,31)(H2,32,33,34,35,36)/t19-/m0/s1 WJOMMYWEPXHYNA-IBGZPJMESA-N 50527602 CHEMBL4581057 Histone deacetylase 4 Homo sapiens 1428 ChEMBL 10.1021/acs.jmedchem.0c00193 10.7270/Q2KS6W0V 32212730 Thakur, A; Tawa, GJ; Henderson, MJ; Danchik, C; Liu, S; Shah, P; Wang, AQ; Dunn, G; Kabir, M; Padilha, EC; Xu, X; Simeonov, A; Kharbanda, S; Stone, R; Grewal, G National Center for Advancing Translational Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50527602 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50527602&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 142506225 440736184 C02860 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51294149 CC[C@H](Nc1ncnc2[nH]cnc12)c1nc2cccc(CCCCC(=O)NO)c2c(=O)n1-c1ccccc1 InChI=1S/C27H28N8O3/c1-2-19(32-25-23-24(29-15-28-23)30-16-31-25)26-33-20-13-8-10-17(9-6-7-14-21(36)34-38)22(20)27(37)35(26)18-11-4-3-5-12-18/h3-5,8,10-13,15-16,19,38H,2,6-7,9,14H2,1H3,(H,34,36)(H2,28,29,30,31,32)/t19-/m0/s1 FFOIKUZKPAJVBY-IBGZPJMESA-N 50527608 CHEMBL4445342 Histone deacetylase 4 Homo sapiens 70910 ChEMBL 10.1021/acs.jmedchem.0c00193 10.7270/Q2KS6W0V 32212730 Thakur, A; Tawa, GJ; Henderson, MJ; Danchik, C; Liu, S; Shah, P; Wang, AQ; Dunn, G; Kabir, M; Padilha, EC; Xu, X; Simeonov, A; Kharbanda, S; Stone, R; Grewal, G National Center for Advancing Translational Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50527608 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50527608&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 142506033 440736190 C02860 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51294150 CC[C@H](Nc1ncnc2[nH]cnc12)c1nc2cccc(CCCCCC(=O)NO)c2c(=O)n1-c1ccccc1 InChI=1S/C28H30N8O3/c1-2-20(33-26-24-25(30-16-29-24)31-17-32-26)27-34-21-14-9-11-18(10-5-3-8-15-22(37)35-39)23(21)28(38)36(27)19-12-6-4-7-13-19/h4,6-7,9,11-14,16-17,20,39H,2-3,5,8,10,15H2,1H3,(H,35,37)(H2,29,30,31,32,33)/t20-/m0/s1 HQLYDYYQRFGZDZ-FQEVSTJZSA-N 50527619 CHEMBL4451623 Histone deacetylase 4 Homo sapiens 11290 ChEMBL 10.1021/acs.jmedchem.0c00193 10.7270/Q2KS6W0V 32212730 Thakur, A; Tawa, GJ; Henderson, MJ; Danchik, C; Liu, S; Shah, P; Wang, AQ; Dunn, G; Kabir, M; Padilha, EC; Xu, X; Simeonov, A; Kharbanda, S; Stone, R; Grewal, G National Center for Advancing Translational Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50527619 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50527619&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 142506210 440736201 C02860 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51294151 CC[C@H](Nc1ncnc2[nH]cnc12)c1nc2cccc(NCc3ccc(cc3)C(=O)NO)c2c(=O)n1-c1ccccc1 InChI=1S/C30H27N9O3/c1-2-21(36-27-25-26(33-16-32-25)34-17-35-27)28-37-23-10-6-9-22(24(23)30(41)39(28)20-7-4-3-5-8-20)31-15-18-11-13-19(14-12-18)29(40)38-42/h3-14,16-17,21,31,42H,2,15H2,1H3,(H,38,40)(H2,32,33,34,35,36)/t21-/m0/s1 OLUMCBYQNVOFLW-NRFANRHFSA-N 50527627 CHEMBL4516095 Histone deacetylase 4 Homo sapiens 1751 ChEMBL 10.1021/acs.jmedchem.0c00193 10.7270/Q2KS6W0V 32212730 Thakur, A; Tawa, GJ; Henderson, MJ; Danchik, C; Liu, S; Shah, P; Wang, AQ; Dunn, G; Kabir, M; Padilha, EC; Xu, X; Simeonov, A; Kharbanda, S; Stone, R; Grewal, G National Center for Advancing Translational Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50527627 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50527627&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 142506189 440736209 C02860 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51294152 FC(F)(F)c1nc(no1)-c1cccc(c1)C(=O)NCC1(CCOCC1)c1nc(cs1)-c1ccccc1 InChI=1S/C25H21F3N4O3S/c26-25(27,28)22-31-20(32-35-22)17-7-4-8-18(13-17)21(33)29-15-24(9-11-34-12-10-24)23-30-19(14-36-23)16-5-2-1-3-6-16/h1-8,13-14H,9-12,15H2,(H,29,33) HORXBWNTEDOVKN-UHFFFAOYSA-N 50446481 CHEMBL3110004::US10011611, TMP269::US10722597, Compound TMP-269 Histone deacetylase 4 Homo sapiens 244 ChEMBL 10.1021/acs.jmedchem.0c00193 10.7270/Q2KS6W0V 32212730 Thakur, A; Tawa, GJ; Henderson, MJ; Danchik, C; Liu, S; Shah, P; Wang, AQ; Dunn, G; Kabir, M; Padilha, EC; Xu, X; Simeonov, A; Kharbanda, S; Stone, R; Grewal, G National Center for Advancing Translational Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446481 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446481&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search NU9 3ZNR 53344908 194944377 CHEMBL3110004 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51289429 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 30100 ChEMBL 10.1016/j.bmc.2019.07.052 10.7270/Q2VX0KZ8 31431326 Pflieger, M; Hamacher, A; Öz, T; Horstick-Muche, N; Boesen, B; Schrenk, C; Kassack, MU; Kurz, T Heinrich-Heine-University D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51289451 ONC(=O)\C=C\c1ccc(CONC(=O)c2ccc3ccccc3n2)cc1 InChI=1S/C20H17N3O4/c24-19(22-26)12-9-14-5-7-15(8-6-14)13-27-23-20(25)18-11-10-16-3-1-2-4-17(16)21-18/h1-12,26H,13H2,(H,22,24)(H,23,25)/b12-9+ SCYAVNQVZVEEPH-FMIVXFBMSA-N 50525661 CHEMBL4459795 Histone deacetylase 4 Homo sapiens 9540 ChEMBL 10.1016/j.bmc.2019.07.052 10.7270/Q2VX0KZ8 31431326 Pflieger, M; Hamacher, A; Öz, T; Horstick-Muche, N; Boesen, B; Schrenk, C; Kassack, MU; Kurz, T Heinrich-Heine-University D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50525661 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50525661&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155527385 440734243 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51289452 COc1ccc(NC(=O)NOCc2ccc(\C=C\C(=O)NO)cc2)cc1 InChI=1S/C18H19N3O5/c1-25-16-9-7-15(8-10-16)19-18(23)21-26-12-14-4-2-13(3-5-14)6-11-17(22)20-24/h2-11,24H,12H2,1H3,(H,20,22)(H2,19,21,23)/b11-6+ LZFRGGLRIPWNJS-IZZDOVSWSA-N 50525673 CHEMBL4535463 Histone deacetylase 4 Homo sapiens 25200 ChEMBL 10.1016/j.bmc.2019.07.052 10.7270/Q2VX0KZ8 31431326 Pflieger, M; Hamacher, A; Öz, T; Horstick-Muche, N; Boesen, B; Schrenk, C; Kassack, MU; Kurz, T Heinrich-Heine-University D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50525673 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50525673&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155547606 440734255 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51289453 CN1CCc2c(C1)c1ccccc1n2Cc1ccc(cc1)C(=O)NO InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::Tubastatin A::US10227295, Compound Tubastatin A::US10456394, Tubastatin A::US11207431, Example D::US8748451, 6::US9249087, Tubacin::US9751832, Tubastatin A::US9956192, Compound Tubastatin-A Histone deacetylase 4 Homo sapiens 5380 ChEMBL 10.1016/j.bmc.2019.07.052 10.7270/Q2VX0KZ8 31431326 Pflieger, M; Hamacher, A; Öz, T; Horstick-Muche, N; Boesen, B; Schrenk, C; Kassack, MU; Kurz, T Heinrich-Heine-University D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 ZINC51951670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51289454 FC(F)(F)c1nc(no1)-c1cccc(c1)C(=O)NCC1(CCOCC1)c1nc(cs1)-c1ccccc1 InChI=1S/C25H21F3N4O3S/c26-25(27,28)22-31-20(32-35-22)17-7-4-8-18(13-17)21(33)29-15-24(9-11-34-12-10-24)23-30-19(14-36-23)16-5-2-1-3-6-16/h1-8,13-14H,9-12,15H2,(H,29,33) HORXBWNTEDOVKN-UHFFFAOYSA-N 50446481 CHEMBL3110004::US10011611, TMP269::US10722597, Compound TMP-269 Histone deacetylase 4 Homo sapiens 1770 ChEMBL 10.1016/j.bmc.2019.07.052 10.7270/Q2VX0KZ8 31431326 Pflieger, M; Hamacher, A; Öz, T; Horstick-Muche, N; Boesen, B; Schrenk, C; Kassack, MU; Kurz, T Heinrich-Heine-University D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446481 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446481&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search NU9 3ZNR 53344908 194944377 CHEMBL3110004 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51289480 Cc1[nH]c2ccccc2c1CCNCc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C21H23N3O2/c1-15-18(19-4-2-3-5-20(19)23-15)12-13-22-14-17-8-6-16(7-9-17)10-11-21(25)24-26/h2-11,22-23,26H,12-14H2,1H3,(H,24,25)/b11-10+ FPOHNWQLNRZRFC-ZHACJKMWSA-N 29589 Faridak::LBH-589::LBH-589B::Panobinostat::US10722597, Compound Panobinostat Histone deacetylase 4 Homo sapiens 640 ChEMBL 10.1016/j.bmc.2019.07.052 10.7270/Q2VX0KZ8 31431326 Pflieger, M; Hamacher, A; Öz, T; Horstick-Muche, N; Boesen, B; Schrenk, C; Kassack, MU; Kurz, T Heinrich-Heine-University D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=29589 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=29589&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search LBH 5EF8 6918837 81055018 ZINC22010649 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51289482 CCCCN(Cc1ccc(cc1)C(=O)NO)C(=O)Nc1ccccc1 InChI=1S/C19H23N3O3/c1-2-3-13-22(19(24)20-17-7-5-4-6-8-17)14-15-9-11-16(12-10-15)18(23)21-25/h4-12,25H,2-3,13-14H2,1H3,(H,20,24)(H,21,23) JZWXMCPARMXZQV-UHFFFAOYSA-N 50398716 CHEMBL2179618::US10227295, Compound 5g::US9409858, 5g::US9751832, Compound 5g::US9956192, Compound 5g Histone deacetylase 4 Homo sapiens 7570 ChEMBL 10.1016/j.bmc.2019.07.052 10.7270/Q2VX0KZ8 31431326 Pflieger, M; Hamacher, A; Öz, T; Horstick-Muche, N; Boesen, B; Schrenk, C; Kassack, MU; Kurz, T Heinrich-Heine-University D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50398716 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50398716&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N4R 5G0J,5G0I 71462653 163347740 CHEMBL2179618 ZINC95573398 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 940390 CC(O)COC[C@H]1O[C@@H]2O[C@@H]3[C@@H](COCC(C)O)O[C@H](O[C@@H]4[C@@H](COCC(C)O)O[C@H](O[C@@H]5[C@@H](COCC(C)O)O[C@H](O[C@@H]6[C@@H](COCC(C)O)O[C@H](O[C@@H]7[C@@H](COCC(C)O)O[C@H](O[C@@H]8[C@@H](COCC(C)O)O[C@H](O[C@H]1[C@@H](O)[C@@H]2O)[C@@H](O)[C@@H]8O)[C@@H](O)[C@@H]7O)[C@@H](O)[C@@H]6O)[C@@H](O)[C@@H]5O)[C@@H](O)[C@@H]4O)[C@@H](O)[C@@H]3O InChI=1S/C63H112O42/c1-22(64)8-85-15-29-50-36(71)43(78)57(92-29)100-51-30(16-86-9-23(2)65)94-59(45(80)38(51)73)102-53-32(18-88-11-25(4)67)96-61(47(82)40(53)75)104-55-34(20-90-13-27(6)69)98-63(49(84)42(55)77)105-56-35(21-91-14-28(7)70)97-62(48(83)41(56)76)103-54-33(19-89-12-26(5)68)95-60(46(81)39(54)74)101-52-31(17-87-10-24(3)66)93-58(99-50)44(79)37(52)72/h22-84H,8-21H2,1-7H3/t22?,23?,24?,25?,26?,27?,28?,29-,30-,31-,32-,33-,34-,35-,36+,37+,38+,39+,40+,41+,42+,43+,44+,45+,46+,47+,48+,49+,50-,51-,52-,53-,54-,55-,56-,57-,58-,59-,60-,61-,62-,63-/m1/s1 ODLHGICHYURWBS-LMNZQWFYSA-N 455844 US10722597, Compound HP-beta-CD Histone deacetylase 4 Homo sapiens 567 US Patent 10.7270/Q2G44TB8 aid1804665 US10722597 Coulter, T; Damment, S; Pace, A; Palmer, D MIDATECH LTD. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=455844 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=455844&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 138319308 440971647 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 940394 Cc1[nH]c2ccccc2c1CCNCc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C21H23N3O2/c1-15-18(19-4-2-3-5-20(19)23-15)12-13-22-14-17-8-6-16(7-9-17)10-11-21(25)24-26/h2-11,22-23,26H,12-14H2,1H3,(H,24,25)/b11-10+ FPOHNWQLNRZRFC-ZHACJKMWSA-N 29589 Faridak::LBH-589::LBH-589B::Panobinostat::US10722597, Compound Panobinostat Histone deacetylase 4 Homo sapiens 1550 US Patent 10.7270/Q2G44TB8 aid1804665 US10722597 Coulter, T; Damment, S; Pace, A; Palmer, D MIDATECH LTD. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=29589 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=29589&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search LBH 5EF8 6918837 81055018 ZINC22010649 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 940398 FC(F)(F)c1nc(no1)-c1cccc(c1)C(=O)NCC1(CCOCC1)c1nc(cs1)-c1ccccc1 InChI=1S/C25H21F3N4O3S/c26-25(27,28)22-31-20(32-35-22)17-7-4-8-18(13-17)21(33)29-15-24(9-11-34-12-10-24)23-30-19(14-36-23)16-5-2-1-3-6-16/h1-8,13-14H,9-12,15H2,(H,29,33) HORXBWNTEDOVKN-UHFFFAOYSA-N 50446481 CHEMBL3110004::US10011611, TMP269::US10722597, Compound TMP-269 Histone deacetylase 4 Homo sapiens 376 US Patent 10.7270/Q2G44TB8 aid1804665 US10722597 Coulter, T; Damment, S; Pace, A; Palmer, D MIDATECH LTD. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446481 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446481&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search NU9 3ZNR 53344908 194944377 CHEMBL3110004 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51333308 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acsmedchemlett.9b00561 10.7270/Q26M3BCW 32435375 Rangasamy, L; Ortín, I; Zapico, JM; Coderch, C; Ramos, A; de Pascual-Teresa, B Universidad San Pablo-CEU http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51331801 COc1cc(cc(OC)c1OC)C(=O)NOCCCCCC(=O)NO InChI=1S/C16H24N2O7/c1-22-12-9-11(10-13(23-2)15(12)24-3)16(20)18-25-8-6-4-5-7-14(19)17-21/h9-10,21H,4-8H2,1-3H3,(H,17,19)(H,18,20) WSFZAZKSARVIJQ-UHFFFAOYSA-N 50538984 CHEMBL4643795 Histone deacetylase 4 Homo sapiens 93100 ChEMBL 10.1016/j.bmc.2019.115108 10.7270/Q2NV9NSQ 31787463 Asfaha, Y; Schrenk, C; Alves Avelar, LA; Lange, F; Wang, C; Bandolik, JJ; Hamacher, A; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50538984 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50538984&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 156018790 442140547 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51331802 CC(C)(C)c1cc(cc(c1)C(C)(C)C)C(=O)NOCCCCCC(=O)NO InChI=1S/C21H34N2O4/c1-20(2,3)16-12-15(13-17(14-16)21(4,5)6)19(25)23-27-11-9-7-8-10-18(24)22-26/h12-14,26H,7-11H2,1-6H3,(H,22,24)(H,23,25) PCYKSKSJYJIDFL-UHFFFAOYSA-N 50538985 CHEMBL4645307 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmc.2019.115108 10.7270/Q2NV9NSQ 31787463 Asfaha, Y; Schrenk, C; Alves Avelar, LA; Lange, F; Wang, C; Bandolik, JJ; Hamacher, A; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50538985 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50538985&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 156018382 442140548 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51331803 ONC(=O)CCCCCONC(=O)c1cc(F)cc(F)c1 InChI=1S/C13H16F2N2O4/c14-10-6-9(7-11(15)8-10)13(19)17-21-5-3-1-2-4-12(18)16-20/h6-8,20H,1-5H2,(H,16,18)(H,17,19) JLMGVUDRUZZHQL-UHFFFAOYSA-N 50538986 CHEMBL4638555 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmc.2019.115108 10.7270/Q2NV9NSQ 31787463 Asfaha, Y; Schrenk, C; Alves Avelar, LA; Lange, F; Wang, C; Bandolik, JJ; Hamacher, A; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50538986 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50538986&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 156011728 442140549 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51331804 COc1cc(OC)cc(c1)C(=O)NOCCCCCC(=O)NO InChI=1S/C15H22N2O6/c1-21-12-8-11(9-13(10-12)22-2)15(19)17-23-7-5-3-4-6-14(18)16-20/h8-10,20H,3-7H2,1-2H3,(H,16,18)(H,17,19) WARMWIVORGODLX-UHFFFAOYSA-N 50538987 CHEMBL4645688 Histone deacetylase 4 Homo sapiens 49200 ChEMBL 10.1016/j.bmc.2019.115108 10.7270/Q2NV9NSQ 31787463 Asfaha, Y; Schrenk, C; Alves Avelar, LA; Lange, F; Wang, C; Bandolik, JJ; Hamacher, A; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50538987 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50538987&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 156019761 442140550 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51331805 ONC(=O)CCCCCONC(=O)c1cc(cc(c1)C(F)(F)F)C(F)(F)F InChI=1S/C15H16F6N2O4/c16-14(17,18)10-6-9(7-11(8-10)15(19,20)21)13(25)23-27-5-3-1-2-4-12(24)22-26/h6-8,26H,1-5H2,(H,22,24)(H,23,25) MDCKZAKVNQPMGB-UHFFFAOYSA-N 50538988 CHEMBL4638018 Histone deacetylase 4 Homo sapiens 83700 ChEMBL 10.1016/j.bmc.2019.115108 10.7270/Q2NV9NSQ 31787463 Asfaha, Y; Schrenk, C; Alves Avelar, LA; Lange, F; Wang, C; Bandolik, JJ; Hamacher, A; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50538988 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50538988&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 156012703 442140551 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51331806 ONC(=O)CCCCCONC(=O)c1cc(Br)cc(Br)c1 InChI=1S/C13H16Br2N2O4/c14-10-6-9(7-11(15)8-10)13(19)17-21-5-3-1-2-4-12(18)16-20/h6-8,20H,1-5H2,(H,16,18)(H,17,19) OMDYXKRBVJJEEK-UHFFFAOYSA-N 50538989 CHEMBL4639388 Histone deacetylase 4 Homo sapiens 31800 ChEMBL 10.1016/j.bmc.2019.115108 10.7270/Q2NV9NSQ 31787463 Asfaha, Y; Schrenk, C; Alves Avelar, LA; Lange, F; Wang, C; Bandolik, JJ; Hamacher, A; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50538989 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50538989&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 156013281 442140552 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51331807 ONC(=O)CCCCCONC(=O)c1cc(I)cc(I)c1I InChI=1S/C13H15I3N2O4/c14-8-6-9(12(16)10(15)7-8)13(20)18-22-5-3-1-2-4-11(19)17-21/h6-7,21H,1-5H2,(H,17,19)(H,18,20) NTYOIGBEMWFXEN-UHFFFAOYSA-N 50538990 CHEMBL4636427 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmc.2019.115108 10.7270/Q2NV9NSQ 31787463 Asfaha, Y; Schrenk, C; Alves Avelar, LA; Lange, F; Wang, C; Bandolik, JJ; Hamacher, A; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50538990 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50538990&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 156012735 442140553 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51331808 ONC(=O)CCCCCONC(=O)c1c(Cl)cncc1Cl InChI=1S/C12H15Cl2N3O4/c13-8-6-15-7-9(14)11(8)12(19)17-21-5-3-1-2-4-10(18)16-20/h6-7,20H,1-5H2,(H,16,18)(H,17,19) HKGUNQCCAGITDN-UHFFFAOYSA-N 50538991 CHEMBL4635256 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmc.2019.115108 10.7270/Q2NV9NSQ 31787463 Asfaha, Y; Schrenk, C; Alves Avelar, LA; Lange, F; Wang, C; Bandolik, JJ; Hamacher, A; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50538991 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50538991&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 156014007 442140554 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51331809 Cc1cc(C)cc(c1)C(=O)NOCCCCC(=O)NO InChI=1S/C14H20N2O4/c1-10-7-11(2)9-12(8-10)14(18)16-20-6-4-3-5-13(17)15-19/h7-9,19H,3-6H2,1-2H3,(H,15,17)(H,16,18) IOASXSSMHGWLRP-UHFFFAOYSA-N 50538992 CHEMBL4643138 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmc.2019.115108 10.7270/Q2NV9NSQ 31787463 Asfaha, Y; Schrenk, C; Alves Avelar, LA; Lange, F; Wang, C; Bandolik, JJ; Hamacher, A; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50538992 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50538992&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 156018398 442140555 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51331810 Cc1cc(C)cc(c1)C(=O)NOCCCCCC(=O)NO InChI=1S/C15H22N2O4/c1-11-8-12(2)10-13(9-11)15(19)17-21-7-5-3-4-6-14(18)16-20/h8-10,20H,3-7H2,1-2H3,(H,16,18)(H,17,19) VRYZCEONIWEUAV-UHFFFAOYSA-N 50424996 CHEMBL2312168 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.bmc.2019.115108 10.7270/Q2NV9NSQ 31787463 Asfaha, Y; Schrenk, C; Alves Avelar, LA; Lange, F; Wang, C; Bandolik, JJ; Hamacher, A; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50424996 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50424996&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71520717 164153871 CHEMBL2312168 ZINC95593440 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51331811 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 28400 ChEMBL 10.1016/j.bmc.2019.115108 10.7270/Q2NV9NSQ 31787463 Asfaha, Y; Schrenk, C; Alves Avelar, LA; Lange, F; Wang, C; Bandolik, JJ; Hamacher, A; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51331812 ONC(=O)C(c1ccc(cc1)-c1ncc(cn1)C(F)(F)F)c1ccccc1F InChI=1S/C19H13F4N3O2/c20-15-4-2-1-3-14(15)16(18(27)26-28)11-5-7-12(8-6-11)17-24-9-13(10-25-17)19(21,22)23/h1-10,16,28H,(H,26,27) LMGDHGQJJLEAPQ-UHFFFAOYSA-N 50503690 CHEMBL4456445 Histone deacetylase 4 Homo sapiens 170 ChEMBL 10.1016/j.bmc.2019.115108 10.7270/Q2NV9NSQ 31787463 Asfaha, Y; Schrenk, C; Alves Avelar, LA; Lange, F; Wang, C; Bandolik, JJ; Hamacher, A; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503690 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503690&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 81689842 440712275 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51344712 CN1CC(C1)C(=O)N[C@@H](CCCCCC(=O)c1ccon1)c1ncc([nH]1)-c1ccccc1F 50544211 CHEMBL4641682 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1021/acsmedchemlett.0c00302 10.7270/Q2RV0S85 32676157 Liu, J; Kelly, J; Yu, W; Clausen, D; Yu, Y; Kim, H; Duffy, JL; Chung, CC; Myers, RW; Carroll, S; Klein, DJ; Fells, J; Holloway, MK; Wu, J; Wu, G; Howell, BJ; Barnard, RJO; Kozlowski, JA Merck & Co. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50544211 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50544211&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 146317294 442145774 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51339490 CC(C)N(C(=O)c1cc(cc(c1)C(F)(F)F)C(F)(F)F)c1ccc(cc1)C(=O)NO InChI=1S/C19H16F6N2O3/c1-10(2)27(15-5-3-11(4-6-15)16(28)26-30)17(29)12-7-13(18(20,21)22)9-14(8-12)19(23,24)25/h3-10,30H,1-2H3,(H,26,28) JVCQXJCACOCTST-UHFFFAOYSA-N 50542229 CHEMBL4642821 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.0c01025 10.7270/Q2CC1470 32672458 Hassan, MM; Israelian, J; Nawar, N; Ganda, G; Manaswiyoungkul, P; Raouf, YS; Armstrong, D; Sedighi, A; Olaoye, OO; Erdogan, F; Cabral, AD; Angeles, F; Altintas, R; de Araujo, ED; Gunning, PT University of Toronto Mississauga http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50542229 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50542229&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 156016331 442143792 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51339491 COc1ccc(Cn2ccc3ccc(cc23)C(=O)NO)cc1 InChI=1S/C17H16N2O3/c1-22-15-6-2-12(3-7-15)11-19-9-8-13-4-5-14(10-16(13)19)17(20)18-21/h2-10,21H,11H2,1H3,(H,18,20) AJRGHIGYPXNABY-UHFFFAOYSA-N 50397360 CHEMBL2170177::US10188756, Compound CN110 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.0c01025 10.7270/Q2CC1470 32672458 Hassan, MM; Israelian, J; Nawar, N; Ganda, G; Manaswiyoungkul, P; Raouf, YS; Armstrong, D; Sedighi, A; Olaoye, OO; Erdogan, F; Cabral, AD; Angeles, F; Altintas, R; de Araujo, ED; Gunning, PT University of Toronto Mississauga http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50397360 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50397360&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search GKW 6HQY,6HSF 24753719 163346384 CHEMBL2170177 ZINC43178454 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51345092 O=C(NC(c1ccccc1)c1ccccc1)c1cc(nc2ccccc12)-c1cc2ccccc2o1 InChI=1S/C31H22N2O2/c34-31(33-30(21-11-3-1-4-12-21)22-13-5-2-6-14-22)25-20-27(32-26-17-9-8-16-24(25)26)29-19-23-15-7-10-18-28(23)35-29/h1-20,30H,(H,33,34) JNULQPRWYHVXHT-UHFFFAOYSA-N 50544391 CHEMBL4636189 Histone deacetylase 4 Homo sapiens >200000 ChEMBL 10.1021/acs.jmedchem.0c01183 10.7270/Q20C50C7 32787077 Chen, X; Sun, W; Huang, S; Zhang, H; Lin, G; Li, H; Qiao, J; Li, L; Yang, S Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50544391 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50544391&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 156013743 442145954 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51344072 CN1CCN(CC1)c1ccc(c(N)c1)[N+]([O-])=O InChI=1S/C11H16N4O2/c1-13-4-6-14(7-5-13)9-2-3-11(15(16)17)10(12)8-9/h2-3,8H,4-7,12H2,1H3 MWLBMGPQZJDFKZ-UHFFFAOYSA-N 50544037 CHEMBL1370863 Histone deacetylase 4 Homo sapiens >200000 ChEMBL 10.1016/j.bmcl.2020.127215 10.7270/Q2VT1WN9 32631504 Sun, W; Chen, X; Huang, S; Li, W; Tian, C; Yang, S; Li, L Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50544037 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50544037&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 2760034 442145600 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51336128 Cc1cc(C(=O)NCc2c(C)cc(C)[nH]c2=O)c(C)n1-c1cccc(NC(=O)CCCCCCC(=O)NO)c1 InChI=1S/C29H37N5O5/c1-18-14-19(2)31-29(38)25(18)17-30-28(37)24-15-20(3)34(21(24)4)23-11-9-10-22(16-23)32-26(35)12-7-5-6-8-13-27(36)33-39/h9-11,14-16,39H,5-8,12-13,17H2,1-4H3,(H,30,37)(H,31,38)(H,32,35)(H,33,36) HQAHZUWVVKNTRB-UHFFFAOYSA-N 50540803 CHEMBL4633299 Histone deacetylase 4 Homo sapiens 36800 ChEMBL 10.1021/acsmedchemlett.0c00014 10.7270/Q2HM5D0B 32435414 Romanelli, A; Stazi, G; Fioravanti, R; Zwergel, C; Di Bello, E; Pomella, S; Perrone, C; Battistelli, C; Strippoli, R; Tripodi, M; Del Bufalo, D; Rota, R; Trisciuoglio, D; Mai, A; Valente, S Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50540803 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50540803&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 156010365 442142366 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51336129 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 490 ChEMBL 10.1021/acsmedchemlett.0c00014 10.7270/Q2HM5D0B 32435414 Romanelli, A; Stazi, G; Fioravanti, R; Zwergel, C; Di Bello, E; Pomella, S; Perrone, C; Battistelli, C; Strippoli, R; Tripodi, M; Del Bufalo, D; Rota, R; Trisciuoglio, D; Mai, A; Valente, S Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51393750 ONC(=O)c1ccc(CN2C(=O)c3ccccc3C2=O)cc1-c1ccccc1 InChI=1S/C22H16N2O4/c25-20(23-28)16-11-10-14(12-19(16)15-6-2-1-3-7-15)13-24-21(26)17-8-4-5-9-18(17)22(24)27/h1-12,28H,13H2,(H,23,25) ONODKKVQHKQFFX-UHFFFAOYSA-N 50563273 CHEMBL4748500 Histone deacetylase 4 Homo sapiens 28 ChEMBL 10.1021/acs.jmedchem.0c01967 10.7270/Q2DV1PMP 33570940 Mak, JYW; Wu, KC; Gupta, PK; Barbero, S; McLaughlin, MG; Lucke, AJ; Tng, J; Lim, J; Loh, Z; Sweet, MJ; Reid, RC; Liu, L; Fairlie, DP The University of Queensland http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50563273 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50563273&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162649913 461683611 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51393751 ONC(=O)c1ccc(CN2C(=O)c3cccc(F)c3C2=O)cc1-c1ccccc1 InChI=1S/C22H15FN2O4/c23-18-8-4-7-16-19(18)22(28)25(21(16)27)12-13-9-10-15(20(26)24-29)17(11-13)14-5-2-1-3-6-14/h1-11,29H,12H2,(H,24,26) YSAJLBSZOVKZCD-UHFFFAOYSA-N 50563274 CHEMBL4799406 Histone deacetylase 4 Homo sapiens 13 ChEMBL 10.1021/acs.jmedchem.0c01967 10.7270/Q2DV1PMP 33570940 Mak, JYW; Wu, KC; Gupta, PK; Barbero, S; McLaughlin, MG; Lucke, AJ; Tng, J; Lim, J; Loh, Z; Sweet, MJ; Reid, RC; Liu, L; Fairlie, DP The University of Queensland http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50563274 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50563274&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162676442 461683612 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51393752 ONC(=O)c1ccc(CN2C(=O)c3ccccc3S2(=O)=O)cc1-c1ccccc1 InChI=1S/C21H16N2O5S/c24-20(22-26)16-11-10-14(12-18(16)15-6-2-1-3-7-15)13-23-21(25)17-8-4-5-9-19(17)29(23,27)28/h1-12,26H,13H2,(H,22,24) XYLVZKXNIYAIQC-UHFFFAOYSA-N 50563275 CHEMBL4761013 Histone deacetylase 4 Homo sapiens 49 ChEMBL 10.1021/acs.jmedchem.0c01967 10.7270/Q2DV1PMP 33570940 Mak, JYW; Wu, KC; Gupta, PK; Barbero, S; McLaughlin, MG; Lucke, AJ; Tng, J; Lim, J; Loh, Z; Sweet, MJ; Reid, RC; Liu, L; Fairlie, DP The University of Queensland http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50563275 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50563275&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162660277 461683613 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51393753 CC(C)(CNC(=O)c1cccc(c1)-c1noc(n1)C(F)(F)F)c1coc(n1)-c1ccccc1 InChI=1S/C23H19F3N4O3/c1-22(2,17-12-32-20(28-17)14-7-4-3-5-8-14)13-27-19(31)16-10-6-9-15(11-16)18-29-21(33-30-18)23(24,25)26/h3-12H,13H2,1-2H3,(H,27,31) QTCSXAUJBQZZSN-UHFFFAOYSA-N 50563276 CHEMBL4751615 Histone deacetylase 4 Homo sapiens 354 ChEMBL 10.1021/acs.jmedchem.0c01967 10.7270/Q2DV1PMP 33570940 Mak, JYW; Wu, KC; Gupta, PK; Barbero, S; McLaughlin, MG; Lucke, AJ; Tng, J; Lim, J; Loh, Z; Sweet, MJ; Reid, RC; Liu, L; Fairlie, DP The University of Queensland http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50563276 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50563276&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 67324851 461683614 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51391759 CC(C)Oc1ccc(cc1-c1cn(C)c(=O)c2[nH]c(cc12)C(=O)NCc1ccc(cc1)C(=O)Nc1ccccc1N)C(C)(C)O InChI=1S/C35H37N5O5/c1-20(2)45-30-15-14-23(35(3,4)44)16-24(30)26-19-40(5)34(43)31-25(26)17-29(38-31)33(42)37-18-21-10-12-22(13-11-21)32(41)39-28-9-7-6-8-27(28)36/h6-17,19-20,38,44H,18,36H2,1-5H3,(H,37,42)(H,39,41) SFYLADBQGNFSOV-UHFFFAOYSA-N 50562298 CHEMBL4747126 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2020.112868 10.7270/Q26M3BJ4 33077265 Chen, J; Li, Y; Zhang, J; Zhang, M; Wei, A; Liu, H; Xie, Z; Ren, W; Duan, W; Zhang, Z; Shen, A; Hu, Y Shanghai Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50562298 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50562298&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155431223 461832690 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51391760 CC(C)Oc1ccc(cc1-c1cn(C)c(=O)c2[nH]c(cc12)C(=O)NCCCCCCC(=O)NO)C(C)(C)O InChI=1S/C28H38N4O6/c1-17(2)38-23-12-11-18(28(3,4)36)14-19(23)21-16-32(5)27(35)25-20(21)15-22(30-25)26(34)29-13-9-7-6-8-10-24(33)31-37/h11-12,14-17,30,36-37H,6-10,13H2,1-5H3,(H,29,34)(H,31,33) ZPZTZOURCDUBLM-UHFFFAOYSA-N 50562307 CHEMBL4755061 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2020.112868 10.7270/Q26M3BJ4 33077265 Chen, J; Li, Y; Zhang, J; Zhang, M; Wei, A; Liu, H; Xie, Z; Ren, W; Duan, W; Zhang, Z; Shen, A; Hu, Y Shanghai Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50562307 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50562307&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155431440 461832699 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51391761 Cc1cc(F)cc(C)c1Oc1ccc(cc1-c1cn(C)c(=O)c2[nH]c(cc12)C(=O)NCCCCCCC(=O)NO)C(C)(C)O InChI=1S/C33H39FN4O6/c1-19-14-22(34)15-20(2)30(19)44-27-12-11-21(33(3,4)42)16-23(27)25-18-38(5)32(41)29-24(25)17-26(36-29)31(40)35-13-9-7-6-8-10-28(39)37-43/h11-12,14-18,36,42-43H,6-10,13H2,1-5H3,(H,35,40)(H,37,39) OEMGJZQIDXYGFV-UHFFFAOYSA-N 50562310 CHEMBL4794499 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2020.112868 10.7270/Q26M3BJ4 33077265 Chen, J; Li, Y; Zhang, J; Zhang, M; Wei, A; Liu, H; Xie, Z; Ren, W; Duan, W; Zhang, Z; Shen, A; Hu, Y Shanghai Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50562310 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50562310&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155431228 461832702 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51391762 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2020.112868 10.7270/Q26M3BJ4 33077265 Chen, J; Li, Y; Zhang, J; Zhang, M; Wei, A; Liu, H; Xie, Z; Ren, W; Duan, W; Zhang, Z; Shen, A; Hu, Y Shanghai Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51388332 ONC(=O)c1ccc(CN(Cc2nnnn2Cc2ccccc2)C(=O)c2ccccc2C(F)(F)F)cc1 InChI=1S/C25H21F3N6O3/c26-25(27,28)21-9-5-4-8-20(21)24(36)33(14-18-10-12-19(13-11-18)23(35)30-37)16-22-29-31-32-34(22)15-17-6-2-1-3-7-17/h1-13,37H,14-16H2,(H,30,35) MEWDNULKAXEKII-UHFFFAOYSA-N 50560884 CHEMBL4800426 Histone deacetylase 4 Homo sapiens 55400 ChEMBL 10.1021/acs.jmedchem.9b01888 10.7270/Q2T157C4 32803970 Reßing, N; Sönnichsen, M; Osko, JD; Schöler, A; Schliehe-Diecks, J; Skerhut, A; Borkhardt, A; Hauer, J; Kassack, MU; Christianson, DW; Bhatia, S; Hansen, FK Leipzig University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50560884 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50560884&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search P5Y 6PYE 146680839 461831276 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51388333 Cc1[nH]c2ccccc2c1CCNCc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C21H23N3O2/c1-15-18(19-4-2-3-5-20(19)23-15)12-13-22-14-17-8-6-16(7-9-17)10-11-21(25)24-26/h2-11,22-23,26H,12-14H2,1H3,(H,24,25)/b11-10+ FPOHNWQLNRZRFC-ZHACJKMWSA-N 29589 Faridak::LBH-589::LBH-589B::Panobinostat::US10722597, Compound Panobinostat Histone deacetylase 4 Homo sapiens 480 ChEMBL 10.1021/acs.jmedchem.9b01888 10.7270/Q2T157C4 32803970 Reßing, N; Sönnichsen, M; Osko, JD; Schöler, A; Schliehe-Diecks, J; Skerhut, A; Borkhardt, A; Hauer, J; Kassack, MU; Christianson, DW; Bhatia, S; Hansen, FK Leipzig University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=29589 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=29589&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search LBH 5EF8 6918837 81055018 ZINC22010649 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51388432 NCc1ccc(NC(=O)N(CCCCO)Cc2ccc(cc2)C(=O)NO)cc1 InChI=1S/C20H26N4O4/c21-13-15-5-9-18(10-6-15)22-20(27)24(11-1-2-12-25)14-16-3-7-17(8-4-16)19(26)23-28/h3-10,25,28H,1-2,11-14,21H2,(H,22,27)(H,23,26) VTRGFHYHEAEHGS-UHFFFAOYSA-N 50560908 CHEMBL4777296 Histone deacetylase 4 Homo sapiens 8250 ChEMBL 10.1021/acs.jmedchem.0c00567 10.7270/Q2JH3QW7 32815366 Noonepalle, S; Shen, S; Ptáček, J; Tavares, MT; Zhang, G; Stránský, J; Pavlíček, J; Ferreira, GM; Hadley, M; Pelaez, G; Bařinka, C; Kozikowski, AP; Villagra, A The George Washington University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50560908 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50560908&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N28 6TCY 154699463 461831300 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51388433 CCCCN(Cc1ccc(cc1)C(=O)NO)C(=O)Nc1ccc(CN)cc1 InChI=1S/C20H26N4O3/c1-2-3-12-24(14-16-4-8-17(9-5-16)19(25)23-27)20(26)22-18-10-6-15(13-21)7-11-18/h4-11,27H,2-3,12-14,21H2,1H3,(H,22,26)(H,23,25) GESBEDAZDXKNGG-UHFFFAOYSA-N 50560909 CHEMBL4759584 Histone deacetylase 4 Homo sapiens 23100 ChEMBL 10.1021/acs.jmedchem.0c00567 10.7270/Q2JH3QW7 32815366 Noonepalle, S; Shen, S; Ptáček, J; Tavares, MT; Zhang, G; Stránský, J; Pavlíček, J; Ferreira, GM; Hadley, M; Pelaez, G; Bařinka, C; Kozikowski, AP; Villagra, A The George Washington University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50560909 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50560909&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162657468 461831301 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51388434 OCCCCN(Cc1ccc(cc1)C(=O)NO)C(=O)Nc1ccccc1 InChI=1S/C19H23N3O4/c23-13-5-4-12-22(19(25)20-17-6-2-1-3-7-17)14-15-8-10-16(11-9-15)18(24)21-26/h1-3,6-11,23,26H,4-5,12-14H2,(H,20,25)(H,21,24) PDBSLDBGQHDGCM-UHFFFAOYSA-N 50279258 CHEMBL4177129 Histone deacetylase 4 Homo sapiens 14000 ChEMBL 10.1021/acs.jmedchem.0c00567 10.7270/Q2JH3QW7 32815366 Noonepalle, S; Shen, S; Ptáček, J; Tavares, MT; Zhang, G; Stránský, J; Pavlíček, J; Ferreira, GM; Hadley, M; Pelaez, G; Bařinka, C; Kozikowski, AP; Villagra, A The George Washington University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50279258 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50279258&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 145971506 406793669 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51388435 CCCCN(Cc1ccc(cc1)C(=O)NO)C(=O)Nc1ccccc1 InChI=1S/C19H23N3O3/c1-2-3-13-22(19(24)20-17-7-5-4-6-8-17)14-15-9-11-16(12-10-15)18(23)21-25/h4-12,25H,2-3,13-14H2,1H3,(H,20,24)(H,21,23) JZWXMCPARMXZQV-UHFFFAOYSA-N 50398716 CHEMBL2179618::US10227295, Compound 5g::US9409858, 5g::US9751832, Compound 5g::US9956192, Compound 5g Histone deacetylase 4 Homo sapiens 14800 ChEMBL 10.1021/acs.jmedchem.0c00567 10.7270/Q2JH3QW7 32815366 Noonepalle, S; Shen, S; Ptáček, J; Tavares, MT; Zhang, G; Stránský, J; Pavlíček, J; Ferreira, GM; Hadley, M; Pelaez, G; Bařinka, C; Kozikowski, AP; Villagra, A The George Washington University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50398716 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50398716&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N4R 5G0J,5G0I 71462653 163347740 CHEMBL2179618 ZINC95573398 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51364605 ONC(=O)c1ccc(Nc2c3ccccc3nc3ccccc23)cc1 InChI=1S/C20H15N3O2/c24-20(23-25)13-9-11-14(12-10-13)21-19-15-5-1-3-7-17(15)22-18-8-4-2-6-16(18)19/h1-12,25H,(H,21,22)(H,23,24) HYCPLKOVNZFNAS-UHFFFAOYSA-N 50551540 CHEMBL4762873 Histone deacetylase 4 Homo sapiens 2240 ChEMBL 10.1016/j.ejmech.2020.112193 10.7270/Q2FX7F3B 32151835 Tseng, HJ; Lin, MH; Shiao, YJ; Yang, YC; Chu, JC; Chen, CY; Chen, YY; Lin, TE; Su, CJ; Pan, SL; Chen, LC; Wang, CY; Hsu, KC; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50551540 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50551540&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162660161 461681880 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51364606 ONC(=O)Cc1ccc(Nc2c3ccccc3nc3ccccc23)cc1 InChI=1S/C21H17N3O2/c25-20(24-26)13-14-9-11-15(12-10-14)22-21-16-5-1-3-7-18(16)23-19-8-4-2-6-17(19)21/h1-12,26H,13H2,(H,22,23)(H,24,25) QSJDYSVPIFWJMO-UHFFFAOYSA-N 50551541 CHEMBL4757768 Histone deacetylase 4 Homo sapiens 26630 ChEMBL 10.1016/j.ejmech.2020.112193 10.7270/Q2FX7F3B 32151835 Tseng, HJ; Lin, MH; Shiao, YJ; Yang, YC; Chu, JC; Chen, CY; Chen, YY; Lin, TE; Su, CJ; Pan, SL; Chen, LC; Wang, CY; Hsu, KC; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50551541 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50551541&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162656816 461681881 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51364607 ONC(=O)c1ccc(Nc2c3ccccc3nc3ccc(F)cc23)cc1 InChI=1S/C20H14FN3O2/c21-13-7-10-18-16(11-13)19(15-3-1-2-4-17(15)23-18)22-14-8-5-12(6-9-14)20(25)24-26/h1-11,26H,(H,22,23)(H,24,25) FNXJKKUKSKUSPD-UHFFFAOYSA-N 50551543 CHEMBL4757035 Histone deacetylase 4 Homo sapiens 3040 ChEMBL 10.1016/j.ejmech.2020.112193 10.7270/Q2FX7F3B 32151835 Tseng, HJ; Lin, MH; Shiao, YJ; Yang, YC; Chu, JC; Chen, CY; Chen, YY; Lin, TE; Su, CJ; Pan, SL; Chen, LC; Wang, CY; Hsu, KC; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50551543 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50551543&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162656473 461681883 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51364608 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 33040 ChEMBL 10.1016/j.ejmech.2020.112193 10.7270/Q2FX7F3B 32151835 Tseng, HJ; Lin, MH; Shiao, YJ; Yang, YC; Chu, JC; Chen, CY; Chen, YY; Lin, TE; Su, CJ; Pan, SL; Chen, LC; Wang, CY; Hsu, KC; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51364609 ONC(=O)c1cccc(Nc2c3ccccc3nc3ccccc23)c1 InChI=1S/C20H15N3O2/c24-20(23-25)13-6-5-7-14(12-13)21-19-15-8-1-3-10-17(15)22-18-11-4-2-9-16(18)19/h1-12,25H,(H,21,22)(H,23,24) IGGDIHCMNIOYJN-UHFFFAOYSA-N 50551542 CHEMBL4753828 Histone deacetylase 4 Homo sapiens 29380 ChEMBL 10.1016/j.ejmech.2020.112193 10.7270/Q2FX7F3B 32151835 Tseng, HJ; Lin, MH; Shiao, YJ; Yang, YC; Chu, JC; Chen, CY; Chen, YY; Lin, TE; Su, CJ; Pan, SL; Chen, LC; Wang, CY; Hsu, KC; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50551542 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50551542&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162653512 461681882 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51364610 ONC(=O)CCc1ccc(Nc2c3ccccc3nc3ccccc23)cc1 InChI=1S/C22H19N3O2/c26-21(25-27)14-11-15-9-12-16(13-10-15)23-22-17-5-1-3-7-19(17)24-20-8-4-2-6-18(20)22/h1-10,12-13,27H,11,14H2,(H,23,24)(H,25,26) AGYUQCCMUDLPIU-UHFFFAOYSA-N 50462732 CHEMBL4248676 Histone deacetylase 4 Homo sapiens 7060 ChEMBL 10.1016/j.ejmech.2020.112193 10.7270/Q2FX7F3B 32151835 Tseng, HJ; Lin, MH; Shiao, YJ; Yang, YC; Chu, JC; Chen, CY; Chen, YY; Lin, TE; Su, CJ; Pan, SL; Chen, LC; Wang, CY; Hsu, KC; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50462732 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50462732&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 145983855 433929997 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51364611 ONC(=O)c1ccc(Nc2c3ccccc3nc3ccc(Br)cc23)cc1 InChI=1S/C20H14BrN3O2/c21-13-7-10-18-16(11-13)19(15-3-1-2-4-17(15)23-18)22-14-8-5-12(6-9-14)20(25)24-26/h1-11,26H,(H,22,23)(H,24,25) PESSDQDERPAVNH-UHFFFAOYSA-N 50551544 CHEMBL4796066 Histone deacetylase 4 Homo sapiens 7850 ChEMBL 10.1016/j.ejmech.2020.112193 10.7270/Q2FX7F3B 32151835 Tseng, HJ; Lin, MH; Shiao, YJ; Yang, YC; Chu, JC; Chen, CY; Chen, YY; Lin, TE; Su, CJ; Pan, SL; Chen, LC; Wang, CY; Hsu, KC; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50551544 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50551544&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162673723 461681884 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51364612 ONC(=O)c1ccc(Nc2c3ccccc3nc3ccc(OC(F)(F)F)cc23)cc1 InChI=1S/C21H14F3N3O3/c22-21(23,24)30-14-9-10-18-16(11-14)19(15-3-1-2-4-17(15)26-18)25-13-7-5-12(6-8-13)20(28)27-29/h1-11,29H,(H,25,26)(H,27,28) DWYXNGVQEJZWQA-UHFFFAOYSA-N 50551539 CHEMBL4751082 Histone deacetylase 4 Homo sapiens 14710 ChEMBL 10.1016/j.ejmech.2020.112193 10.7270/Q2FX7F3B 32151835 Tseng, HJ; Lin, MH; Shiao, YJ; Yang, YC; Chu, JC; Chen, CY; Chen, YY; Lin, TE; Su, CJ; Pan, SL; Chen, LC; Wang, CY; Hsu, KC; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50551539 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50551539&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162651817 461681879 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51364613 ONC(=O)c1ccc(Nc2c3ccccc3nc3ccc(OCc4ccccc4)cc23)cc1 InChI=1S/C27H21N3O3/c31-27(30-32)19-10-12-20(13-11-19)28-26-22-8-4-5-9-24(22)29-25-15-14-21(16-23(25)26)33-17-18-6-2-1-3-7-18/h1-16,32H,17H2,(H,28,29)(H,30,31) QJZZSSBITISGGT-UHFFFAOYSA-N 50551538 CHEMBL4761847 Histone deacetylase 4 Homo sapiens 1210 ChEMBL 10.1016/j.ejmech.2020.112193 10.7270/Q2FX7F3B 32151835 Tseng, HJ; Lin, MH; Shiao, YJ; Yang, YC; Chu, JC; Chen, CY; Chen, YY; Lin, TE; Su, CJ; Pan, SL; Chen, LC; Wang, CY; Hsu, KC; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50551538 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50551538&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162659066 461681878 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51364614 COc1cc2nc3ccccc3c(Nc3ccc(cc3)C(=O)NO)c2c(OC)c1OC InChI=1S/C23H21N3O5/c1-29-18-12-17-19(22(31-3)21(18)30-2)20(15-6-4-5-7-16(15)25-17)24-14-10-8-13(9-11-14)23(27)26-28/h4-12,28H,1-3H3,(H,24,25)(H,26,27) RXYDUXPNMOBQTR-UHFFFAOYSA-N 50551537 CHEMBL4753795 Histone deacetylase 4 Homo sapiens 15730 ChEMBL 10.1016/j.ejmech.2020.112193 10.7270/Q2FX7F3B 32151835 Tseng, HJ; Lin, MH; Shiao, YJ; Yang, YC; Chu, JC; Chen, CY; Chen, YY; Lin, TE; Su, CJ; Pan, SL; Chen, LC; Wang, CY; Hsu, KC; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50551537 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50551537&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162653917 461681877 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51364615 COc1ccc2nc3cc(Cl)ccc3c(Nc3ccc(cc3)C(=O)NO)c2n1 InChI=1S/C20H15ClN4O3/c1-28-17-9-8-15-19(24-17)18(14-7-4-12(21)10-16(14)23-15)22-13-5-2-11(3-6-13)20(26)25-27/h2-10,27H,1H3,(H,22,23)(H,25,26) RLHSWYLCHQWPQD-UHFFFAOYSA-N 50551536 CHEMBL4750838 Histone deacetylase 4 Homo sapiens >40000 ChEMBL 10.1016/j.ejmech.2020.112193 10.7270/Q2FX7F3B 32151835 Tseng, HJ; Lin, MH; Shiao, YJ; Yang, YC; Chu, JC; Chen, CY; Chen, YY; Lin, TE; Su, CJ; Pan, SL; Chen, LC; Wang, CY; Hsu, KC; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50551536 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50551536&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162652310 461681876 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51364616 ONC(=O)c1ccc(Nc2c3CCCCc3nc3ccccc23)cc1 InChI=1S/C20H19N3O2/c24-20(23-25)13-9-11-14(12-10-13)21-19-15-5-1-3-7-17(15)22-18-8-4-2-6-16(18)19/h1,3,5,7,9-12,25H,2,4,6,8H2,(H,21,22)(H,23,24) CZOYPJGGAMPDBF-UHFFFAOYSA-N 50551534 CHEMBL4799871 Histone deacetylase 4 Homo sapiens >40000 ChEMBL 10.1016/j.ejmech.2020.112193 10.7270/Q2FX7F3B 32151835 Tseng, HJ; Lin, MH; Shiao, YJ; Yang, YC; Chu, JC; Chen, CY; Chen, YY; Lin, TE; Su, CJ; Pan, SL; Chen, LC; Wang, CY; Hsu, KC; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50551534 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50551534&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162677045 461681874 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51364617 ONC(=O)c1ccc(Nc2ccnc3ccccc23)cc1 InChI=1S/C16H13N3O2/c20-16(19-21)11-5-7-12(8-6-11)18-15-9-10-17-14-4-2-1-3-13(14)15/h1-10,21H,(H,17,18)(H,19,20) CRQRFXAGXWHWTJ-UHFFFAOYSA-N 50551535 CHEMBL4752558 Histone deacetylase 4 Homo sapiens >40000 ChEMBL 10.1016/j.ejmech.2020.112193 10.7270/Q2FX7F3B 32151835 Tseng, HJ; Lin, MH; Shiao, YJ; Yang, YC; Chu, JC; Chen, CY; Chen, YY; Lin, TE; Su, CJ; Pan, SL; Chen, LC; Wang, CY; Hsu, KC; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50551535 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50551535&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162652776 461681875 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51390694 CSc1ccccc1C(=O)NCCCC[C@H](NC(=O)c1cncs1)c1ncc([nH]1)-c1ccc2ccccc2c1 50561967 CHEMBL4763995 Histone deacetylase 4 Homo sapiens >40000 ChEMBL 10.1021/acsmedchemlett.0c00462 10.7270/Q2TH8RDR 33335670 Liu, J; Yu, Y; Kelly, J; Sha, D; Alhassan, AB; Yu, W; Maletic, MM; Duffy, JL; Klein, DJ; Holloway, MK; Carroll, S; Howell, BJ; Barnard, RJO; Wolkenberg, S; Kozlowski, JA Merck & Co. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50561967 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50561967&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search WB4 7KBH 155289405 461832359 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51373364 Nc1ccc(cn1)-c1nc(N2CCOCC2)c2ncn(CCCCCCC(=O)NO)c2n1 InChI=1S/C21H28N8O3/c22-16-7-6-15(13-23-16)19-25-20(28-9-11-32-12-10-28)18-21(26-19)29(14-24-18)8-4-2-1-3-5-17(30)27-31/h6-7,13-14,31H,1-5,8-12H2,(H2,22,23)(H,27,30) IXTBKGBJNGTKQS-UHFFFAOYSA-N 50555460 CHEMBL4785064 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.7b01465 10.7270/Q2765K0S 29360358 Chen, D; Soh, CK; Goh, WH; Wang, H A*STAR http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50555460 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50555460&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118366956 461694228 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51373365 OCc1cccc(c1)-c1nc(N2CCOCC2)c2ncn(CCCCCCC(=O)NO)c2n1 InChI=1S/C23H30N6O4/c30-15-17-6-5-7-18(14-17)21-25-22(28-10-12-33-13-11-28)20-23(26-21)29(16-24-20)9-4-2-1-3-8-19(31)27-32/h5-7,14,16,30,32H,1-4,8-13,15H2,(H,27,31) JBFFDSGEOZGWCK-UHFFFAOYSA-N 50555461 CHEMBL4749655 Histone deacetylase 4 Homo sapiens 4591 ChEMBL 10.1021/acs.jmedchem.7b01465 10.7270/Q2765K0S 29360358 Chen, D; Soh, CK; Goh, WH; Wang, H A*STAR http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50555461 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50555461&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118366969 461694229 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51373366 Nc1ncc(cn1)-c1nc(N2CCOCC2)c2ccn(CCCCCCC(=O)NO)c2n1 InChI=1S/C21H28N8O3/c22-21-23-13-15(14-24-21)18-25-19-16(20(26-18)29-9-11-32-12-10-29)6-8-28(19)7-4-2-1-3-5-17(30)27-31/h6,8,13-14,31H,1-5,7,9-12H2,(H,27,30)(H2,22,23,24) YLDAIYDYJXZDGW-UHFFFAOYSA-N 50555464 CHEMBL4744689 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.7b01465 10.7270/Q2765K0S 29360358 Chen, D; Soh, CK; Goh, WH; Wang, H A*STAR http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50555464 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50555464&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118374514 461694232 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51373367 COc1ccc(cn1)-c1nc(N2CCOCC2)c2sc(CN(C)c3ncc(cn3)C(=O)NO)cc2n1 InChI=1S/C23H24N8O4S/c1-30(23-25-11-15(12-26-23)22(32)29-33)13-16-9-17-19(36-16)21(31-5-7-35-8-6-31)28-20(27-17)14-3-4-18(34-2)24-10-14/h3-4,9-12,33H,5-8,13H2,1-2H3,(H,29,32) JOWXJLIFIIOYMS-UHFFFAOYSA-N 50188961 CHEMBL3622533 Histone deacetylase 4 Homo sapiens 479 ChEMBL 10.1021/acs.jmedchem.7b01465 10.7270/Q2765K0S 29360358 Chen, D; Soh, CK; Goh, WH; Wang, H A*STAR http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50188961 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50188961&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 54575456 104072687 CHEMBL3622533 ZINC13444145 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51373368 CCCCc1nc2cc(\C=C\C(=O)NO)ccc2n1CCN(CC)CC InChI=1S/C20H30N4O2/c1-4-7-8-19-21-17-15-16(10-12-20(25)22-26)9-11-18(17)24(19)14-13-23(5-2)6-3/h9-12,15,26H,4-8,13-14H2,1-3H3,(H,22,25)/b12-10+ JHDKZFFAIZKUCU-ZRDIBKRKSA-N 50105330 CHEMBL1851943 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.7b01465 10.7270/Q2765K0S 29360358 Chen, D; Soh, CK; Goh, WH; Wang, H A*STAR http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105330 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105330&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 49855250 318590496 CHEMBL1851943 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51374003 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1 InChI=1S/C24H27N5O3/c30-22(28-32)15-9-1-2-10-16-25-23(31)19-17-26-24(27-18-19)29(20-11-5-3-6-12-20)21-13-7-4-8-14-21/h3-8,11-14,17-18,32H,1-2,9-10,15-16H2,(H,25,31)(H,28,30) QGZYDVAGYRLSKP-UHFFFAOYSA-N 50439674 RICOLINOSTAT::US10858323, Compound 2::US11207431, Example E::US8609678, 2-(diphenylamino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [26] Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1016/j.ejmech.2020.112411 10.7270/Q2JH3QVS 32615502 Gawel, JM; Shouksmith, AE; Raouf, YS; Nawar, N; Toutah, K; Bukhari, S; Manaswiyoungkul, P; Olaoye, OO; Israelian, J; Radu, TB; Cabral, AD; Sina, D; Sedighi, A; de Araujo, ED; Gunning, PT University of Toronto Mississauga http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50439674 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50439674&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search AH4 5WGL 53340666 175451991 ZINC89630354 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51374004 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1Cl InChI=1S/C24H26ClN5O3/c25-20-12-7-8-13-21(20)30(19-10-4-3-5-11-19)24-27-16-18(17-28-24)23(32)26-15-9-2-1-6-14-22(31)29-33/h3-5,7-8,10-13,16-17,33H,1-2,6,9,14-15H2,(H,26,32)(H,29,31) VLIUIBXPEDFJRF-UHFFFAOYSA-N 110036 US8609678, 2-((2-chlorophenyl)(phenyl)amino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [89] Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1016/j.ejmech.2020.112411 10.7270/Q2JH3QVS 32615502 Gawel, JM; Shouksmith, AE; Raouf, YS; Nawar, N; Toutah, K; Bukhari, S; Manaswiyoungkul, P; Olaoye, OO; Israelian, J; Radu, TB; Cabral, AD; Sina, D; Sedighi, A; de Araujo, ED; Gunning, PT University of Toronto Mississauga http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=110036 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=110036&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 53340426 186526906 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51374005 ONC(=O)c1ccc(CNC(=O)c2c(F)c(F)c(F)c(F)c2F)cc1 InChI=1S/C15H9F5N2O3/c16-9-8(10(17)12(19)13(20)11(9)18)15(24)21-5-6-1-3-7(4-2-6)14(23)22-25/h1-4,25H,5H2,(H,21,24)(H,22,23) KMHKOOKREYIIBC-UHFFFAOYSA-N 50555680 CHEMBL4784006 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1016/j.ejmech.2020.112411 10.7270/Q2JH3QVS 32615502 Gawel, JM; Shouksmith, AE; Raouf, YS; Nawar, N; Toutah, K; Bukhari, S; Manaswiyoungkul, P; Olaoye, OO; Israelian, J; Radu, TB; Cabral, AD; Sina, D; Sedighi, A; de Araujo, ED; Gunning, PT University of Toronto Mississauga http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50555680 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50555680&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155155878 461694448 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51374006 Cn1cc(CNCC2CCN(CC2)c2ncc(cn2)C(=O)NO)c2ccccc12 InChI=1S/C21H26N6O2/c1-26-14-17(18-4-2-3-5-19(18)26)11-22-10-15-6-8-27(9-7-15)21-23-12-16(13-24-21)20(28)25-29/h2-5,12-15,22,29H,6-11H2,1H3,(H,25,28) PAWIYAYFNXQGAP-UHFFFAOYSA-N 50105327 JNJ-26481585::Quisinostat Histone deacetylase 4 Homo sapiens 4.6 ChEMBL 10.1016/j.ejmech.2020.112411 10.7270/Q2JH3QVS 32615502 Gawel, JM; Shouksmith, AE; Raouf, YS; Nawar, N; Toutah, K; Bukhari, S; Manaswiyoungkul, P; Olaoye, OO; Israelian, J; Radu, TB; Cabral, AD; Sina, D; Sedighi, A; de Araujo, ED; Gunning, PT University of Toronto Mississauga http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105327 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105327&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search GOK 7Q1B,6HSK,6HSH 11538455 318590494 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367665 C[C@H](CN1CCCCCC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C19H23F3N4O2/c1-13(12-26-10-4-2-3-5-11-26)23-17(27)15-8-6-14(7-9-15)16-24-18(28-25-16)19(20,21)22/h6-9,13H,2-5,10-12H2,1H3,(H,23,27)/t13-/m1/s1 IZFWXPXCTQFPQU-CYBMUJFWSA-N 243178 (R)-N-(1-(Azepan-1-yl)propan-2-yl)-4- (5-(trifluoromethyl)-1,2,4-oxadiazol-3- yl)benzamide::US10053434, 13 Histone deacetylase 4 Homo sapiens 10.0 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=243178 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=243178&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122669605 376221562 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367666 C[C@H](CN1CCC[C@H](C1)OC(F)F)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C19H21F5N4O3/c1-11(9-28-8-2-3-14(10-28)30-18(20)21)25-16(29)13-6-4-12(5-7-13)15-26-17(31-27-15)19(22,23)24/h4-7,11,14,18H,2-3,8-10H2,1H3,(H,25,29)/t11-,14-/m1/s1 YOGWQNKZBZCDFV-BXUZGUMPSA-N 50552908 CHEMBL4753102 Histone deacetylase 4 Homo sapiens 20 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552908 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552908&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122678093 461691676 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367667 C[C@H](CN1CCC[C@@H](C1)OC(F)F)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C19H21F5N4O3/c1-11(9-28-8-2-3-14(10-28)30-18(20)21)25-16(29)13-6-4-12(5-7-13)15-26-17(31-27-15)19(22,23)24/h4-7,11,14,18H,2-3,8-10H2,1H3,(H,25,29)/t11-,14+/m1/s1 YOGWQNKZBZCDFV-RISCZKNCSA-N 50552909 CHEMBL4754665 Histone deacetylase 4 Homo sapiens 3.0 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552909 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552909&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122678125 461691677 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367668 C[C@H](CN1CCC(F)(F)CC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C18H19F5N4O2/c1-11(10-27-8-6-17(19,20)7-9-27)24-15(28)13-4-2-12(3-5-13)14-25-16(29-26-14)18(21,22)23/h2-5,11H,6-10H2,1H3,(H,24,28)/t11-/m1/s1 PTMBMYDOYIOFGC-LLVKDONJSA-N 50552910 CHEMBL4752150 Histone deacetylase 4 Homo sapiens 130 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552910 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552910&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162652623 461691678 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367669 C[C@H](CN1CCC(F)CC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C18H20F4N4O2/c1-11(10-26-8-6-14(19)7-9-26)23-16(27)13-4-2-12(3-5-13)15-24-17(28-25-15)18(20,21)22/h2-5,11,14H,6-10H2,1H3,(H,23,27)/t11-/m1/s1 FPSCUKUKYRNPDM-LLVKDONJSA-N 50552911 CHEMBL4797931 Histone deacetylase 4 Homo sapiens 30 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552911 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552911&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162676125 461691679 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367670 C[C@H](CN1CCCC(C)(C)C1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C20H25F3N4O2/c1-13(11-27-10-4-9-19(2,3)12-27)24-17(28)15-7-5-14(6-8-15)16-25-18(29-26-16)20(21,22)23/h5-8,13H,4,9-12H2,1-3H3,(H,24,28)/t13-/m1/s1 BBOXDPRCICCASY-CYBMUJFWSA-N 50552912 CHEMBL4760047 Histone deacetylase 4 Homo sapiens 2.0 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552912 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552912&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162657496 461691680 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367671 C[C@H](CN1CCCCC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C18H21F3N4O2/c1-12(11-25-9-3-2-4-10-25)22-16(26)14-7-5-13(6-8-14)15-23-17(27-24-15)18(19,20)21/h5-8,12H,2-4,9-11H2,1H3,(H,22,26)/t12-/m1/s1 WTZFUFARAWDPGC-GFCCVEGCSA-N 162840 US9056843, 131 Histone deacetylase 4 Homo sapiens 10.0 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162840 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162840&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230957 310304777 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367672 C[C@H](CN1CCC(F)(F)C1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C17H17F5N4O2/c1-10(8-26-7-6-16(18,19)9-26)23-14(27)12-4-2-11(3-5-12)13-24-15(28-25-13)17(20,21)22/h2-5,10H,6-9H2,1H3,(H,23,27)/t10-/m1/s1 RBNLEULNMMUQNN-SNVBAGLBSA-N 50552913 CHEMBL4752226 Histone deacetylase 4 Homo sapiens 230 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552913 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552913&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162652432 461691681 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367673 C[C@H](CN1CCC[C@H]1C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C18H21F3N4O2/c1-11(10-25-9-3-4-12(25)2)22-16(26)14-7-5-13(6-8-14)15-23-17(27-24-15)18(19,20)21/h5-8,11-12H,3-4,9-10H2,1-2H3,(H,22,26)/t11-,12-/m1/s1 DBWSFWPXCPNWRZ-VXGBXAGGSA-N 50552914 CHEMBL4764348 Histone deacetylase 4 Homo sapiens 70 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552914 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552914&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162661194 461691682 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367674 C[C@H](CN1CCC[C@@H]1C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C18H21F3N4O2/c1-11(10-25-9-3-4-12(25)2)22-16(26)14-7-5-13(6-8-14)15-23-17(27-24-15)18(19,20)21/h5-8,11-12H,3-4,9-10H2,1-2H3,(H,22,26)/t11-,12+/m1/s1 DBWSFWPXCPNWRZ-NEPJUHHUSA-N 50552915 CHEMBL4798111 Histone deacetylase 4 Homo sapiens 10.0 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552915 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552915&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162675553 461691683 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367675 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1(CN2CCCC2)CC1 InChI=1S/C18H19F3N4O2/c19-18(20,21)16-22-14(24-27-16)12-3-5-13(6-4-12)15(26)23-17(7-8-17)11-25-9-1-2-10-25/h3-6H,1-2,7-11H2,(H,23,26) MTMQPKCXWHSWNP-UHFFFAOYSA-N 50552916 CHEMBL4740322 Histone deacetylase 4 Homo sapiens 40 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552916 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552916&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162644920 461691684 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367676 CC(C)(CN1CCCC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C18H21F3N4O2/c1-17(2,11-25-9-3-4-10-25)23-15(26)13-7-5-12(6-8-13)14-22-16(27-24-14)18(19,20)21/h5-8H,3-4,9-11H2,1-2H3,(H,23,26) QHDTVFVVAFOPPR-UHFFFAOYSA-N 50552917 CHEMBL4753030 Histone deacetylase 4 Homo sapiens 280 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552917 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552917&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162653733 461691685 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367677 C[C@@H](CN1CCCC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C17H19F3N4O2/c1-11(10-24-8-2-3-9-24)21-15(25)13-6-4-12(5-7-13)14-22-16(26-23-14)17(18,19)20/h4-7,11H,2-3,8-10H2,1H3,(H,21,25)/t11-/m0/s1 GPAXDYNOSUVDDO-NSHDSACASA-N 50552918 CHEMBL3910908 Histone deacetylase 4 Homo sapiens 50 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552918 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552918&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 134131794 461691686 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367678 C[C@H](CN1CCCC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C17H19F3N4O2/c1-11(10-24-8-2-3-9-24)21-15(25)13-6-4-12(5-7-13)14-22-16(26-23-14)17(18,19)20/h4-7,11H,2-3,8-10H2,1H3,(H,21,25)/t11-/m1/s1 GPAXDYNOSUVDDO-LLVKDONJSA-N 162839 US9056843, 130 Histone deacetylase 4 Homo sapiens 10.0 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162839 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162839&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230767 310304776 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367679 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NCCN1CCCC1 InChI=1S/C16H17F3N4O2/c17-16(18,19)15-21-13(22-25-15)11-3-5-12(6-4-11)14(24)20-7-10-23-8-1-2-9-23/h3-6H,1-2,7-10H2,(H,20,24) PVQMNPDPHHUNAN-UHFFFAOYSA-N 50552919 CHEMBL4747488 Histone deacetylase 4 Homo sapiens 30 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552919 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552919&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162650481 461691687 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367680 CCCN(CCC)C[C@@H](C)NC(=O)c1ccc(cc1)-c1nc(no1)C(F)(F)F InChI=1S/C19H25F3N4O2/c1-4-10-26(11-5-2)12-13(3)23-16(27)14-6-8-15(9-7-14)17-24-18(25-28-17)19(20,21)22/h6-9,13H,4-5,10-12H2,1-3H3,(H,23,27)/t13-/m1/s1 TVKINPHWFZJRCN-CYBMUJFWSA-N 50552920 CHEMBL4779720 Histone deacetylase 4 Homo sapiens 28000 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552920 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552920&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162664796 461691688 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367681 CCCN(CCC)C[C@@H](C)NC(=O)c1ccc(cc1)-c1ncon1 InChI=1S/C18H26N4O2/c1-4-10-22(11-5-2)12-14(3)20-18(23)16-8-6-15(7-9-16)17-19-13-24-21-17/h6-9,13-14H,4-5,10-12H2,1-3H3,(H,20,23)/t14-/m1/s1 HRPPPBKCIIMXSI-CQSZACIVSA-N 50552921 CHEMBL4745553 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552921 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552921&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162647562 461691689 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367682 CCCN(CCC)C[C@@H](C)NC(=O)c1ccc(cc1)-c1noc(C)n1 InChI=1S/C19H28N4O2/c1-5-11-23(12-6-2)13-14(3)20-19(24)17-9-7-16(8-10-17)18-21-15(4)25-22-18/h7-10,14H,5-6,11-13H2,1-4H3,(H,20,24)/t14-/m1/s1 DTAORECSHQWLHS-CQSZACIVSA-N 50552922 CHEMBL4741190 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552922 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552922&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90164459 461691690 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367683 CCCN(CCC)C[C@@H](C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)F InChI=1S/C19H26F2N4O2/c1-4-10-25(11-5-2)12-13(3)22-18(26)15-8-6-14(7-9-15)17-23-19(16(20)21)27-24-17/h6-9,13,16H,4-5,10-12H2,1-3H3,(H,22,26)/t13-/m1/s1 NRPYXHWGQIFCGW-CYBMUJFWSA-N 50552923 CHEMBL4799829 Histone deacetylase 4 Homo sapiens 890 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552923 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552923&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162676841 461691691 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367684 CCCN(CCC)C[C@@H](C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C19H25F3N4O2/c1-4-10-26(11-5-2)12-13(3)23-17(27)15-8-6-14(7-9-15)16-24-18(28-25-16)19(20,21)22/h6-9,13H,4-5,10-12H2,1-3H3,(H,23,27)/t13-/m1/s1 HMXFCVJIASWKMB-CYBMUJFWSA-N 162846 US9056843, 137 Histone deacetylase 4 Homo sapiens 3.0 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162846 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162846&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230790 310304783 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367709 C[C@H](CN1CCCCCC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C19H23F3N4O2/c1-13(12-26-10-4-2-3-5-11-26)23-17(27)15-8-6-14(7-9-15)16-24-18(28-25-16)19(20,21)22/h6-9,13H,2-5,10-12H2,1H3,(H,23,27)/t13-/m1/s1 IZFWXPXCTQFPQU-CYBMUJFWSA-N 243178 (R)-N-(1-(Azepan-1-yl)propan-2-yl)-4- (5-(trifluoromethyl)-1,2,4-oxadiazol-3- yl)benzamide::US10053434, 13 Histone deacetylase 4 Homo sapiens 30 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=243178 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=243178&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122669605 376221562 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367710 C[C@H](CN1CCC[C@H](C1)OC(F)F)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C19H21F5N4O3/c1-11(9-28-8-2-3-14(10-28)30-18(20)21)25-16(29)13-6-4-12(5-7-13)15-26-17(31-27-15)19(22,23)24/h4-7,11,14,18H,2-3,8-10H2,1H3,(H,25,29)/t11-,14-/m1/s1 YOGWQNKZBZCDFV-BXUZGUMPSA-N 50552908 CHEMBL4753102 Histone deacetylase 4 Homo sapiens 60 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552908 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552908&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122678093 461691676 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367711 C[C@H](CN1CCC[C@@H](C1)OC(F)F)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C19H21F5N4O3/c1-11(9-28-8-2-3-14(10-28)30-18(20)21)25-16(29)13-6-4-12(5-7-13)15-26-17(31-27-15)19(22,23)24/h4-7,11,14,18H,2-3,8-10H2,1H3,(H,25,29)/t11-,14+/m1/s1 YOGWQNKZBZCDFV-RISCZKNCSA-N 50552909 CHEMBL4754665 Histone deacetylase 4 Homo sapiens 10.0 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552909 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552909&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122678125 461691677 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367712 C[C@H](CN1CCC(F)(F)CC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C18H19F5N4O2/c1-11(10-27-8-6-17(19,20)7-9-27)24-15(28)13-4-2-12(3-5-13)14-25-16(29-26-14)18(21,22)23/h2-5,11H,6-10H2,1H3,(H,24,28)/t11-/m1/s1 PTMBMYDOYIOFGC-LLVKDONJSA-N 50552910 CHEMBL4752150 Histone deacetylase 4 Homo sapiens 380 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552910 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552910&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162652623 461691678 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367713 C[C@H](CN1CCC(F)CC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C18H20F4N4O2/c1-11(10-26-8-6-14(19)7-9-26)23-16(27)13-4-2-12(3-5-13)15-24-17(28-25-15)18(20,21)22/h2-5,11,14H,6-10H2,1H3,(H,23,27)/t11-/m1/s1 FPSCUKUKYRNPDM-LLVKDONJSA-N 50552911 CHEMBL4797931 Histone deacetylase 4 Homo sapiens 100 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552911 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552911&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162676125 461691679 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367714 C[C@H](CN1CCCC(C)(C)C1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C20H25F3N4O2/c1-13(11-27-10-4-9-19(2,3)12-27)24-17(28)15-7-5-14(6-8-15)16-25-18(29-26-16)20(21,22)23/h5-8,13H,4,9-12H2,1-3H3,(H,24,28)/t13-/m1/s1 BBOXDPRCICCASY-CYBMUJFWSA-N 50552912 CHEMBL4760047 Histone deacetylase 4 Homo sapiens 10.0 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552912 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552912&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162657496 461691680 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367715 C[C@H](CN1CCCCC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C18H21F3N4O2/c1-12(11-25-9-3-2-4-10-25)22-16(26)14-7-5-13(6-8-14)15-23-17(27-24-15)18(19,20)21/h5-8,12H,2-4,9-11H2,1H3,(H,22,26)/t12-/m1/s1 WTZFUFARAWDPGC-GFCCVEGCSA-N 162840 US9056843, 131 Histone deacetylase 4 Homo sapiens 70 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162840 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162840&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230957 310304777 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367716 C[C@H](CN1CCC(F)(F)C1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C17H17F5N4O2/c1-10(8-26-7-6-16(18,19)9-26)23-14(27)12-4-2-11(3-5-12)13-24-15(28-25-13)17(20,21)22/h2-5,10H,6-9H2,1H3,(H,23,27)/t10-/m1/s1 RBNLEULNMMUQNN-SNVBAGLBSA-N 50552913 CHEMBL4752226 Histone deacetylase 4 Homo sapiens 1300 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552913 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552913&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162652432 461691681 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367717 C[C@H](CN1CCC[C@H]1C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C18H21F3N4O2/c1-11(10-25-9-3-4-12(25)2)22-16(26)14-7-5-13(6-8-14)15-23-17(27-24-15)18(19,20)21/h5-8,11-12H,3-4,9-10H2,1-2H3,(H,22,26)/t11-,12-/m1/s1 DBWSFWPXCPNWRZ-VXGBXAGGSA-N 50552914 CHEMBL4764348 Histone deacetylase 4 Homo sapiens 600 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552914 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552914&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162661194 461691682 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367718 C[C@H](CN1CCC[C@@H]1C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C18H21F3N4O2/c1-11(10-25-9-3-4-12(25)2)22-16(26)14-7-5-13(6-8-14)15-23-17(27-24-15)18(19,20)21/h5-8,11-12H,3-4,9-10H2,1-2H3,(H,22,26)/t11-,12+/m1/s1 DBWSFWPXCPNWRZ-NEPJUHHUSA-N 50552915 CHEMBL4798111 Histone deacetylase 4 Homo sapiens 40 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552915 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552915&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162675553 461691683 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367719 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1(CN2CCCC2)CC1 InChI=1S/C18H19F3N4O2/c19-18(20,21)16-22-14(24-27-16)12-3-5-13(6-4-12)15(26)23-17(7-8-17)11-25-9-1-2-10-25/h3-6H,1-2,7-11H2,(H,23,26) MTMQPKCXWHSWNP-UHFFFAOYSA-N 50552916 CHEMBL4740322 Histone deacetylase 4 Homo sapiens 180 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552916 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552916&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162644920 461691684 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367720 CC(C)(CN1CCCC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C18H21F3N4O2/c1-17(2,11-25-9-3-4-10-25)23-15(26)13-7-5-12(6-8-13)14-22-16(27-24-14)18(19,20)21/h5-8H,3-4,9-11H2,1-2H3,(H,23,26) QHDTVFVVAFOPPR-UHFFFAOYSA-N 50552917 CHEMBL4753030 Histone deacetylase 4 Homo sapiens 310 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552917 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552917&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162653733 461691685 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367721 C[C@@H](CN1CCCC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C17H19F3N4O2/c1-11(10-24-8-2-3-9-24)21-15(25)13-6-4-12(5-7-13)14-22-16(26-23-14)17(18,19)20/h4-7,11H,2-3,8-10H2,1H3,(H,21,25)/t11-/m0/s1 GPAXDYNOSUVDDO-NSHDSACASA-N 50552918 CHEMBL3910908 Histone deacetylase 4 Homo sapiens 730 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552918 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552918&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 134131794 461691686 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367722 C[C@H](CN1CCCC1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C17H19F3N4O2/c1-11(10-24-8-2-3-9-24)21-15(25)13-6-4-12(5-7-13)14-22-16(26-23-14)17(18,19)20/h4-7,11H,2-3,8-10H2,1H3,(H,21,25)/t11-/m1/s1 GPAXDYNOSUVDDO-LLVKDONJSA-N 162839 US9056843, 130 Histone deacetylase 4 Homo sapiens 70 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162839 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162839&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230767 310304776 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367723 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NCCN1CCCC1 InChI=1S/C16H17F3N4O2/c17-16(18,19)15-21-13(22-25-15)11-3-5-12(6-4-11)14(24)20-7-10-23-8-1-2-9-23/h3-6H,1-2,7-10H2,(H,20,24) PVQMNPDPHHUNAN-UHFFFAOYSA-N 50552919 CHEMBL4747488 Histone deacetylase 4 Homo sapiens 250 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552919 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552919&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162650481 461691687 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367724 CCCN(CCC)C[C@@H](C)NC(=O)c1ccc(cc1)-c1nc(no1)C(F)(F)F InChI=1S/C19H25F3N4O2/c1-4-10-26(11-5-2)12-13(3)23-16(27)14-6-8-15(9-7-14)17-24-18(25-28-17)19(20,21)22/h6-9,13H,4-5,10-12H2,1-3H3,(H,23,27)/t13-/m1/s1 TVKINPHWFZJRCN-CYBMUJFWSA-N 50552920 CHEMBL4779720 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552920 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552920&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162664796 461691688 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367725 CCCN(CCC)C[C@@H](C)NC(=O)c1ccc(cc1)-c1ncon1 InChI=1S/C18H26N4O2/c1-4-10-22(11-5-2)12-14(3)20-18(23)16-8-6-15(7-9-16)17-19-13-24-21-17/h6-9,13-14H,4-5,10-12H2,1-3H3,(H,20,23)/t14-/m1/s1 HRPPPBKCIIMXSI-CQSZACIVSA-N 50552921 CHEMBL4745553 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552921 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552921&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162647562 461691689 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367726 CCCN(CCC)C[C@@H](C)NC(=O)c1ccc(cc1)-c1noc(C)n1 InChI=1S/C19H28N4O2/c1-5-11-23(12-6-2)13-14(3)20-19(24)17-9-7-16(8-10-17)18-21-15(4)25-22-18/h7-10,14H,5-6,11-13H2,1-4H3,(H,20,24)/t14-/m1/s1 DTAORECSHQWLHS-CQSZACIVSA-N 50552922 CHEMBL4741190 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552922 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552922&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90164459 461691690 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367727 CCCN(CCC)C[C@@H](C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)F InChI=1S/C19H26F2N4O2/c1-4-10-25(11-5-2)12-13(3)22-18(26)15-8-6-14(7-9-15)17-23-19(16(20)21)27-24-17/h6-9,13,16H,4-5,10-12H2,1-3H3,(H,22,26)/t13-/m1/s1 NRPYXHWGQIFCGW-CYBMUJFWSA-N 50552923 CHEMBL4799829 Histone deacetylase 4 Homo sapiens 19000 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50552923 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50552923&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162676841 461691691 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367728 CCCN(CCC)C[C@@H](C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C19H25F3N4O2/c1-4-10-26(11-5-2)12-13(3)23-17(27)15-8-6-14(7-9-15)16-24-18(28-25-16)19(20,21)22/h6-9,13H,4-5,10-12H2,1-3H3,(H,23,27)/t13-/m1/s1 HMXFCVJIASWKMB-CYBMUJFWSA-N 162846 US9056843, 137 Histone deacetylase 4 Homo sapiens 20 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162846 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162846&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230790 310304783 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51367729 CCCN(CCC)C[C@@H](C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C19H25F3N4O2/c1-4-10-26(11-5-2)12-13(3)23-17(27)15-8-6-14(7-9-15)16-24-18(28-25-16)19(20,21)22/h6-9,13H,4-5,10-12H2,1-3H3,(H,23,27)/t13-/m1/s1 HMXFCVJIASWKMB-CYBMUJFWSA-N 162846 US9056843, 137 Histone deacetylase 4 Homo sapiens 44 ChEMBL 10.1021/acsmedchemlett.0c00532 10.7270/Q2474FHW 33738065 Stott, AJ; Maillard, MC; Beaumont, V; Allcock, D; Aziz, O; Borchers, AH; Blackaby, W; Breccia, P; Creighton-Gutteridge, G; Haughan, AF; Jarvis, RE; Luckhurst, CA; Matthews, KL; McAllister, G; Pollack, S; Saville-Stones, E; Van de Poël, AJ; Vater, HD; Vann, J; Williams, R; Yates, D; Muñoz-Sanjuán, I; Dominguez, C Charles River Discovery http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162846 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162846&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230790 310304783 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51355024 ONC(=O)c1ccc(CN2[C@H]3CCCC[C@H]3CS(=O)(=O)c3ccccc23)cc1 InChI=1S/C21H24N2O4S/c24-21(22-25)16-11-9-15(10-12-16)13-23-18-6-2-1-5-17(18)14-28(26,27)20-8-4-3-7-19(20)23/h3-4,7-12,17-18,25H,1-2,5-6,13-14H2,(H,22,24)/t17-,18-/m0/s1 DMIDPYMXHVUIIM-ROUUACIJSA-N 50548181 CHEMBL4744479 Histone deacetylase 4 Homo sapiens >8000 ChEMBL 10.1016/j.ejmech.2017.10.040 10.7270/Q25H7KV7 29133060 Wang, XX; Wan, RZ; Liu, ZP Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50548181 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50548181&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162648243 461678521 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51355038 ONC(=O)c1ccc(Cn2c3CCS(=O)(=O)c3c3ccccc23)cc1 InChI=1S/C18H16N2O4S/c21-18(19-22)13-7-5-12(6-8-13)11-20-15-4-2-1-3-14(15)17-16(20)9-10-25(17,23)24/h1-8,22H,9-11H2,(H,19,21) ZXADRTUZWSITDT-UHFFFAOYSA-N 50252392 CHEMBL4069287 Histone deacetylase 4 Homo sapiens 1000 ChEMBL 10.1016/j.ejmech.2017.10.040 10.7270/Q25H7KV7 29133060 Wang, XX; Wan, RZ; Liu, ZP Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50252392 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50252392&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118656853 401963029 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51355071 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1 InChI=1S/C24H27N5O3/c30-22(28-32)15-9-1-2-10-16-25-23(31)19-17-26-24(27-18-19)29(20-11-5-3-6-12-20)21-13-7-4-8-14-21/h3-8,11-14,17-18,32H,1-2,9-10,15-16H2,(H,25,31)(H,28,30) QGZYDVAGYRLSKP-UHFFFAOYSA-N 50439674 RICOLINOSTAT::US10858323, Compound 2::US11207431, Example E::US8609678, 2-(diphenylamino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [26] Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1016/j.ejmech.2017.10.040 10.7270/Q25H7KV7 29133060 Wang, XX; Wan, RZ; Liu, ZP Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50439674 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50439674&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search AH4 5WGL 53340666 175451991 ZINC89630354 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51355078 CN(C)c1cccc2c(cccc12)S(=O)(=O)NCCCCCC(=O)NO InChI=1S/C18H25N3O4S/c1-21(2)16-10-6-9-15-14(16)8-7-11-17(15)26(24,25)19-13-5-3-4-12-18(22)20-23/h6-11,19,23H,3-5,12-13H2,1-2H3,(H,20,22) IAFMTZMOWYBUMQ-UHFFFAOYSA-N 50548184 CHEMBL4759256 Histone deacetylase 4 Homo sapiens 330 ChEMBL 10.1016/j.ejmech.2017.10.040 10.7270/Q25H7KV7 29133060 Wang, XX; Wan, RZ; Liu, ZP Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50548184 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50548184&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44124386 461678524 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1124046 CN(Cc1ccc(cc1F)C(=O)NO)CC12CC3CC(CC(C3)C1)C2 InChI=1S/C20H27FN2O2/c1-23(11-17-3-2-16(7-18(17)21)19(24)22-25)12-20-8-13-4-14(9-20)6-15(5-13)10-20/h2-3,7,13-15,25H,4-6,8-12H2,1H3,(H,22,24) IGZQZELTOHAHNW-UHFFFAOYSA-N 50369345 CHEMBL4165724::US11207431, Example 1 Histone deacetylase 4 Homo sapiens 7.10 US Patent 10.7270/Q2639SXJ aid1806213 US11207431 Hooker, J; Wang, C; Strebl-Bantillo, MG The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50369345 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50369345&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search HBV 6DVO 134812690 160848447 ZINC49055016 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1124047 ONC(=O)CCCCCC(=O)Nc1ccccc1 InChI=1S/C13H18N2O3/c16-12(14-11-7-3-1-4-8-11)9-5-2-6-10-13(17)15-18/h1,3-4,7-8,18H,2,5-6,9-10H2,(H,14,16)(H,15,17) XCELUDLGZVVNON-UHFFFAOYSA-N 337661 US10227295, Compound TSA::US11207431, TSA::US9751832, TSA::US9956192, Compound TSA Histone deacetylase 4 Homo sapiens 2900 US Patent 10.7270/Q2639SXJ aid1806213 US11207431 Hooker, J; Wang, C; Strebl-Bantillo, MG The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=337661 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=337661&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44392341 384989708 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1124096 CN(Cc1ccc(cc1F)C(=O)NO)CC12CC3CC(CC(C3)C1)C2 InChI=1S/C20H27FN2O2/c1-23(11-17-3-2-16(7-18(17)21)19(24)22-25)12-20-8-13-4-14(9-20)6-15(5-13)10-20/h2-3,7,13-15,25H,4-6,8-12H2,1H3,(H,22,24) IGZQZELTOHAHNW-UHFFFAOYSA-N 50369345 CHEMBL4165724::US11207431, Example 1 Histone deacetylase 4 Homo sapiens 11300 US Patent 10.7270/Q2639SXJ aid1806213 US11207431 Hooker, J; Wang, C; Strebl-Bantillo, MG The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50369345 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50369345&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search HBV 6DVO 134812690 160848447 ZINC49055016 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1124097 CN(Cc1ccc(\C=C\C(=O)NO)cc1)CC12CC3CC(CC(C3)C1)C2 InChI=1S/C22H30N2O2/c1-24(14-17-4-2-16(3-5-17)6-7-21(25)23-26)15-22-11-18-8-19(12-22)10-20(9-18)13-22/h2-7,18-20,26H,8-15H2,1H3,(H,23,25)/b7-6+ WNIDBXBLQFPAJA-VOTSOKGWSA-N 323709 US10188756, Compound CN133::US11207431, Martinostat Histone deacetylase 4 Homo sapiens 240 US Patent 10.7270/Q2639SXJ aid1806213 US11207431 Hooker, J; Wang, C; Strebl-Bantillo, MG The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=323709 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=323709&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 90479372 384578788 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1124098 CN(Cc1ccc(\C=C\C(=O)NO)cc1F)CC12CC3CC(CC(C3)C1)C2 InChI=1S/C22H29FN2O2/c1-25(14-22-10-16-6-17(11-22)8-18(7-16)12-22)13-19-4-2-15(9-20(19)23)3-5-21(26)24-27/h2-5,9,16-18,27H,6-8,10-14H2,1H3,(H,24,26)/b5-3+ JJVJGQDLQUPOQJ-HWKANZROSA-N 323718 US10188756, Compound CN149::US11207431, Example B Histone deacetylase 4 Homo sapiens >1000 US Patent 10.7270/Q2639SXJ aid1806213 US11207431 Hooker, J; Wang, C; Strebl-Bantillo, MG The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=323718 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=323718&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122550533 384578797 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1124099 CN(c1ncc(cn1)C(=O)NO)C12CC3CC(CC(C3)C1)C2 InChI=1S/C16H22N4O2/c1-20(15-17-8-13(9-18-15)14(21)19-22)16-5-10-2-11(6-16)4-12(3-10)7-16/h8-12,22H,2-7H2,1H3,(H,19,21) IXDSXOZCSDIMHI-UHFFFAOYSA-N 531084 US11207431, Example C Histone deacetylase 4 Homo sapiens 34.0 US Patent 10.7270/Q2639SXJ aid1806213 US11207431 Hooker, J; Wang, C; Strebl-Bantillo, MG The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=531084 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=531084&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 146397914 463794549 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1124100 CN1CCc2c(C1)c1ccccc1n2Cc1ccc(cc1)C(=O)NO InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::Tubastatin A::US10227295, Compound Tubastatin A::US10456394, Tubastatin A::US11207431, Example D::US8748451, 6::US9249087, Tubacin::US9751832, Tubastatin A::US9956192, Compound Tubastatin-A Histone deacetylase 4 Homo sapiens >30.0 US Patent 10.7270/Q2639SXJ aid1806213 US11207431 Hooker, J; Wang, C; Strebl-Bantillo, MG The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 ZINC51951670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1124101 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1 InChI=1S/C24H27N5O3/c30-22(28-32)15-9-1-2-10-16-25-23(31)19-17-26-24(27-18-19)29(20-11-5-3-6-12-20)21-13-7-4-8-14-21/h3-8,11-14,17-18,32H,1-2,9-10,15-16H2,(H,25,31)(H,28,30) QGZYDVAGYRLSKP-UHFFFAOYSA-N 50439674 RICOLINOSTAT::US10858323, Compound 2::US11207431, Example E::US8609678, 2-(diphenylamino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [26] Histone deacetylase 4 Homo sapiens >1000 US Patent 10.7270/Q2639SXJ aid1806213 US11207431 Hooker, J; Wang, C; Strebl-Bantillo, MG The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50439674 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50439674&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search AH4 5WGL 53340666 175451991 ZINC89630354 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1124102 CC(=O)Nc1ccc(cc1)C(=O)Nc1ccccc1N InChI=1S/C15H15N3O2/c1-10(19)17-12-8-6-11(7-9-12)15(20)18-14-5-3-2-4-13(14)16/h2-9H,16H2,1H3,(H,17,19)(H,18,20) VAZAPHZUAVEOMC-UHFFFAOYSA-N 19422 4-(acetylamino)-N-(2-amino-phenyl) benzamide::CI-994::N-(2-aminophenyl)-4-acetamidobenzamide::N-acetyldinaline::US11207431, Example F::US11377423, CI-994 Histone deacetylase 4 Homo sapiens >33.0 US Patent 10.7270/Q2639SXJ aid1806213 US11207431 Hooker, J; Wang, C; Strebl-Bantillo, MG The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19422 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19422&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 2746 46519444 ZINC00003803 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1124103 CN(Cc1ccc(cc1F)C(=O)NO)CC12CC3CC(CC(C3)C1)C2 InChI=1S/C20H27FN2O2/c1-23(11-17-3-2-16(7-18(17)21)19(24)22-25)12-20-8-13-4-14(9-20)6-15(5-13)10-20/h2-3,7,13-15,25H,4-6,8-12H2,1H3,(H,22,24) IGZQZELTOHAHNW-UHFFFAOYSA-N 50369345 CHEMBL4165724::US11207431, Example 1 Histone deacetylase 4 Homo sapiens 11300 US Patent 10.7270/Q2639SXJ aid1806213 US11207431 Hooker, J; Wang, C; Strebl-Bantillo, MG The General Hospital Corporation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50369345 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50369345&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search HBV 6DVO 134812690 160848447 ZINC49055016 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51397198 Nc1ccccc1NC(=O)c1ccc(Cn2cnc3c(Nc4ccc(F)c(Cl)c4)nc(N)nc23)cc1 InChI=1S/C25H20ClFN8O/c26-17-11-16(9-10-18(17)27)31-22-21-23(34-25(29)33-22)35(13-30-21)12-14-5-7-15(8-6-14)24(36)32-20-4-2-1-3-19(20)28/h1-11,13H,12,28H2,(H,32,36)(H3,29,31,33,34) BWFYYTOGYBJCQR-UHFFFAOYSA-N 50564441 CHEMBL4790678 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2020.112291 10.7270/Q26W9FT0 32325365 Nepali, K; Chang, TY; Lai, MJ; Hsu, KC; Yen, Y; Lin, TE; Lee, SB; Liou, JP Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50564441 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50564441&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162670784 461684779 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51397199 Nc1ccccc1NC(=O)c1ccc(CNC(=O)OCc2cccnc2)cc1 InChI=1S/C21H20N4O3/c22-18-5-1-2-6-19(18)25-20(26)17-9-7-15(8-10-17)13-24-21(27)28-14-16-4-3-11-23-12-16/h1-12H,13-14,22H2,(H,24,27)(H,25,26) INVTYAOGFAGBOE-UHFFFAOYSA-N 19410 CHEMBL27759::MS-275::US11377423, MS-275::US11672788, Compound Entinostat::US9265734, MS-275::US9796664, Compound MS-275::benzamide-type inhibitor, 3::pyridin-3-ylmethyl N-({4-[(2-aminophenyl)carbamoyl]phenyl}methyl)carbamate Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2020.112291 10.7270/Q26W9FT0 32325365 Nepali, K; Chang, TY; Lai, MJ; Hsu, KC; Yen, Y; Lin, TE; Lee, SB; Liou, JP Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19410 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19410&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4261 46519433 CHEMBL27759 7007 ZINC01488870 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51398807 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1 InChI=1S/C24H27N5O3/c30-22(28-32)15-9-1-2-10-16-25-23(31)19-17-26-24(27-18-19)29(20-11-5-3-6-12-20)21-13-7-4-8-14-21/h3-8,11-14,17-18,32H,1-2,9-10,15-16H2,(H,25,31)(H,28,30) QGZYDVAGYRLSKP-UHFFFAOYSA-N 50439674 RICOLINOSTAT::US10858323, Compound 2::US11207431, Example E::US8609678, 2-(diphenylamino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [26] Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50439674 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50439674&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search AH4 5WGL 53340666 175451991 ZINC89630354 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51398808 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1Cl InChI=1S/C24H26ClN5O3/c25-20-12-7-8-13-21(20)30(19-10-4-3-5-11-19)24-27-16-18(17-28-24)23(32)26-15-9-2-1-6-14-22(31)29-33/h3-5,7-8,10-13,16-17,33H,1-2,6,9,14-15H2,(H,26,32)(H,29,31) VLIUIBXPEDFJRF-UHFFFAOYSA-N 110036 US8609678, 2-((2-chlorophenyl)(phenyl)amino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [89] Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=110036 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=110036&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 53340426 186526906 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51398826 CCN(CC)Cc1ccc2cc(COC(=O)Nc3ccc(cc3)C(=O)NO)ccc2c1 InChI=1S/C24H27N3O4/c1-3-27(4-2)15-17-5-7-21-14-18(6-8-20(21)13-17)16-31-24(29)25-22-11-9-19(10-12-22)23(28)26-30/h5-14,30H,3-4,15-16H2,1-2H3,(H,25,29)(H,26,28) YALNUENQHAQXEA-UHFFFAOYSA-N 50105329 CHEMBL1213492 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105329 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105329&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search QCM 6UOC 9804992 318590495 CHEMBL1213492 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51398836 CN(C)Cc1c(oc2ccccc12)C(=O)NCCOc1ccc(cc1)C(=O)NO InChI=1S/C21H23N3O5/c1-24(2)13-17-16-5-3-4-6-18(16)29-19(17)21(26)22-11-12-28-15-9-7-14(8-10-15)20(25)23-27/h3-10,27H,11-13H2,1-2H3,(H,22,26)(H,23,25) MAUCONCHVWBMHK-UHFFFAOYSA-N 24622 3-[(dimethylamino)methyl]-N-{2-[4-(hydroxycarbamoyl)phenoxy]ethyl}-1-benzofuran-2-carboxamide::CRA-024781 Histone deacetylase 4 Homo sapiens 60 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=24622 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=24622&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11749858 56269573 ZINC06716700 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51398837 Cn1cc(CNCC2CCN(CC2)c2ncc(cn2)C(=O)NO)c2ccccc12 InChI=1S/C21H26N6O2/c1-26-14-17(18-4-2-3-5-19(18)26)11-22-10-15-6-8-27(9-7-15)21-23-12-16(13-24-21)20(28)25-29/h2-5,12-15,22,29H,6-11H2,1H3,(H,25,28) PAWIYAYFNXQGAP-UHFFFAOYSA-N 50105327 JNJ-26481585::Quisinostat Histone deacetylase 4 Homo sapiens 0.600000 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105327 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105327&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search GOK 7Q1B,6HSK,6HSH 11538455 318590494 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51398858 COc1ccc(cn1)-c1nc(N2CCOCC2)c2sc(CN(C)c3ncc(cn3)C(=O)NO)cc2n1 InChI=1S/C23H24N8O4S/c1-30(23-25-11-15(12-26-23)22(32)29-33)13-16-9-17-19(36-16)21(31-5-7-35-8-6-31)28-20(27-17)14-3-4-18(34-2)24-10-14/h3-4,9-12,33H,5-8,13H2,1-2H3,(H,29,32) JOWXJLIFIIOYMS-UHFFFAOYSA-N 50188961 CHEMBL3622533 Histone deacetylase 4 Homo sapiens 409 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50188961 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50188961&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 54575456 104072687 CHEMBL3622533 ZINC13444145 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51398869 Nc1ccccc1NC(=O)c1ccc(CNC(=O)OCc2cccnc2)cc1 InChI=1S/C21H20N4O3/c22-18-5-1-2-6-19(18)25-20(26)17-9-7-15(8-10-17)13-24-21(27)28-14-16-4-3-11-23-12-16/h1-12H,13-14,22H2,(H,24,27)(H,25,26) INVTYAOGFAGBOE-UHFFFAOYSA-N 19410 CHEMBL27759::MS-275::US11377423, MS-275::US11672788, Compound Entinostat::US9265734, MS-275::US9796664, Compound MS-275::benzamide-type inhibitor, 3::pyridin-3-ylmethyl N-({4-[(2-aminophenyl)carbamoyl]phenyl}methyl)carbamate Histone deacetylase 4 Homo sapiens >10.0 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19410 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19410&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4261 46519433 CHEMBL27759 7007 ZINC01488870 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51398877 Nc1ccccc1NC(=O)c1ccc(CNc2nccc(n2)-c2cccnc2)cc1 InChI=1S/C23H20N6O/c24-19-5-1-2-6-21(19)28-22(30)17-9-7-16(8-10-17)14-27-23-26-13-11-20(29-23)18-4-3-12-25-15-18/h1-13,15H,14,24H2,(H,28,30)(H,26,27,29) HRNLUBSXIHFDHP-UHFFFAOYSA-N 24624 CHEMBL272980::MGCD-0103::MGCD0103::N-(2-aminophenyl)-4-({[4-(pyridin-3-yl)pyrimidin-2-yl]amino}methyl)benzamide::US10227295, Compound MGCD0103::US11377423, MGCD-0103::US9409858, MGCD0103::US9751832, MGCD0103::US9956192, Compound MGCD0103 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=24624 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=24624&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 9865515 56269575 CHEMBL272980 7008 ZINC13986811 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51398886 Cn1cc(cn1)-c1ccc(cc1)S(=O)(=O)n1ccc(\C=C\C(=O)Nc2ccccc2N)c1 InChI=1S/C23H21N5O3S/c1-27-16-19(14-25-27)18-7-9-20(10-8-18)32(30,31)28-13-12-17(15-28)6-11-23(29)26-22-5-3-2-4-21(22)24/h2-16H,24H2,1H3,(H,26,29)/b11-6+ PRXXYMVLYKJITB-IZZDOVSWSA-N 50470579 4sc-202::Domatinostat Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50470579 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50470579&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 15985904 433937844 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51398910 CCCCNNC(=O)c1ccc(Br)cc1 InChI=1S/C11H15BrN2O/c1-2-3-8-13-14-11(15)9-4-6-10(12)7-5-9/h4-7,13H,2-3,8H2,1H3,(H,14,15) BVQCFCYPFJOOAV-UHFFFAOYSA-N 163619 UF010::US10807944, Compound UF010 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=163619 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=163619&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4596836 310305336 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51398922 N=C1Sc2ccccc2C2=NCCCN12 InChI=1S/C11H11N3S/c12-11-14-7-3-6-13-10(14)8-4-1-2-5-9(8)15-11/h1-2,4-5,12H,3,6-7H2 JNENSSREQFBZGT-UHFFFAOYSA-N 50565138 CHEMBL595227::PD-404182 Histone deacetylase 4 Homo sapiens 9000 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50565138 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50565138&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6603967 461685476 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51398926 COc1cccc2n(C)c(=O)c(C(=O)N(C)c3ccc(cc3)C(F)(F)F)c(O)c12 InChI=1S/C20H17F3N2O4/c1-24(12-9-7-11(8-10-12)20(21,22)23)18(27)16-17(26)15-13(25(2)19(16)28)5-4-6-14(15)29-3/h4-10,26H,1-3H3 ONDYALNGTUAJDX-UHFFFAOYSA-N 50565139 Tasquinimod Histone deacetylase 4 Homo sapiens 10.0 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50565139 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50565139&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 54682876 461685477 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51398928 Nc1ccc(cc1NC(=O)c1ccc2nc(ccc2c1)N1CCNCC1)-c1cccs1 InChI=1S/C24H23N5OS/c25-19-6-3-17(22-2-1-13-31-22)15-21(19)28-24(30)18-4-7-20-16(14-18)5-8-23(27-20)29-11-9-26-10-12-29/h1-8,13-15,26H,9-12,25H2,(H,28,30) VURDNNVAYZDGDK-UHFFFAOYSA-N 182757 US9145412, Table 1, Compound 23 Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=182757 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=182757&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72374405 313634280 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51398937 CC(=O)Nc1ccc(cc1)C(=O)Nc1ccc(F)cc1N InChI=1S/C15H14FN3O2/c1-9(20)18-12-5-2-10(3-6-12)15(21)19-14-7-4-11(16)8-13(14)17/h2-8H,17H2,1H3,(H,18,20)(H,19,21) RRJDFENBXIEAPD-UHFFFAOYSA-N 178100 BRD3308::US11377423, Cmpd 1 Histone deacetylase 4 Homo sapiens >30000 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=178100 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=178100&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72734382 313063491 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51398951 CN1CCc2c(C1)c1ccccc1n2Cc1ccc(cc1)C(=O)NO InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::Tubastatin A::US10227295, Compound Tubastatin A::US10456394, Tubastatin A::US11207431, Example D::US8748451, 6::US9249087, Tubacin::US9751832, Tubastatin A::US9956192, Compound Tubastatin-A Histone deacetylase 4 Homo sapiens 3000 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 ZINC51951670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51398952 ONC(=O)c1ccc(CN2CCCc3cc(Cl)ccc23)cc1 InChI=1S/C17H17ClN2O2/c18-15-7-8-16-14(10-15)2-1-9-20(16)11-12-3-5-13(6-4-12)17(21)19-22/h3-8,10,22H,1-2,9,11H2,(H,19,21) MNAYBFFSFQRSIT-UHFFFAOYSA-N 417049 4-((6-chloro-3,4-dihydroquinolin-1(2H)-yl)methyl)-N-hydroxybenzamide::US10456394, Example 2 Histone deacetylase 4 Homo sapiens 11000 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=417049 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=417049&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 130345472 433916959 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51398974 COc1ccc(Cn2ccc3ccc(cc23)C(=O)NO)cc1 InChI=1S/C17H16N2O3/c1-22-15-6-2-12(3-7-15)11-19-9-8-13-4-5-14(10-16(13)19)17(20)18-21/h2-10,21H,11H2,1H3,(H,18,20) AJRGHIGYPXNABY-UHFFFAOYSA-N 50397360 CHEMBL2170177::US10188756, Compound CN110 Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50397360 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50397360&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search GKW 6HQY,6HSF 24753719 163346384 CHEMBL2170177 ZINC43178454 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51398975 COc1ccc(\C=C\C(=O)NO)c(c1)-c1ccc(cc1)-c1ccccc1 InChI=1S/C22H19NO3/c1-26-20-13-11-19(12-14-22(24)23-25)21(15-20)18-9-7-17(8-10-18)16-5-3-2-4-6-16/h2-15,25H,1H3,(H,23,24)/b14-12+ ASHPRZYGCOMVHO-WYMLVPIESA-N 50246866 CHEMBL4078458::US11505523, Compound 22d Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50246866 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50246866&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 70676597 401960626 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51398983 CCCCCCCCCCCCCCCCNNC(=O)c1cccs1 InChI=1S/C21H38N2OS/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-18-22-23-21(24)20-17-16-19-25-20/h16-17,19,22H,2-15,18H2,1H3,(H,23,24) HSHXDCVZWHOWCS-UHFFFAOYSA-N 50565135 CHEMBL4777961 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50565135 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50565135&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 139035087 461685473 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51399006 FC(F)(F)c1nc(no1)-c1cccc(c1)C(=O)NCC1(CCOCC1)c1nc(cs1)-c1ccccc1 InChI=1S/C25H21F3N4O3S/c26-25(27,28)22-31-20(32-35-22)17-7-4-8-18(13-17)21(33)29-15-24(9-11-34-12-10-24)23-30-19(14-36-23)16-5-2-1-3-6-16/h1-8,13-14H,9-12,15H2,(H,29,33) HORXBWNTEDOVKN-UHFFFAOYSA-N 50446481 CHEMBL3110004::US10011611, TMP269::US10722597, Compound TMP-269 Histone deacetylase 4 Homo sapiens 126 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446481 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446481&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search NU9 3ZNR 53344908 194944377 CHEMBL3110004 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51399013 Nc1cc(F)ccc1NC(=O)c1ccc(CNC(=O)\C=C\c2cccnc2)cc1 InChI=1S/C22H19FN4O2/c23-18-8-9-20(19(24)12-18)27-22(29)17-6-3-16(4-7-17)14-26-21(28)10-5-15-2-1-11-25-13-15/h1-13H,14,24H2,(H,26,28)(H,27,29)/b10-5+ SZMJVTADHFNAIS-BJMVGYQFSA-N 50457079 CS-055::CS055::Chidamide::Epidaza in China::HBI-8000::Tucidinostat::US11377423, HUYA::US11672788, Compound Chidamide Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50457079 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50457079&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 12136798 433924346 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51399014 C\C=C1/NC(=O)[C@H]2CSSCC\C=C\[C@@H](CC(=O)N[C@H](C(C)C)C(=O)N2)OC(=O)[C@@H](NC1=O)C(C)C InChI=1S/C24H36N4O6S2/c1-6-16-21(30)28-20(14(4)5)24(33)34-15-9-7-8-10-35-36-12-17(22(31)25-16)26-23(32)19(13(2)3)27-18(29)11-15/h6-7,9,13-15,17,19-20H,8,10-12H2,1-5H3,(H,25,31)(H,26,32)(H,27,29)(H,28,30)/b9-7+,16-6-/t15-,17+,19+,20-/m0/s1 OHRURASPPZQGQM-QSVHVVLASA-N 50048864 CHEMBL3310505 Histone deacetylase 4 Homo sapiens 647 ChEMBL 10.1021/acs.jmedchem.0c00830 10.7270/Q2F76H9K 32608981 Ho, TCS; Chan, AHY; Ganesan, A University of East Anglia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50048864 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50048864&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11947684 103979245 CHEMBL3310505 ZINC13745305 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51400112 COc1cc(OC)c2c(nc(nc2c1)-c1cc(C)c(OCCCCCC(=O)NO)c(C)c1)N1CCN(C)CC1 InChI=1S/C29H39N5O5/c1-19-15-21(16-20(2)27(19)39-14-8-6-7-9-25(35)32-36)28-30-23-17-22(37-4)18-24(38-5)26(23)29(31-28)34-12-10-33(3)11-13-34/h15-18,36H,6-14H2,1-5H3,(H,32,35) NTUCJWZWDDQYER-UHFFFAOYSA-N 50565547 CHEMBL4781177 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1016/j.ejmech.2020.112648 10.7270/Q2Z323DQ 32791401 Yao, D; Li, C; Jiang, J; Huang, J; Wang, J; He, Z; Zhang, J Shenzhen Technology University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50565547 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50565547&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162663441 461685885 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51400113 COc1cc(OC)c2c(nc(nc2c1)-c1cc(C)c(OCCCCCC(=O)NO)c(C)c1)N1CCS(=O)(=O)CC1 InChI=1S/C28H36N4O7S/c1-18-14-20(15-19(2)26(18)39-11-7-5-6-8-24(33)31-34)27-29-22-16-21(37-3)17-23(38-4)25(22)28(30-27)32-9-12-40(35,36)13-10-32/h14-17,34H,5-13H2,1-4H3,(H,31,33) YRUAJZFECDBHMT-UHFFFAOYSA-N 50565548 CHEMBL4790998 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1016/j.ejmech.2020.112648 10.7270/Q2Z323DQ 32791401 Yao, D; Li, C; Jiang, J; Huang, J; Wang, J; He, Z; Zhang, J Shenzhen Technology University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50565548 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50565548&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162671396 461685886 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51400114 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1016/j.ejmech.2020.112648 10.7270/Q2Z323DQ 32791401 Yao, D; Li, C; Jiang, J; Huang, J; Wang, J; He, Z; Zhang, J Shenzhen Technology University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51400171 Cl.CN(C)CCOc1ccc(cc1)-c1cc(=O)c2c(O)cc(OCCCCCC(=O)NO)cc2o1 InChI=1S/C25H30N2O7.ClH/c1-27(2)11-13-33-18-9-7-17(8-10-18)22-16-21(29)25-20(28)14-19(15-23(25)34-22)32-12-5-3-4-6-24(30)26-31;/h7-10,14-16,28,31H,3-6,11-13H2,1-2H3,(H,26,30);1H HDHBTUFDSFLMOP-UHFFFAOYSA-N 50565587 CHEMBL4798571 Histone deacetylase 4 Homo sapiens 307 ChEMBL 10.1016/j.ejmech.2020.112677 10.7270/Q2JS9V5H 32823005 Wei, M; Xie, M; Zhang, Z; Wei, Y; Zhang, J; Pan, H; Li, B; Wang, J; Song, Y; Chong, C; Zhao, R; Wang, J; Yu, L; Yang, G; Yang, C Nankai University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50565587 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50565587&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162674636 461685925 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51406384 ONC(=N)c1ccc2nc([nH]c2c1)-c1cccc(c1)-c1cn2ccccc2n1 InChI=1S/C21H16N6O/c22-20(26-28)14-7-8-16-17(11-14)25-21(24-16)15-5-3-4-13(10-15)18-12-27-9-2-1-6-19(27)23-18/h1-12,28H,(H2,22,26)(H,24,25) WEMGUFBETKXSRV-UHFFFAOYSA-N 50568243 CHEMBL4846752 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.bmc.2021.116251 10.7270/Q2BK1H5D 34116381 El-Awady, R; Saleh, E; Hamoudi, R; Ramadan, WS; Mazitschek, R; Nael, MA; Elokely, KM; Abou-Gharbia, M; Childers, WE; Srinivasulu, V; Aloum, L; Menon, V; Al-Tel, TH University of Sharjah http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50568243 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50568243&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164609294 471058388 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51406385 CC(C)(C)Nc1c(nc2ccccn12)-c1cccc(c1)-c1nc2cc(ccc2[nH]1)-c1noc(n1)C(F)(F)F InChI=1S/C27H22F3N7O/c1-26(2,3)35-24-21(33-20-9-4-5-12-37(20)24)15-7-6-8-16(13-15)22-31-18-11-10-17(14-19(18)32-22)23-34-25(38-36-23)27(28,29)30/h4-14,35H,1-3H3,(H,31,32) JAJHZQMZEXOYNC-UHFFFAOYSA-N 50568244 CHEMBL4862147 Histone deacetylase 4 Homo sapiens 1646 ChEMBL 10.1016/j.bmc.2021.116251 10.7270/Q2BK1H5D 34116381 El-Awady, R; Saleh, E; Hamoudi, R; Ramadan, WS; Mazitschek, R; Nael, MA; Elokely, KM; Abou-Gharbia, M; Childers, WE; Srinivasulu, V; Aloum, L; Menon, V; Al-Tel, TH University of Sharjah http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50568244 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50568244&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164620433 471058389 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51406386 CC(C)(C)Nc1c(nc2cnccn12)-c1cccc(c1)-c1nc2cc(ccc2[nH]1)-c1noc(n1)C(F)(F)F InChI=1S/C26H21F3N8O/c1-25(2,3)35-23-20(33-19-13-30-9-10-37(19)23)14-5-4-6-15(11-14)21-31-17-8-7-16(12-18(17)32-21)22-34-24(38-36-22)26(27,28)29/h4-13,35H,1-3H3,(H,31,32) CBLVNPKXHYVYCY-UHFFFAOYSA-N 50568245 CHEMBL4861149 Histone deacetylase 4 Homo sapiens 8000 ChEMBL 10.1016/j.bmc.2021.116251 10.7270/Q2BK1H5D 34116381 El-Awady, R; Saleh, E; Hamoudi, R; Ramadan, WS; Mazitschek, R; Nael, MA; Elokely, KM; Abou-Gharbia, M; Childers, WE; Srinivasulu, V; Aloum, L; Menon, V; Al-Tel, TH University of Sharjah http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50568245 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50568245&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164612605 471058390 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51406387 CC(C)(C)Nc1c(nc2ccccn12)-c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C20H18F3N5O/c1-19(2,3)26-17-15(24-14-6-4-5-11-28(14)17)12-7-9-13(10-8-12)16-25-18(29-27-16)20(21,22)23/h4-11,26H,1-3H3 QCKNTQLUQMEQRQ-UHFFFAOYSA-N 50568246 CHEMBL4854692 Histone deacetylase 4 Homo sapiens 3584 ChEMBL 10.1016/j.bmc.2021.116251 10.7270/Q2BK1H5D 34116381 El-Awady, R; Saleh, E; Hamoudi, R; Ramadan, WS; Mazitschek, R; Nael, MA; Elokely, KM; Abou-Gharbia, M; Childers, WE; Srinivasulu, V; Aloum, L; Menon, V; Al-Tel, TH University of Sharjah http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50568246 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50568246&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164611293 471058391 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51406388 CC(C)(C)Nc1c(nc2ccccn12)-c1cccc(c1)C(=O)Nc1ccc(F)cc1N InChI=1S/C24H24FN5O/c1-24(2,3)29-22-21(28-20-9-4-5-12-30(20)22)15-7-6-8-16(13-15)23(31)27-19-11-10-17(25)14-18(19)26/h4-14,29H,26H2,1-3H3,(H,27,31) GKGCYVKOTVLEOB-UHFFFAOYSA-N 50568247 CHEMBL4854201 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.bmc.2021.116251 10.7270/Q2BK1H5D 34116381 El-Awady, R; Saleh, E; Hamoudi, R; Ramadan, WS; Mazitschek, R; Nael, MA; Elokely, KM; Abou-Gharbia, M; Childers, WE; Srinivasulu, V; Aloum, L; Menon, V; Al-Tel, TH University of Sharjah http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50568247 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50568247&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164609642 471058392 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51406389 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.bmc.2021.116251 10.7270/Q2BK1H5D 34116381 El-Awady, R; Saleh, E; Hamoudi, R; Ramadan, WS; Mazitschek, R; Nael, MA; Elokely, KM; Abou-Gharbia, M; Childers, WE; Srinivasulu, V; Aloum, L; Menon, V; Al-Tel, TH University of Sharjah http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51406390 FC(F)(F)c1nc(no1)-c1ccc(cc1)C(=O)NC1CCN(Cc2ccccc2)C1 InChI=1S/C21H19F3N4O2/c22-21(23,24)20-26-18(27-30-20)15-6-8-16(9-7-15)19(29)25-17-10-11-28(13-17)12-14-4-2-1-3-5-14/h1-9,17H,10-13H2,(H,25,29) LGDCOYCPANTWSM-UHFFFAOYSA-N 50568248 CHEMBL4879105 Histone deacetylase 4 Homo sapiens 19 ChEMBL 10.1016/j.bmc.2021.116251 10.7270/Q2BK1H5D 34116381 El-Awady, R; Saleh, E; Hamoudi, R; Ramadan, WS; Mazitschek, R; Nael, MA; Elokely, KM; Abou-Gharbia, M; Childers, WE; Srinivasulu, V; Aloum, L; Menon, V; Al-Tel, TH University of Sharjah http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50568248 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50568248&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164626703 471058393 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51419779 ONC(=O)c1ccc(Cn2nnnc2-c2cccs2)cc1 InChI=1S/C13H11N5O2S/c19-13(15-20)10-5-3-9(4-6-10)8-18-12(14-16-17-18)11-2-1-7-21-11/h1-7,20H,8H2,(H,15,19) UFUGFWWXDWPEQE-UHFFFAOYSA-N 50531020 CHEMBL4448410 Histone deacetylase 4 Homo sapiens 3068 ChEMBL 10.1021/acsmedchemlett.1c00425 10.7270/Q2639THK 34795871 Sandrone, G; Cukier, CD; Zrubek, K; Marchini, M; Vergani, B; Caprini, G; Fossati, G; Steinkühler, C; Stevenazzi, A Italfarmaco S.p.A http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531020 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531020&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search UZW 7O2P 135357843 440739602 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51419780 ONC(=O)c1cc(F)c(Cn2nnnc2-c2cccs2)c(F)c1 InChI=1S/C13H9F2N5O2S/c14-9-4-7(13(21)17-22)5-10(15)8(9)6-20-12(16-18-19-20)11-2-1-3-23-11/h1-5,22H,6H2,(H,17,21) RCMJXOWHNPWZBG-UHFFFAOYSA-N 50573491 CHEMBL4862563 Histone deacetylase 4 Homo sapiens 660 ChEMBL 10.1021/acsmedchemlett.1c00425 10.7270/Q2639THK 34795871 Sandrone, G; Cukier, CD; Zrubek, K; Marchini, M; Vergani, B; Caprini, G; Fossati, G; Steinkühler, C; Stevenazzi, A Italfarmaco S.p.A http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50573491 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50573491&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 135357552 471063636 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51419781 ONC(=O)c1ccc(Cn2nnc(n2)-c2ncccn2)cc1 InChI=1S/C13H11N7O2/c21-13(18-22)10-4-2-9(3-5-10)8-20-17-12(16-19-20)11-14-6-1-7-15-11/h1-7,22H,8H2,(H,18,21) PMHARNDBRDSPAO-UHFFFAOYSA-N 50531013 CHEMBL4453121 Histone deacetylase 4 Homo sapiens 4601 ChEMBL 10.1021/acsmedchemlett.1c00425 10.7270/Q2639THK 34795871 Sandrone, G; Cukier, CD; Zrubek, K; Marchini, M; Vergani, B; Caprini, G; Fossati, G; Steinkühler, C; Stevenazzi, A Italfarmaco S.p.A http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531013 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531013&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 135357654 440739595 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51419782 ONC(=O)c1cc(F)c(Cn2nnc(n2)-c2ncccn2)c(F)c1 InChI=1S/C13H9F2N7O2/c14-9-4-7(13(23)20-24)5-10(15)8(9)6-22-19-12(18-21-22)11-16-2-1-3-17-11/h1-5,24H,6H2,(H,20,23) IAJVLFQKWJCAML-UHFFFAOYSA-N 50531051 CHEMBL4470373 Histone deacetylase 4 Homo sapiens 562 ChEMBL 10.1021/acsmedchemlett.1c00425 10.7270/Q2639THK 34795871 Sandrone, G; Cukier, CD; Zrubek, K; Marchini, M; Vergani, B; Caprini, G; Fossati, G; Steinkühler, C; Stevenazzi, A Italfarmaco S.p.A http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531051 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531051&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search V05 7O2R 155534057 440739633 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51414538 ONC(=O)CCCCCONC(=O)c1cc2ccccc2[nH]1 InChI=1S/C15H19N3O4/c19-14(17-21)8-2-1-5-9-22-18-15(20)13-10-11-6-3-4-7-12(11)16-13/h3-4,6-7,10,16,21H,1-2,5,8-9H2,(H,17,19)(H,18,20) ONBTZOITFPUQHO-UHFFFAOYSA-N 50571348 CHEMBL4850081 Histone deacetylase 4 Homo sapiens 55700 ChEMBL 10.1016/j.ejmech.2020.113095 10.7270/Q22Z1991 33360560 Alves Avelar, LA; Schrenk, C; Sönnichsen, M; Hamacher, A; Hansen, FK; Schliehe-Diecks, J; Borkhardt, A; Bhatia, S; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50571348 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50571348&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164613889 471061493 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51414539 ONC(=O)CCCCCONC(=O)c1ccc2ccccc2n1 InChI=1S/C16H19N3O4/c20-15(18-22)8-2-1-5-11-23-19-16(21)14-10-9-12-6-3-4-7-13(12)17-14/h3-4,6-7,9-10,22H,1-2,5,8,11H2,(H,18,20)(H,19,21) BCYYHAWIHKEKFQ-UHFFFAOYSA-N 50571357 CHEMBL4866536 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.ejmech.2020.113095 10.7270/Q22Z1991 33360560 Alves Avelar, LA; Schrenk, C; Sönnichsen, M; Hamacher, A; Hansen, FK; Schliehe-Diecks, J; Borkhardt, A; Bhatia, S; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50571357 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50571357&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164621418 471061502 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51414540 ONC(=O)CCCCCONC(=O)c1nccc2ccccc12 InChI=1S/C16H19N3O4/c20-14(18-22)8-2-1-5-11-23-19-16(21)15-13-7-4-3-6-12(13)9-10-17-15/h3-4,6-7,9-10,22H,1-2,5,8,11H2,(H,18,20)(H,19,21) BMUUUIGOTZRXBG-UHFFFAOYSA-N 50571359 CHEMBL4870868 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1016/j.ejmech.2020.113095 10.7270/Q22Z1991 33360560 Alves Avelar, LA; Schrenk, C; Sönnichsen, M; Hamacher, A; Hansen, FK; Schliehe-Diecks, J; Borkhardt, A; Bhatia, S; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50571359 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50571359&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164618589 471061504 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51414541 ONC(=O)CCCCCONC(=O)c1cnc2ccccc2n1 InChI=1S/C15H18N4O4/c20-14(18-22)8-2-1-5-9-23-19-15(21)13-10-16-11-6-3-4-7-12(11)17-13/h3-4,6-7,10,22H,1-2,5,8-9H2,(H,18,20)(H,19,21) LUTFGXARJQOWLQ-UHFFFAOYSA-N 50571360 CHEMBL4875953 Histone deacetylase 4 Homo sapiens 60800 ChEMBL 10.1016/j.ejmech.2020.113095 10.7270/Q22Z1991 33360560 Alves Avelar, LA; Schrenk, C; Sönnichsen, M; Hamacher, A; Hansen, FK; Schliehe-Diecks, J; Borkhardt, A; Bhatia, S; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50571360 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50571360&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164625953 471061505 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51414542 ONC(=O)CCCCCONC(=O)c1ccc2ccccc2c1 InChI=1S/C17H20N2O4/c20-16(18-22)8-2-1-5-11-23-19-17(21)15-10-9-13-6-3-4-7-14(13)12-15/h3-4,6-7,9-10,12,22H,1-2,5,8,11H2,(H,18,20)(H,19,21) YDGNQLWJPVIXKO-UHFFFAOYSA-N 50571361 CHEMBL4876405 Histone deacetylase 4 Homo sapiens 51800 ChEMBL 10.1016/j.ejmech.2020.113095 10.7270/Q22Z1991 33360560 Alves Avelar, LA; Schrenk, C; Sönnichsen, M; Hamacher, A; Hansen, FK; Schliehe-Diecks, J; Borkhardt, A; Bhatia, S; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50571361 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50571361&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164626366 471061506 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51414543 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 47800 ChEMBL 10.1016/j.ejmech.2020.113095 10.7270/Q22Z1991 33360560 Alves Avelar, LA; Schrenk, C; Sönnichsen, M; Hamacher, A; Hansen, FK; Schliehe-Diecks, J; Borkhardt, A; Bhatia, S; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51414544 ONC(=O)C(c1ccc(cc1)-c1ncc(cn1)C(F)(F)F)c1ccccc1F InChI=1S/C19H13F4N3O2/c20-15-4-2-1-3-14(15)16(18(27)26-28)11-5-7-12(8-6-11)17-24-9-13(10-25-17)19(21,22)23/h1-10,16,28H,(H,26,27) LMGDHGQJJLEAPQ-UHFFFAOYSA-N 50503690 CHEMBL4456445 Histone deacetylase 4 Homo sapiens 450 ChEMBL 10.1016/j.ejmech.2020.113095 10.7270/Q22Z1991 33360560 Alves Avelar, LA; Schrenk, C; Sönnichsen, M; Hamacher, A; Hansen, FK; Schliehe-Diecks, J; Borkhardt, A; Bhatia, S; Kassack, MU; Kurz, T Heinrich-Heine-Universit£t D£sseldorf http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503690 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503690&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 81689842 440712275 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412696 ONC(=O)c1ccc(CN2c3ccccc3Sc3ccccc23)cc1 InChI=1S/C20H16N2O2S/c23-20(21-24)15-11-9-14(10-12-15)13-22-16-5-1-3-7-18(16)25-19-8-4-2-6-17(19)22/h1-12,24H,13H2,(H,21,23) MKMZJKFJHZVYQT-UHFFFAOYSA-N 50517568 CHEMBL4438566 Histone deacetylase 4 Homo sapiens >40000 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50517568 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50517568&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 141733188 440726150 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412697 ONC(=O)c1ccc(CN2c3ccccc3Sc3ccc(Cl)cc23)cc1 InChI=1S/C20H15ClN2O2S/c21-15-9-10-19-17(11-15)23(16-3-1-2-4-18(16)26-19)12-13-5-7-14(8-6-13)20(24)22-25/h1-11,25H,12H2,(H,22,24) MTMFVZNBGMTGHQ-UHFFFAOYSA-N 50517570 CHEMBL4530950 Histone deacetylase 4 Homo sapiens 3600 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50517570 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50517570&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155546107 440726152 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412698 ONC(=O)c1ccc(CN2c3ccccc3Sc3ccc(cc23)C(F)(F)F)cc1 InChI=1S/C21H15F3N2O2S/c22-21(23,24)15-9-10-19-17(11-15)26(16-3-1-2-4-18(16)29-19)12-13-5-7-14(8-6-13)20(27)25-28/h1-11,28H,12H2,(H,25,27) GRKNLMXQUPJNQM-UHFFFAOYSA-N 50517565 CHEMBL4472834 Histone deacetylase 4 Homo sapiens 7590 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50517565 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50517565&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155535974 440726147 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412699 COc1ccc2Sc3ccccc3N(Cc3ccc(cc3)C(=O)NO)c2c1 InChI=1S/C21H18N2O3S/c1-26-16-10-11-20-18(12-16)23(17-4-2-3-5-19(17)27-20)13-14-6-8-15(9-7-14)21(24)22-25/h2-12,25H,13H2,1H3,(H,22,24) WIQDMYVWEJAYQM-UHFFFAOYSA-N 50517567 CHEMBL4545246 Histone deacetylase 4 Homo sapiens 4760 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50517567 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50517567&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155553215 440726149 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412700 CSc1ccc2Sc3ccccc3N(Cc3ccc(cc3)C(=O)NO)c2c1 InChI=1S/C21H18N2O2S2/c1-26-16-10-11-20-18(12-16)23(17-4-2-3-5-19(17)27-20)13-14-6-8-15(9-7-14)21(24)22-25/h2-12,25H,13H2,1H3,(H,22,24) AZSLZMAUZIBWOG-UHFFFAOYSA-N 50570667 CHEMBL4877300 Histone deacetylase 4 Homo sapiens 5800 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50570667 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50570667&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164629157 471060812 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412701 NC(=O)c1ccc2Sc3ccccc3N(Cc3ccc(cc3)C(=O)NO)c2c1 InChI=1S/C21H17N3O3S/c22-20(25)15-9-10-19-17(11-15)24(16-3-1-2-4-18(16)28-19)12-13-5-7-14(8-6-13)21(26)23-27/h1-11,27H,12H2,(H2,22,25)(H,23,26) QZBVZNKZPACUDP-UHFFFAOYSA-N 50570668 CHEMBL4862510 Histone deacetylase 4 Homo sapiens 600 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50570668 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50570668&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164625429 471060813 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412702 C\C(=N/O)c1ccc2Sc3ccccc3N(Cc3ccc(cc3)C(=O)NO)c2c1 InChI=1S/C22H19N3O3S/c1-14(23-27)17-10-11-21-19(12-17)25(18-4-2-3-5-20(18)29-21)13-15-6-8-16(9-7-15)22(26)24-28/h2-12,27-28H,13H2,1H3,(H,24,26)/b23-14+ VHJKUBXNSBFZJV-OEAKJJBVSA-N 50570669 CHEMBL4877805 Histone deacetylase 4 Homo sapiens 3850 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50570669 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50570669&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164626034 471060814 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412703 ONC(=O)c1ccc(CN2c3ccccc3[S+]([O-])c3ccccc23)cc1 InChI=1S/C20H16N2O3S/c23-20(21-24)15-11-9-14(10-12-15)13-22-16-5-1-3-7-18(16)26(25)19-8-4-2-6-17(19)22/h1-12,24H,13H2,(H,21,23) PXJSYQWAMWAEEN-UHFFFAOYSA-N 50517575 CHEMBL4473451 Histone deacetylase 4 Homo sapiens 6620 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50517575 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50517575&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155536301 440726157 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412704 ONC(=O)c1ccc(CN2c3ccccc3[S+]([O-])c3ccc(Cl)cc23)cc1 InChI=1S/C20H15ClN2O3S/c21-15-9-10-19-17(11-15)23(16-3-1-2-4-18(16)27(19)26)12-13-5-7-14(8-6-13)20(24)22-25/h1-11,25H,12H2,(H,22,24) JNLOBRPTWNLUDP-UHFFFAOYSA-N 50570670 CHEMBL4874671 Histone deacetylase 4 Homo sapiens 11620 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50570670 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50570670&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164625685 471060815 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412705 ONC(=O)c1ccc(CN2c3ccccc3[S+]([O-])c3ccc(cc23)C(F)(F)F)cc1 InChI=1S/C21H15F3N2O3S/c22-21(23,24)15-9-10-19-17(11-15)26(16-3-1-2-4-18(16)30(19)29)12-13-5-7-14(8-6-13)20(27)25-28/h1-11,28H,12H2,(H,25,27) NLSSVOKSELRTJW-UHFFFAOYSA-N 50570671 CHEMBL4877023 Histone deacetylase 4 Homo sapiens >40000 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50570671 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50570671&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164627475 471060816 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412706 COc1ccc2[S+]([O-])c3ccccc3N(Cc3ccc(cc3)C(=O)NO)c2c1 InChI=1S/C21H18N2O4S/c1-27-16-10-11-20-18(12-16)23(17-4-2-3-5-19(17)28(20)26)13-14-6-8-15(9-7-14)21(24)22-25/h2-12,25H,13H2,1H3,(H,22,24) MJWCDRMPNYBCEJ-UHFFFAOYSA-N 50570672 CHEMBL4858210 Histone deacetylase 4 Homo sapiens 21860 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50570672 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50570672&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164611961 471060817 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412707 CSc1ccc2[S+]([O-])c3ccccc3N(Cc3ccc(cc3)C(=O)NO)c2c1 InChI=1S/C21H18N2O3S2/c1-27-16-10-11-20-18(12-16)23(17-4-2-3-5-19(17)28(20)26)13-14-6-8-15(9-7-14)21(24)22-25/h2-12,25H,13H2,1H3,(H,22,24) BXNQLYZTLIIXAP-UHFFFAOYSA-N 50570673 CHEMBL4872697 Histone deacetylase 4 Homo sapiens >40000 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50570673 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50570673&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164619071 471060818 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412708 NC(=O)c1ccc2[S+]([O-])c3ccccc3N(Cc3ccc(cc3)C(=O)NO)c2c1 InChI=1S/C21H17N3O4S/c22-20(25)15-9-10-19-17(11-15)24(16-3-1-2-4-18(16)29(19)28)12-13-5-7-14(8-6-13)21(26)23-27/h1-11,27H,12H2,(H2,22,25)(H,23,26) GHZDPJSQRIMLOB-UHFFFAOYSA-N 50570674 CHEMBL4847771 Histone deacetylase 4 Homo sapiens 12940 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50570674 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50570674&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164616061 471060819 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412709 C\C(=N/O)c1ccc2[S+]([O-])c3ccccc3N(Cc3ccc(cc3)C(=O)NO)c2c1 InChI=1S/C22H19N3O4S/c1-14(23-27)17-10-11-21-19(12-17)25(18-4-2-3-5-20(18)30(21)29)13-15-6-8-16(9-7-15)22(26)24-28/h2-12,27-28H,13H2,1H3,(H,24,26)/b23-14+ CCKKWDXFXMBWJL-OEAKJJBVSA-N 50570675 CHEMBL4846564 Histone deacetylase 4 Homo sapiens >40000 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50570675 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50570675&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164609512 471060820 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412710 NC(=O)c1ccc2Sc3ccccc3N(Cc3ccc(\C=C\C(=O)NO)cc3)c2c1 InChI=1S/C23H19N3O3S/c24-23(28)17-10-11-21-19(13-17)26(18-3-1-2-4-20(18)30-21)14-16-7-5-15(6-8-16)9-12-22(27)25-29/h1-13,29H,14H2,(H2,24,28)(H,25,27)/b12-9+ ZPGFFUPJVVYKGI-FMIVXFBMSA-N 50570676 CHEMBL4859992 Histone deacetylase 4 Homo sapiens 3260 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50570676 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50570676&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164618031 471060821 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412711 ONC(=O)c1ccc(CN2c3ccccc3Sc3ccc(cc23)C(=O)Nc2ccccn2)cc1 InChI=1S/C26H20N4O3S/c31-25(28-24-7-3-4-14-27-24)19-12-13-23-21(15-19)30(20-5-1-2-6-22(20)34-23)16-17-8-10-18(11-9-17)26(32)29-33/h1-15,33H,16H2,(H,29,32)(H,27,28,31) XIGDWHNBRJVSHI-UHFFFAOYSA-N 50570677 CHEMBL4852441 Histone deacetylase 4 Homo sapiens 1440 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50570677 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50570677&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164617889 471060822 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412712 Cc1ccc(NC(=O)c2ccc3Sc4ccccc4N(Cc4ccc(cc4)C(=O)NO)c3c2)nc1 InChI=1S/C27H22N4O3S/c1-17-6-13-25(28-15-17)29-26(32)20-11-12-24-22(14-20)31(21-4-2-3-5-23(21)35-24)16-18-7-9-19(10-8-18)27(33)30-34/h2-15,34H,16H2,1H3,(H,30,33)(H,28,29,32) ZDGSWCNMNJYQEI-UHFFFAOYSA-N 50570678 CHEMBL4861336 Histone deacetylase 4 Homo sapiens 3810 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50570678 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50570678&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164613147 471060823 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412713 ONC(=O)c1ccc(CN2c3ccccc3Sc3ccc(cc23)C(=O)Nc2ccc(Br)cn2)cc1 InChI=1S/C26H19BrN4O3S/c27-19-10-12-24(28-14-19)29-25(32)18-9-11-23-21(13-18)31(20-3-1-2-4-22(20)35-23)15-16-5-7-17(8-6-16)26(33)30-34/h1-14,34H,15H2,(H,30,33)(H,28,29,32) IJBHQQMTDZNJTA-UHFFFAOYSA-N 50570679 CHEMBL4874716 Histone deacetylase 4 Homo sapiens 2280 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50570679 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50570679&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164626486 471060824 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412714 ONC(=O)c1ccc(Nc2c3ccccc3nc3ccc(Br)cc23)cc1 InChI=1S/C20H14BrN3O2/c21-13-7-10-18-16(11-13)19(15-3-1-2-4-17(15)23-18)22-14-8-5-12(6-9-14)20(25)24-26/h1-11,26H,(H,22,23)(H,24,25) PESSDQDERPAVNH-UHFFFAOYSA-N 50551544 CHEMBL4796066 Histone deacetylase 4 Homo sapiens 7850 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50551544 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50551544&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162673723 461681884 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51412715 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 30710 ChEMBL 10.1016/j.ejmech.2021.113419 10.7270/Q2ST7TN4 33845233 Hsu, KC; Chu, JC; Tseng, HJ; Liu, CI; Wang, HC; Lin, TE; Lee, HS; Hsin, LW; Wang, AH; Lin, CH; Huang, WJ Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51415018 ONC(=O)c1ccc(CN2CCCc3cc(Cl)ccc23)cc1 InChI=1S/C17H17ClN2O2/c18-15-7-8-16-14(10-15)2-1-9-20(16)11-12-3-5-13(6-4-12)17(21)19-22/h3-8,10,22H,1-2,9,11H2,(H,19,21) MNAYBFFSFQRSIT-UHFFFAOYSA-N 417049 4-((6-chloro-3,4-dihydroquinolin-1(2H)-yl)methyl)-N-hydroxybenzamide::US10456394, Example 2 Histone deacetylase 4 Homo sapiens 2140 ChEMBL 10.1021/acs.jmedchem.0c02210 10.7270/Q2222ZJF 33830764 Shen, S; Picci, C; Ustinova, K; Benoy, V; Kutil, Z; Zhang, G; Tavares, MT; Pavlíček, J; Zimprich, CA; Robers, MB; Van Den Bosch, L; Bařinka, C; Langley, B; Kozikowski, AP University of Illinois at Chicago http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=417049 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=417049&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 130345472 433916959 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51415019 NC(=O)c1ccc2N(Cc3ccc(cc3)C(=O)NO)CCCc2c1 InChI=1S/C18H19N3O3/c19-17(22)15-7-8-16-14(10-15)2-1-9-21(16)11-12-3-5-13(6-4-12)18(23)20-24/h3-8,10,24H,1-2,9,11H2,(H2,19,22)(H,20,23) ZRFMDXMQBRKKOA-UHFFFAOYSA-N 50571528 CHEMBL4846435 Histone deacetylase 4 Homo sapiens 454 ChEMBL 10.1021/acs.jmedchem.0c02210 10.7270/Q2222ZJF 33830764 Shen, S; Picci, C; Ustinova, K; Benoy, V; Kutil, Z; Zhang, G; Tavares, MT; Pavlíček, J; Zimprich, CA; Robers, MB; Van Den Bosch, L; Bařinka, C; Langley, B; Kozikowski, AP University of Illinois at Chicago http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50571528 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50571528&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search QRB 6ZW1 156024937 471061673 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51420975 COc1ccc(\C=C/c2cc(OC)c(OC)c(OC)c2)cc1\C=C\C(=O)Nc1ccccc1N InChI=1S/C27H28N2O5/c1-31-23-13-11-18(9-10-19-16-24(32-2)27(34-4)25(17-19)33-3)15-20(23)12-14-26(30)29-22-8-6-5-7-21(22)28/h5-17H,28H2,1-4H3,(H,29,30)/b10-9-,14-12+ LSKAICRTMVFZOZ-FMDFGENTSA-N 50574023 CHEMBL4874942 Histone deacetylase 4 Homo sapiens 310 ChEMBL 10.1016/j.ejmech.2021.113790 10.7270/Q2611453 34454126 Wang, Y; Sun, M; Wang, Y; Qin, J; Zhang, Y; Pang, Y; Yao, Y; Yang, H; Duan, Y Children's Hospital Affiliated to Zhengzhou University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50574023 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50574023&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164626307 471064168 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51420976 FC(F)(F)c1nc(no1)-c1cccc(c1)C(=O)NCC1(CCOCC1)c1nc(cs1)-c1ccccc1 InChI=1S/C25H21F3N4O3S/c26-25(27,28)22-31-20(32-35-22)17-7-4-8-18(13-17)21(33)29-15-24(9-11-34-12-10-24)23-30-19(14-36-23)16-5-2-1-3-6-16/h1-8,13-14H,9-12,15H2,(H,29,33) HORXBWNTEDOVKN-UHFFFAOYSA-N 50446481 CHEMBL3110004::US10011611, TMP269::US10722597, Compound TMP-269 Histone deacetylase 4 Homo sapiens 180 ChEMBL 10.1016/j.ejmech.2021.113790 10.7270/Q2611453 34454126 Wang, Y; Sun, M; Wang, Y; Qin, J; Zhang, Y; Pang, Y; Yao, Y; Yang, H; Duan, Y Children's Hospital Affiliated to Zhengzhou University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446481 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446481&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search NU9 3ZNR 53344908 194944377 CHEMBL3110004 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51432387 OCCN(C(=O)Cc1ccc(cc1)C(=O)NO)c1ccccc1 InChI=1S/C17H18N2O4/c20-11-10-19(15-4-2-1-3-5-15)16(21)12-13-6-8-14(9-7-13)17(22)18-23/h1-9,20,23H,10-12H2,(H,18,22) RFAZNTABYJYOAR-UHFFFAOYSA-N 198121 HPOB Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2021.113526 10.7270/Q2D79G8J 33992929 Liang, T; Xue, J; Yao, Z; Ye, Y; Yang, X; Hou, X; Fang, H Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=198121 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=198121&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5OJ 5EF7 71532921 318489194 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51432388 CCCCN(Cc1ccc(cc1)C(=O)NO)C(=O)Nc1ccccc1 InChI=1S/C19H23N3O3/c1-2-3-13-22(19(24)20-17-7-5-4-6-8-17)14-15-9-11-16(12-10-15)18(23)21-25/h4-12,25H,2-3,13-14H2,1H3,(H,20,24)(H,21,23) JZWXMCPARMXZQV-UHFFFAOYSA-N 50398716 CHEMBL2179618::US10227295, Compound 5g::US9409858, 5g::US9751832, Compound 5g::US9956192, Compound 5g Histone deacetylase 4 Homo sapiens 9390 ChEMBL 10.1016/j.ejmech.2021.113526 10.7270/Q2D79G8J 33992929 Liang, T; Xue, J; Yao, Z; Ye, Y; Yang, X; Hou, X; Fang, H Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50398716 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50398716&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N4R 5G0J,5G0I 71462653 163347740 CHEMBL2179618 ZINC95573398 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51432389 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1 InChI=1S/C24H27N5O3/c30-22(28-32)15-9-1-2-10-16-25-23(31)19-17-26-24(27-18-19)29(20-11-5-3-6-12-20)21-13-7-4-8-14-21/h3-8,11-14,17-18,32H,1-2,9-10,15-16H2,(H,25,31)(H,28,30) QGZYDVAGYRLSKP-UHFFFAOYSA-N 50439674 RICOLINOSTAT::US10858323, Compound 2::US11207431, Example E::US8609678, 2-(diphenylamino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [26] Histone deacetylase 4 Homo sapiens 7000 ChEMBL 10.1016/j.ejmech.2021.113526 10.7270/Q2D79G8J 33992929 Liang, T; Xue, J; Yao, Z; Ye, Y; Yang, X; Hou, X; Fang, H Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50439674 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50439674&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search AH4 5WGL 53340666 175451991 ZINC89630354 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51432390 OCc1ccc(cc1)[C@@H]1C[C@H](CSc2nc(c(o2)-c2ccccc2)-c2ccccc2)O[C@@H](O1)c1ccc(NC(=O)CCCCCCC(=O)NO)cc1 InChI=1S/C41H43N3O7S/c45-26-28-17-19-29(20-18-28)35-25-34(27-52-41-43-38(30-11-5-3-6-12-30)39(51-41)31-13-7-4-8-14-31)49-40(50-35)32-21-23-33(24-22-32)42-36(46)15-9-1-2-10-16-37(47)44-48/h3-8,11-14,17-24,34-35,40,45,48H,1-2,9-10,15-16,25-27H2,(H,42,46)(H,44,47)/t34-,35+,40+/m1/s1 BHUZLJOUHMBZQY-YXQOSMAKSA-N 22449 CHEMBL356769::N-(4-{(2R,4R,6S)-4-{[(4,5-diphenyl-1,3-oxazol-2-yl)sulfanyl]methyl}-6-[4-(hydroxymethyl)phenyl]-1,3-dioxan-2-yl}phenyl)-N -hydroxyoctanediamide::Tubacin::US9249087, Tubastatin A Histone deacetylase 4 Homo sapiens 17300 ChEMBL 10.1016/j.ejmech.2021.113526 10.7270/Q2D79G8J 33992929 Liang, T; Xue, J; Yao, Z; Ye, Y; Yang, X; Hou, X; Fang, H Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=22449 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=22449&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6675804 49846263 CHEMBL356769 7374 ZINC27551136 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51432391 CN1CCc2c(C1)c1ccccc1n2Cc1ccc(cc1)C(=O)NO InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::Tubastatin A::US10227295, Compound Tubastatin A::US10456394, Tubastatin A::US11207431, Example D::US8748451, 6::US9249087, Tubacin::US9751832, Tubastatin A::US9956192, Compound Tubastatin-A Histone deacetylase 4 Homo sapiens >30000 ChEMBL 10.1016/j.ejmech.2021.113526 10.7270/Q2D79G8J 33992929 Liang, T; Xue, J; Yao, Z; Ye, Y; Yang, X; Hou, X; Fang, H Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 ZINC51951670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51434502 ONC(=O)CCCO\N=C1\C(\Nc2ccccc\12)=C1\C(=O)Nc2ccccc12 InChI=1S/C20H18N4O4/c25-16(23-27)10-5-11-28-24-18-13-7-2-4-9-15(13)21-19(18)17-12-6-1-3-8-14(12)22-20(17)26/h1-4,6-9,21,27H,5,10-11H2,(H,22,26)(H,23,25)/b19-17-,24-18+ PFMKIDRZHBZULH-FTCCNZMVSA-N 50579532 CHEMBL4867598 Histone deacetylase 4 Homo sapiens >5000 ChEMBL 10.1021/acs.jmedchem.1c01311 10.7270/Q2MP574P 34624191 Cao, Z; Yang, F; Wang, J; Gu, Z; Lin, S; Wang, P; An, J; Liu, T; Li, Y; Li, Y; Lin, H; Zhao, Y; He, B Guizhou Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50579532 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50579532&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162640925 471055655 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51434503 OC(=O)CCCO\N=C1\C(\Nc2ccccc\12)=C1\C(=O)Nc2ccccc12 InChI=1S/C20H17N3O4/c24-16(25)10-5-11-27-23-18-13-7-2-4-9-15(13)21-19(18)17-12-6-1-3-8-14(12)22-20(17)26/h1-4,6-9,21H,5,10-11H2,(H,22,26)(H,24,25)/b19-17-,23-18+ FCWICHXUWNYHMX-LCLDVOFVSA-N 50579533 CHEMBL4859978 Histone deacetylase 4 Homo sapiens >5000 ChEMBL 10.1021/acs.jmedchem.1c01311 10.7270/Q2MP574P 34624191 Cao, Z; Yang, F; Wang, J; Gu, Z; Lin, S; Wang, P; An, J; Liu, T; Li, Y; Li, Y; Lin, H; Zhao, Y; He, B Guizhou Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50579533 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50579533&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164617593 471055656 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51434504 ONC(=O)CCCO\N=C1\C(\Nc2ccccc\12)=C1\C(=O)N(CC#C)c2ccccc12 InChI=1S/C23H20N4O4/c1-2-13-27-18-11-6-4-9-16(18)20(23(27)29)22-21(15-8-3-5-10-17(15)24-22)26-31-14-7-12-19(28)25-30/h1,3-6,8-11,24,30H,7,12-14H2,(H,25,28)/b22-20-,26-21+ KHLNXOSMRTVVRE-KZUJFRSNSA-N 50579534 CHEMBL4877598 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.1c01311 10.7270/Q2MP574P 34624191 Cao, Z; Yang, F; Wang, J; Gu, Z; Lin, S; Wang, P; An, J; Liu, T; Li, Y; Li, Y; Lin, H; Zhao, Y; He, B Guizhou Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50579534 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50579534&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164626029 471055657 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51434505 CN1CCc2c(C1)c1ccccc1n2Cc1ccc(cc1)C(=O)NO InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::Tubastatin A::US10227295, Compound Tubastatin A::US10456394, Tubastatin A::US11207431, Example D::US8748451, 6::US9249087, Tubacin::US9751832, Tubastatin A::US9956192, Compound Tubastatin-A Histone deacetylase 4 Homo sapiens >5000 ChEMBL 10.1021/acs.jmedchem.1c01311 10.7270/Q2MP574P 34624191 Cao, Z; Yang, F; Wang, J; Gu, Z; Lin, S; Wang, P; An, J; Liu, T; Li, Y; Li, Y; Lin, H; Zhao, Y; He, B Guizhou Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 ZINC51951670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51434506 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >5000 ChEMBL 10.1021/acs.jmedchem.1c01311 10.7270/Q2MP574P 34624191 Cao, Z; Yang, F; Wang, J; Gu, Z; Lin, S; Wang, P; An, J; Liu, T; Li, Y; Li, Y; Lin, H; Zhao, Y; He, B Guizhou Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51434568 COc1ccc(cc1OC(C(C)C)C(=O)NO)N(C)c1nc(C)nc2ccccc12 InChI=1S/C22H26N4O4/c1-13(2)20(22(27)25-28)30-19-12-15(10-11-18(19)29-5)26(4)21-16-8-6-7-9-17(16)23-14(3)24-21/h6-13,20,28H,1-5H3,(H,25,27) ZTYHIBVAHSWEEK-UHFFFAOYSA-N 50579542 CHEMBL4878408 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.1c01451 10.7270/Q2C53QPJ 34648295 Yang, L; Zhang, W; Qiu, Q; Su, Z; Tang, M; Bai, P; Si, W; Zhu, Z; Liu, Y; Yang, J; Kuang, S; Liu, J; Yan, W; Shi, M; Ye, H; Yang, Z; Chen, L West China Hospital of Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50579542 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50579542&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 163196244 471055665 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51434147 ONC(=O)c1ccc(CN2c3ccccc3Sc3ccccc23)nc1 InChI=1S/C19H15N3O2S/c23-19(21-24)13-9-10-14(20-11-13)12-22-15-5-1-3-7-17(15)25-18-8-4-2-6-16(18)22/h1-11,24H,12H2,(H,21,23) YKILUTGCNNQKON-UHFFFAOYSA-N 50579375 CHEMBL4858133 Histone deacetylase 4 Homo sapiens 5632 ChEMBL 10.1016/j.ejmech.2021.113821 10.7270/Q2HX1HHW 34517222 Wang, XX; Xie, F; Jia, CC; Yan, N; Zeng, YL; Wu, JD; Liu, ZP Shandong University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50579375 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50579375&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 141733191 471055498 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51438110 CC(C)(F)CN1CCc2cc(O)ccc2C1c1ccc(OCCCCCCC(=O)NO)cc1 InChI=1S/C26H35FN2O4/c1-26(2,27)18-29-15-14-20-17-21(30)10-13-23(20)25(29)19-8-11-22(12-9-19)33-16-6-4-3-5-7-24(31)28-32/h8-13,17,25,30,32H,3-7,14-16,18H2,1-2H3,(H,28,31) QYGMMAXPTRPJTK-UHFFFAOYSA-N 50580924 CHEMBL5090940 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1016/j.ejmech.2021.113870 10.7270/Q2BR8X1Z 34610548 Luo, G; Lin, X; Ren, S; Wu, S; Wang, X; Ma, L; Xiang, H China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50580924 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50580924&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166632391 476025929 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51438111 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 54 ChEMBL 10.1016/j.ejmech.2021.113870 10.7270/Q2BR8X1Z 34610548 Luo, G; Lin, X; Ren, S; Wu, S; Wang, X; Ma, L; Xiang, H China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51450309 Cc1cc(Nc2nc(SCc3ccc(cc3)C(=O)Nc3ccc(F)cc3N)nn3cccc23)n[nH]1 InChI=1S/C24H21FN8OS/c1-14-11-21(31-30-14)28-22-20-3-2-10-33(20)32-24(29-22)35-13-15-4-6-16(7-5-15)23(34)27-19-9-8-17(25)12-18(19)26/h2-12H,13,26H2,1H3,(H,27,34)(H2,28,29,30,31,32) FWJQLBLNLGDLIU-UHFFFAOYSA-N 50585581 CHEMBL5085693 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1016/j.ejmech.2021.114082 10.7270/Q2J38XFN 34995925 Cui, H; Huang, J; Lei, Y; Chen, Q; Hu, Z; Niu, J; Wei, R; Yang, K; Li, H; Lu, T; Zhu, Y; Huang, Y China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50585581 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50585581&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 153528580 476021668 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51454401 ONC(=O)CCCSC[C@H](NC(=O)c1ccccc1)C(=O)Nc1ccccc1 InChI=1S/C20H23N3O4S/c24-18(23-27)12-7-13-28-14-17(20(26)21-16-10-5-2-6-11-16)22-19(25)15-8-3-1-4-9-15/h1-6,8-11,17,27H,7,12-14H2,(H,21,26)(H,22,25)(H,23,24)/t17-/m0/s1 KLPIKEBAJICFPE-KRWDZBQOSA-N 50587184 CHEMBL5089854 Histone deacetylase 4 Homo sapiens >200 ChEMBL 10.1016/j.ejmech.2021.113799 10.7270/Q2V128Q6 34500130 Wang, J; Cao, Z; Wang, F; Wang, P; An, J; Fu, X; Liu, T; Li, Y; Li, Y; Zhao, Y; Lin, H; He, B Guizhou Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50587184 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50587184&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 163408803 476023271 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51454402 ONC(=O)CCCSC[C@H](NC(=O)OCc1ccccc1)C(=O)Nc1ccccc1 InChI=1S/C21H25N3O5S/c25-19(24-28)12-7-13-30-15-18(20(26)22-17-10-5-2-6-11-17)23-21(27)29-14-16-8-3-1-4-9-16/h1-6,8-11,18,28H,7,12-15H2,(H,22,26)(H,23,27)(H,24,25)/t18-/m0/s1 VGUURLUFIOIIBI-SFHVURJKSA-N 50587185 CHEMBL5093258 Histone deacetylase 4 Homo sapiens >200 ChEMBL 10.1016/j.ejmech.2021.113799 10.7270/Q2V128Q6 34500130 Wang, J; Cao, Z; Wang, F; Wang, P; An, J; Fu, X; Liu, T; Li, Y; Li, Y; Zhao, Y; Lin, H; He, B Guizhou Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50587185 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50587185&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166632483 476023272 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51454403 ONC(=O)CCCSC[C@H](NC(=O)OCc1ccccc1)C(=O)Nc1cccc2ccccc12 InChI=1S/C25H27N3O5S/c29-23(28-32)14-7-15-34-17-22(27-25(31)33-16-18-8-2-1-3-9-18)24(30)26-21-13-6-11-19-10-4-5-12-20(19)21/h1-6,8-13,22,32H,7,14-17H2,(H,26,30)(H,27,31)(H,28,29)/t22-/m0/s1 ZPFRKIBHYHVPPO-QFIPXVFZSA-N 50587186 CHEMBL5088034 Histone deacetylase 4 Homo sapiens >200 ChEMBL 10.1016/j.ejmech.2021.113799 10.7270/Q2V128Q6 34500130 Wang, J; Cao, Z; Wang, F; Wang, P; An, J; Fu, X; Liu, T; Li, Y; Li, Y; Zhao, Y; Lin, H; He, B Guizhou Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50587186 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50587186&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166634291 476023273 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51454404 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >200 ChEMBL 10.1016/j.ejmech.2021.113799 10.7270/Q2V128Q6 34500130 Wang, J; Cao, Z; Wang, F; Wang, P; An, J; Fu, X; Liu, T; Li, Y; Li, Y; Zhao, Y; Lin, H; He, B Guizhou Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51436466 Nc1ccccc1NC(=O)c1ccc(CCn2ncc3c2nc(N)n2nc(nc32)-c2ccco2)cc1 InChI=1S/C25H21N9O2/c26-18-4-1-2-5-19(18)29-24(35)16-9-7-15(8-10-16)11-12-33-22-17(14-28-33)23-30-21(20-6-3-13-36-20)32-34(23)25(27)31-22/h1-10,13-14H,11-12,26H2,(H2,27,31)(H,29,35) DZRIVOQHNGLBGP-UHFFFAOYSA-N 50580276 CHEMBL5076343 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.1c01155 10.7270/Q2R49VN3 34783558 Yan, W; Ling, L; Wu, Y; Yang, K; Liu, R; Zhang, J; Zhao, S; Zhong, G; Zhao, S; Jiang, H; Xie, C; Cheng, J ShanghaiTech University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50580276 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50580276&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 163196437 476025281 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51435856 CCCCCCCSSCC\C=C\[C@@H]1CC(=O)NCc2nc(cs2)C(=O)N\C(=C/C)C(=O)N[C@@H](CCCCN)C(=O)O1 InChI=1S/C29H45N5O5S3/c1-3-5-6-7-11-16-41-42-17-12-9-13-21-18-25(35)31-19-26-32-24(20-40-26)28(37)33-22(4-2)27(36)34-23(29(38)39-21)14-8-10-15-30/h4,9,13,20-21,23H,3,5-8,10-12,14-19,30H2,1-2H3,(H,31,35)(H,33,37)(H,34,36)/b13-9+,22-4-/t21-,23+/m1/s1 ZGKVKLQBOOZORR-AMGPRCMWSA-N 50580056 CHEMBL5086750 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.0c02161 10.7270/Q2W3816V 33745280 Zhang, K; Liu, Z; Yao, Y; Qiu, Y; Li, F; Chen, D; Hamilton, DJ; Li, Z; Jiang, S China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50580056 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50580056&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166633541 476025061 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51435857 CCCCCCCC(=O)SCC\C=C\[C@@H]1CC(=O)NCc2nc(cs2)C(=O)N\C(=C/C)C(=O)N[C@@H](C(C)C)C(=O)O1 InChI=1S/C29H42N4O6S2/c1-5-7-8-9-10-14-25(35)40-15-12-11-13-20-16-23(34)30-17-24-31-22(18-41-24)28(37)32-21(6-2)27(36)33-26(19(3)4)29(38)39-20/h6,11,13,18-20,26H,5,7-10,12,14-17H2,1-4H3,(H,30,34)(H,32,37)(H,33,36)/b13-11+,21-6-/t20-,26+/m1/s1 WCZYLKXWWUKEBA-QUDUTUPQSA-N 50123628 CHEMBL3622730 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.0c02161 10.7270/Q2W3816V 33745280 Zhang, K; Liu, Z; Yao, Y; Qiu, Y; Li, F; Chen, D; Hamilton, DJ; Li, Z; Jiang, S China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50123628 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50123628&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 60152596 104016055 CHEMBL3622730 C05752 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51446022 CCCNNC(=O)c1ccc(CNC(=O)c2cc3ccccc3[nH]2)cc1 InChI=1S/C20H22N4O2/c1-2-11-22-24-19(25)15-9-7-14(8-10-15)13-21-20(26)18-12-16-5-3-4-6-17(16)23-18/h3-10,12,22-23H,2,11,13H2,1H3,(H,21,26)(H,24,25) XGCLYPPRQZTIBB-UHFFFAOYSA-N 50584230 CHEMBL5083249 Histone deacetylase 4 Homo sapiens >5000 ChEMBL 10.1021/acs.jmedchem.1c01472 10.7270/Q28W3J6H 34942071 Jiang, Y; Xu, J; Yue, K; Huang, C; Qin, M; Chi, D; Yu, Q; Zhu, Y; Hou, X; Xu, T; Li, M; Chou, CJ; Li, X Ocean University of China http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50584230 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50584230&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 163196273 476020317 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51446023 CCCNNC(=O)c1ccc(CNC(=O)\C=C\c2ccccc2)cc1 InChI=1S/C20H23N3O2/c1-2-14-22-23-20(25)18-11-8-17(9-12-18)15-21-19(24)13-10-16-6-4-3-5-7-16/h3-13,22H,2,14-15H2,1H3,(H,21,24)(H,23,25)/b13-10+ MHZUZIALEUTHIU-JLHYYAGUSA-N 476626 N-(4-(2-propylhydrazine-1- carbonyl)benzyl)cinnamamide::US10870618, Compound 3b Histone deacetylase 4 Homo sapiens >5000 ChEMBL 10.1021/acs.jmedchem.1c01472 10.7270/Q28W3J6H 34942071 Jiang, Y; Xu, J; Yue, K; Huang, C; Qin, M; Chi, D; Yu, Q; Zhu, Y; Hou, X; Xu, T; Li, M; Chou, CJ; Li, X Ocean University of China http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=476626 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=476626&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 137700029 442076672 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51446024 Cc1[nH]c2ccccc2c1CCNCc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C21H23N3O2/c1-15-18(19-4-2-3-5-20(19)23-15)12-13-22-14-17-8-6-16(7-9-17)10-11-21(25)24-26/h2-11,22-23,26H,12-14H2,1H3,(H,24,25)/b11-10+ FPOHNWQLNRZRFC-ZHACJKMWSA-N 29589 Faridak::LBH-589::LBH-589B::Panobinostat::US10722597, Compound Panobinostat Histone deacetylase 4 Homo sapiens 203 ChEMBL 10.1021/acs.jmedchem.1c01472 10.7270/Q28W3J6H 34942071 Jiang, Y; Xu, J; Yue, K; Huang, C; Qin, M; Chi, D; Yu, Q; Zhu, Y; Hou, X; Xu, T; Li, M; Chou, CJ; Li, X Ocean University of China http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=29589 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=29589&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search LBH 5EF8 6918837 81055018 ZINC22010649 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1225840 COc1ccc(\C=C\C(=O)NO)c(c1)-c1ccc(Br)cc1 InChI=1S/C16H14BrNO3/c1-21-14-8-4-12(5-9-16(19)18-20)15(10-14)11-2-6-13(17)7-3-11/h2-10,20H,1H3,(H,18,19)/b9-5+ SUDOUVOSYKXTMX-WEVVVXLNSA-N 581349 US11505523, Compound 22b Histone deacetylase 4 Homo sapiens >20.0 US Patent 10.7270/Q2DV1PRG US11505523 Kuo, Y; Huang, W; Chang, C CITY OF HOPE; TAIPEI MEDICAL UNIVERSITY; ACADEMIA SINICA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=581349 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=581349&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 70676448 475727177 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1225847 COc1ccc(\C=C\C(=O)NO)c(c1)-c1ccc(cc1)-c1ccccc1 InChI=1S/C22H19NO3/c1-26-20-13-11-19(12-14-22(24)23-25)21(15-20)18-9-7-17(8-10-18)16-5-3-2-4-6-16/h2-15,25H,1H3,(H,23,24)/b14-12+ ASHPRZYGCOMVHO-WYMLVPIESA-N 50246866 CHEMBL4078458::US11505523, Compound 22d Histone deacetylase 4 Homo sapiens >20.0 US Patent 10.7270/Q2DV1PRG US11505523 Kuo, Y; Huang, W; Chang, C CITY OF HOPE; TAIPEI MEDICAL UNIVERSITY; ACADEMIA SINICA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50246866 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50246866&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 70676597 401960626 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1225854 COc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C10H11NO3/c1-14-9-5-2-8(3-6-9)4-7-10(12)11-13/h2-7,13H,1H3,(H,11,12)/b7-4+ BQDLTSGIXOYYHY-QPJJXVBHSA-N 23269 (2E)-N-hydroxy-3-(4-methoxyphenyl)prop-2-enamide::Cinnamic hydroxamate deriv., 13::US10188756, Compound CN87::US11505523, Compound PCI34051 Histone deacetylase 4 Homo sapiens >20.0 US Patent 10.7270/Q2DV1PRG US11505523 Kuo, Y; Huang, W; Chang, C CITY OF HOPE; TAIPEI MEDICAL UNIVERSITY; ACADEMIA SINICA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=23269 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=23269&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6433883 50091534 ZINC05298904 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51446110 ONC(=O)CCCCCCNc1nn2c(nc3ccccc3c2=O)c2ccccc12 InChI=1S/C22H23N5O3/c28-19(26-30)13-3-1-2-8-14-23-20-15-9-4-5-10-16(15)21-24-18-12-7-6-11-17(18)22(29)27(21)25-20/h4-7,9-12,30H,1-3,8,13-14H2,(H,23,25)(H,26,28) FRODMJXAOPBPTI-UHFFFAOYSA-N 50584253 CHEMBL5087773 Histone deacetylase 4 Homo sapiens 9.0 ChEMBL 10.1016/j.ejmech.2021.114058 10.7270/Q2571GWD 34954595 Liu, Q; Zhang, B; Wang, Y; Wang, X; Gou, S Southeast University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50584253 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50584253&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 163196371 476020340 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51446111 ONC(=O)CCCCCCCNc1nn2c(nc3ccccc3c2=O)c2ccccc12 InChI=1S/C23H25N5O3/c29-20(27-31)14-4-2-1-3-9-15-24-21-16-10-5-6-11-17(16)22-25-19-13-8-7-12-18(19)23(30)28(22)26-21/h5-8,10-13,31H,1-4,9,14-15H2,(H,24,26)(H,27,29) RVZPEXMXOYSXID-UHFFFAOYSA-N 50584257 CHEMBL5084865 Histone deacetylase 4 Homo sapiens 9.0 ChEMBL 10.1016/j.ejmech.2021.114058 10.7270/Q2571GWD 34954595 Liu, Q; Zhang, B; Wang, Y; Wang, X; Gou, S Southeast University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50584257 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50584257&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166633869 476020344 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441951 O=C(COc1ccc2cc(\C=C3\SC(=O)NC3=O)ccc2c1)Nc1ccccc1 InChI=1S/C22H16N2O4S/c25-20(23-17-4-2-1-3-5-17)13-28-18-9-8-15-10-14(6-7-16(15)12-18)11-19-21(26)24-22(27)29-19/h1-12H,13H2,(H,23,25)(H,24,26,27)/b19-11+ MEBKIEPFQXEEGQ-YBFXNURJSA-N 50582524 CHEMBL5089186 Histone deacetylase 4 Homo sapiens 2100 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582524 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582524&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166633634 476027529 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441952 Fc1ccc(NC(=O)COc2ccc3cc(\C=C4\SC(=O)NC4=O)ccc3c2)cc1 InChI=1S/C22H15FN2O4S/c23-16-4-6-17(7-5-16)24-20(26)12-29-18-8-3-14-9-13(1-2-15(14)11-18)10-19-21(27)25-22(28)30-19/h1-11H,12H2,(H,24,26)(H,25,27,28)/b19-10+ BQPVWJGTRGSJEM-VXLYETTFSA-N 50582525 CHEMBL5072376 Histone deacetylase 4 Homo sapiens 1600 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582525 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582525&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166630729 476027530 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441953 Cc1ccc(NC(=O)COc2ccc3cc(\C=C4\SC(=O)NC4=O)ccc3c2)cc1 InChI=1S/C23H18N2O4S/c1-14-2-7-18(8-3-14)24-21(26)13-29-19-9-6-16-10-15(4-5-17(16)12-19)11-20-22(27)25-23(28)30-20/h2-12H,13H2,1H3,(H,24,26)(H,25,27,28)/b20-11+ SZXUDKIXIBVQCU-RGVLZGJSSA-N 50582526 CHEMBL5089555 Histone deacetylase 4 Homo sapiens 1700 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582526 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582526&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166631743 476027531 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441954 COc1ccc(NC(=O)COc2ccc3cc(\C=C4\SC(=O)NC4=O)ccc3c2)cc1 InChI=1S/C23H18N2O5S/c1-29-18-8-5-17(6-9-18)24-21(26)13-30-19-7-4-15-10-14(2-3-16(15)12-19)11-20-22(27)25-23(28)31-20/h2-12H,13H2,1H3,(H,24,26)(H,25,27,28)/b20-11+ CJGFPWJALLMAFT-RGVLZGJSSA-N 50582527 CHEMBL5082287 Histone deacetylase 4 Homo sapiens 4700 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582527 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582527&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166629120 476027532 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441955 FC(F)(F)c1cccc(NC(=O)COc2ccc3cc(\C=C4\SC(=O)NC4=O)ccc3c2)c1 InChI=1S/C23H15F3N2O4S/c24-23(25,26)16-2-1-3-17(11-16)27-20(29)12-32-18-7-6-14-8-13(4-5-15(14)10-18)9-19-21(30)28-22(31)33-19/h1-11H,12H2,(H,27,29)(H,28,30,31)/b19-9+ OWYZZJNJDFOHHK-DJKKODMXSA-N 50582528 CHEMBL5086747 Histone deacetylase 4 Homo sapiens 2500 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582528 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582528&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166633538 476027533 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441956 Clc1cccc(NC(=O)COc2ccc3cc(\C=C4\SC(=O)NC4=O)ccc3c2)c1 InChI=1S/C22H15ClN2O4S/c23-16-2-1-3-17(11-16)24-20(26)12-29-18-7-6-14-8-13(4-5-15(14)10-18)9-19-21(27)25-22(28)30-19/h1-11H,12H2,(H,24,26)(H,25,27,28)/b19-9+ PNNJRMYRBULSQF-DJKKODMXSA-N 50582529 CHEMBL5082106 Histone deacetylase 4 Homo sapiens 3800 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582529 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582529&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166628380 476027534 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441957 COc1cccc(NC(=O)COc2ccc3cc(\C=C4\SC(=O)NC4=O)ccc3c2)c1 InChI=1S/C23H18N2O5S/c1-29-18-4-2-3-17(12-18)24-21(26)13-30-19-8-7-15-9-14(5-6-16(15)11-19)10-20-22(27)25-23(28)31-20/h2-12H,13H2,1H3,(H,24,26)(H,25,27,28)/b20-10+ IVIRQPXVDAKYJH-KEBDBYFISA-N 50582530 CHEMBL5090794 Histone deacetylase 4 Homo sapiens 1600 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582530 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582530&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166636440 476027535 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441958 Clc1ccc(NC(=O)COc2ccc3cc(\C=C4\SC(=O)NC4=O)ccc3c2)cc1Cl InChI=1S/C22H14Cl2N2O4S/c23-17-6-4-15(10-18(17)24)25-20(27)11-30-16-5-3-13-7-12(1-2-14(13)9-16)8-19-21(28)26-22(29)31-19/h1-10H,11H2,(H,25,27)(H,26,28,29)/b19-8+ YUPBCSPXMAZOKZ-UFWORHAWSA-N 50582531 CHEMBL5090922 Histone deacetylase 4 Homo sapiens 5500 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582531 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582531&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166632069 476027536 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441959 Fc1cc(F)c(NC(=O)COc2ccc3cc(\C=C4\SC(=O)NC4=O)ccc3c2)c(Br)c1 InChI=1S/C22H13BrF2N2O4S/c23-16-8-14(24)9-17(25)20(16)26-19(28)10-31-15-4-3-12-5-11(1-2-13(12)7-15)6-18-21(29)27-22(30)32-18/h1-9H,10H2,(H,26,28)(H,27,29,30)/b18-6+ VBAPRGNDRKQXHC-NGYBGAFCSA-N 50582532 CHEMBL5085545 Histone deacetylase 4 Homo sapiens 1100 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582532 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582532&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166631929 476027537 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441960 O=C(COc1ccc2cc(\C=C3\SC(=O)NC3=O)ccc2c1)Nc1ccccc1Oc1ccccc1 InChI=1S/C28H20N2O5S/c31-26(29-23-8-4-5-9-24(23)35-21-6-2-1-3-7-21)17-34-22-13-12-19-14-18(10-11-20(19)16-22)15-25-27(32)30-28(33)36-25/h1-16H,17H2,(H,29,31)(H,30,32,33)/b25-15+ QOTBCUOZNCNIKB-MFKUBSTISA-N 50582533 CHEMBL5091605 Histone deacetylase 4 Homo sapiens 5200 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582533 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582533&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166633360 476027538 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441961 Fc1ccc(NC(=O)COc2ccc3cc(\C=C4\SC(=O)NC4=O)ccc3c2)c(F)c1 InChI=1S/C22H14F2N2O4S/c23-15-4-6-18(17(24)10-15)25-20(27)11-30-16-5-3-13-7-12(1-2-14(13)9-16)8-19-21(28)26-22(29)31-19/h1-10H,11H2,(H,25,27)(H,26,28,29)/b19-8+ HMJUEWPAMZQNST-UFWORHAWSA-N 50582534 CHEMBL5093916 Histone deacetylase 4 Homo sapiens 3900 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582534 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582534&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166632497 476027539 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441962 Cc1cc(Br)ccc1NC(=O)COc1ccc2cc(\C=C3\SC(=O)NC3=O)ccc2c1 InChI=1S/C23H17BrN2O4S/c1-13-8-17(24)5-7-19(13)25-21(27)12-30-18-6-4-15-9-14(2-3-16(15)11-18)10-20-22(28)26-23(29)31-20/h2-11H,12H2,1H3,(H,25,27)(H,26,28,29)/b20-10+ OVYVATCIVXIUCL-KEBDBYFISA-N 50582535 CHEMBL5087514 Histone deacetylase 4 Homo sapiens 550 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582535 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582535&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166635317 476027540 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441963 O=C(COc1ccc2cc(\C=C3\SC(=O)NC3=O)ccc2c1)Nc1ccccn1 InChI=1S/C21H15N3O4S/c25-19(23-18-3-1-2-8-22-18)12-28-16-7-6-14-9-13(4-5-15(14)11-16)10-17-20(26)24-21(27)29-17/h1-11H,12H2,(H,22,23,25)(H,24,26,27)/b17-10+ SLJZGIMAOMHANO-LICLKQGHSA-N 50582536 CHEMBL5082458 Histone deacetylase 4 Homo sapiens 17000 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582536 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582536&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166628619 476027541 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441964 Cc1cccc(NC(=O)COc2ccc3cc(\C=C4\SC(=O)NC4=O)ccc3c2)n1 InChI=1S/C22H17N3O4S/c1-13-3-2-4-19(23-13)24-20(26)12-29-17-8-7-15-9-14(5-6-16(15)11-17)10-18-21(27)25-22(28)30-18/h2-11H,12H2,1H3,(H,23,24,26)(H,25,27,28)/b18-10+ WYJJUCOAYOSRKI-VCHYOVAHSA-N 50582537 CHEMBL5073824 Histone deacetylase 4 Homo sapiens 1100 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582537 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582537&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166630950 476027542 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441965 Brc1ccc(NC(=O)COc2ccc3cc(\C=C4\SC(=O)NC4=O)ccc3c2)cc1 InChI=1S/C22H15BrN2O4S/c23-16-4-6-17(7-5-16)24-20(26)12-29-18-8-3-14-9-13(1-2-15(14)11-18)10-19-21(27)25-22(28)30-19/h1-11H,12H2,(H,24,26)(H,25,27,28)/b19-10+ HBKXKIGCMXKNTC-VXLYETTFSA-N 50582538 CHEMBL5091419 Histone deacetylase 4 Homo sapiens 2900 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582538 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582538&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166635450 476027543 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441966 FC(F)(F)c1cc(Cl)cc(NC(=O)COc2ccc3cc(\C=C4\SC(=O)NC4=O)ccc3c2)c1 InChI=1S/C23H14ClF3N2O4S/c24-16-8-15(23(25,26)27)9-17(10-16)28-20(30)11-33-18-4-3-13-5-12(1-2-14(13)7-18)6-19-21(31)29-22(32)34-19/h1-10H,11H2,(H,28,30)(H,29,31,32)/b19-6+ UKAZSLMSGRZFFC-KPSZGOFPSA-N 50582539 CHEMBL5081178 Histone deacetylase 4 Homo sapiens 4000 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582539 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582539&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166627602 476027544 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441967 [O-][N+](=O)c1ccc(NC(=O)COc2ccc3cc(\C=C4\SC(=O)NC4=O)ccc3c2)cc1 InChI=1S/C22H15N3O6S/c26-20(23-16-4-6-17(7-5-16)25(29)30)12-31-18-8-3-14-9-13(1-2-15(14)11-18)10-19-21(27)24-22(28)32-19/h1-11H,12H2,(H,23,26)(H,24,27,28)/b19-10+ CZWQVHMBWIVBNF-VXLYETTFSA-N 50582540 CHEMBL5085291 Histone deacetylase 4 Homo sapiens 1700 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582540 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582540&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166631636 476027545 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441968 Fc1cc(Br)ccc1NC(=O)COc1ccc2cc(\C=C3\SC(=O)NC3=O)ccc2c1 InChI=1S/C22H14BrFN2O4S/c23-15-4-6-18(17(24)10-15)25-20(27)11-30-16-5-3-13-7-12(1-2-14(13)9-16)8-19-21(28)26-22(29)31-19/h1-10H,11H2,(H,25,27)(H,26,28,29)/b19-8+ VFAYPWCMGURCSZ-UFWORHAWSA-N 50582541 CHEMBL5084422 Histone deacetylase 4 Homo sapiens 1900 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582541 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582541&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166633845 476027546 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441969 Fc1cccc(NC(=O)COc2ccc3cc(\C=C4\SC(=O)NC4=O)ccc3c2)n1 InChI=1S/C21H14FN3O4S/c22-17-2-1-3-18(23-17)24-19(26)11-29-15-7-6-13-8-12(4-5-14(13)10-15)9-16-20(27)25-21(28)30-16/h1-10H,11H2,(H,23,24,26)(H,25,27,28)/b16-9+ XUFIBHNEQBFWHY-CXUHLZMHSA-N 50582542 CHEMBL5094339 Histone deacetylase 4 Homo sapiens 840 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582542 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582542&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166631880 476027547 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441970 Cc1cc(NC(=O)COc2ccc3cc(\C=C4\SC(=O)NC4=O)ccc3c2)no1 InChI=1S/C20H15N3O5S/c1-11-6-17(23-28-11)21-18(24)10-27-15-5-4-13-7-12(2-3-14(13)9-15)8-16-19(25)22-20(26)29-16/h2-9H,10H2,1H3,(H,21,23,24)(H,22,25,26)/b16-8+ PXLGXCHSVLXYDY-LZYBPNLTSA-N 50582543 CHEMBL5092097 Histone deacetylase 4 Homo sapiens 1700 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582543 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582543&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166635110 476027548 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441971 Cc1ccc(NC(=O)COc2ccc3cc(\C=C4\SC(=O)NC4=O)ccc3c2)cc1Cl InChI=1S/C23H17ClN2O4S/c1-13-2-6-17(11-19(13)24)25-21(27)12-30-18-7-5-15-8-14(3-4-16(15)10-18)9-20-22(28)26-23(29)31-20/h2-11H,12H2,1H3,(H,25,27)(H,26,28,29)/b20-9+ NRYSSOYGWNQTEE-AWQFTUOYSA-N 50582544 CHEMBL5073547 Histone deacetylase 4 Homo sapiens 1100 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582544 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582544&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166631050 476027549 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441972 Brc1ccc(NC(=O)COc2ccc3cc(\C=C4\SC(=O)NC4=O)ccc3c2)cc1Br InChI=1S/C22H14Br2N2O4S/c23-17-6-4-15(10-18(17)24)25-20(27)11-30-16-5-3-13-7-12(1-2-14(13)9-16)8-19-21(28)26-22(29)31-19/h1-10H,11H2,(H,25,27)(H,26,28,29)/b19-8+ JJIHQWXMKUJYSJ-UFWORHAWSA-N 50582545 CHEMBL5076630 Histone deacetylase 4 Homo sapiens 4900 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582545 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582545&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166626345 476027550 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441973 O=C(COc1ccc2cc(\C=C3\SC(=O)NC3=O)ccc2c1)Nc1nc2ccccc2s1 InChI=1S/C23H15N3O4S2/c27-20(25-22-24-17-3-1-2-4-18(17)31-22)12-30-16-8-7-14-9-13(5-6-15(14)11-16)10-19-21(28)26-23(29)32-19/h1-11H,12H2,(H,24,25,27)(H,26,28,29)/b19-10+ IYQTWZLKOHLGIY-VXLYETTFSA-N 50582546 CHEMBL5083726 Histone deacetylase 4 Homo sapiens 420 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582546 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582546&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166630289 476027551 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441974 Cc1cccc2sc(NC(=O)COc3ccc4cc(\C=C5\SC(=O)NC5=O)ccc4c3)nc12 InChI=1S/C24H17N3O4S2/c1-13-3-2-4-18-21(13)26-23(32-18)25-20(28)12-31-17-8-7-15-9-14(5-6-16(15)11-17)10-19-22(29)27-24(30)33-19/h2-11H,12H2,1H3,(H,25,26,28)(H,27,29,30)/b19-10+ JHUAWJKZVUHRNQ-VXLYETTFSA-N 50582547 CHEMBL5082258 Histone deacetylase 4 Homo sapiens 1200 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582547 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582547&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166628392 476027552 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441975 CCOc1ccc2nc(NC(=O)COc3ccc4cc(\C=C5\SC(=O)NC5=O)ccc4c3)sc2c1 InChI=1S/C25H19N3O5S2/c1-2-32-18-7-8-19-20(12-18)34-24(26-19)27-22(29)13-33-17-6-5-15-9-14(3-4-16(15)11-17)10-21-23(30)28-25(31)35-21/h3-12H,2,13H2,1H3,(H,26,27,29)(H,28,30,31)/b21-10+ NBSDHIUZKGBOSD-UFFVCSGVSA-N 50582548 CHEMBL5078917 Histone deacetylase 4 Homo sapiens 3600 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582548 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582548&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166628040 476027553 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441976 ONC(=O)C(c1ccccc1)c1ccccc1 InChI=1S/C14H13NO2/c16-14(15-17)13(11-7-3-1-4-8-11)12-9-5-2-6-10-12/h1-10,13,17H,(H,15,16) OFSBBVCLWMCGNY-UHFFFAOYSA-N 50207561 CHEMBL396097::Class IIa HDAC inhibitor, Compound 6::N-hydroxy-2,2-diphenylacetamide Histone deacetylase 4 Homo sapiens 220 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50207561 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50207561&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 239512 104084972 CHEMBL396097 ZINC04522248 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441977 COc1ccc(Cn2ccc3ccc(cc23)C(=O)NO)cc1 InChI=1S/C17H16N2O3/c1-22-15-6-2-12(3-7-15)11-19-9-8-13-4-5-14(10-16(13)19)17(20)18-21/h2-10,21H,11H2,1H3,(H,18,20) AJRGHIGYPXNABY-UHFFFAOYSA-N 50397360 CHEMBL2170177::US10188756, Compound CN110 Histone deacetylase 4 Homo sapiens 10000 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50397360 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50397360&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search GKW 6HQY,6HSF 24753719 163346384 CHEMBL2170177 ZINC43178454 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441978 O=C(CN1C(=O)S\C(=C\c2ccccn2)C1=O)Nc1nc2ccccc2s1 InChI=1S/C18H12N4O3S2/c23-15(21-17-20-12-6-1-2-7-13(12)26-17)10-22-16(24)14(27-18(22)25)9-11-5-3-4-8-19-11/h1-9H,10H2,(H,20,21,23)/b14-9+ UZIRFWMKGFFXMC-NTEUORMPSA-N 50582549 CHEMBL5090204 Histone deacetylase 4 Homo sapiens 9300 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582549 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582549&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164517150 476027554 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441979 [O-][N+](=O)c1ccc(NC(=O)COc2ccc3ccccc3c2\C=C2/SC(=O)NC2=O)cc1 InChI=1S/C22H15N3O6S/c26-20(23-14-6-8-15(9-7-14)25(29)30)12-31-18-10-5-13-3-1-2-4-16(13)17(18)11-19-21(27)24-22(28)32-19/h1-11H,12H2,(H,23,26)(H,24,27,28)/b19-11- QZBGUHPXVNINFZ-ODLFYWEKSA-N 50582550 CHEMBL5085184 Histone deacetylase 4 Homo sapiens 15000 ChEMBL 10.1021/acs.jmedchem.1c00491 10.7270/Q2X352B7 34006099 Tilekar, K; Hess, JD; Upadhyay, N; Bianco, AL; Schweipert, M; Laghezza, A; Loiodice, F; Meyer-Almes, FJ; Aguilera, RJ; Lavecchia, A; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582550 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582550&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166634510 476027555 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441559 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 63 ChEMBL 10.1021/acs.jmedchem.0c02111 10.7270/Q26M3BQC 33586434 Liang, X; Tang, S; Liu, X; Liu, Y; Xu, Q; Wang, X; Saidahmatov, A; Li, C; Wang, J; Zhou, Y; Zhang, Y; Geng, M; Huang, M; Liu, H Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51441560 ONC(=O)CCCCCCn1cc(Nc2ncc3ccn(Cc4ccccc4F)c3n2)cn1 InChI=1S/C23H26FN7O2/c24-20-8-5-4-7-18(20)15-30-12-10-17-13-25-23(28-22(17)30)27-19-14-26-31(16-19)11-6-2-1-3-9-21(32)29-33/h4-5,7-8,10,12-14,16,33H,1-3,6,9,11,15H2,(H,29,32)(H,25,27,28) PVNSNCSGKMVGSM-UHFFFAOYSA-N 50582354 CHEMBL5076728 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.0c02111 10.7270/Q26M3BQC 33586434 Liang, X; Tang, S; Liu, X; Liu, Y; Xu, Q; Wang, X; Saidahmatov, A; Li, C; Wang, J; Zhou, Y; Zhang, Y; Geng, M; Huang, M; Liu, H Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50582354 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50582354&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 141728823 476027359 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51444486 ONC(=O)c1ccc(CN(Cc2cccnc2)S(=O)(=O)c2cc(F)c(F)c(F)c2F)cc1 InChI=1S/C20H15F4N3O4S/c21-15-8-16(18(23)19(24)17(15)22)32(30,31)27(11-13-2-1-7-25-9-13)10-12-3-5-14(6-4-12)20(28)26-29/h1-9,29H,10-11H2,(H,26,28) HBOMISXRZUHCSH-UHFFFAOYSA-N 50583624 CHEMBL5075135 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.0c01922 10.7270/Q2NC6530 33576627 Olaoye, OO; Watson, PR; Nawar, N; Geletu, M; Sedighi, A; Bukhari, S; Raouf, YS; Manaswiyoungkul, P; Erdogan, F; Abdeldayem, A; Cabral, AD; Hassan, MM; Toutah, K; Shouksmith, AE; Gawel, JM; Israelian, J; Radu, TB; Kachhiyapatel, N; de Araujo, ED; Christianson, DW; Gunning, PT University of Toronto Mississauga http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50583624 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50583624&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TO3 7JOM 155144635 476028629 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1234615 CC1(C)N(Cc2c1cccc2C(=O)NO)c1cnc(cn1)C(F)(F)F InChI=1S/C16H15F3N4O2/c1-15(2)11-5-3-4-9(14(24)22-25)10(11)8-23(15)13-7-20-12(6-21-13)16(17,18)19/h3-7,25H,8H2,1-2H3,(H,22,24) XCLPBILTRRWOIL-UHFFFAOYSA-N 50273526 CHEMBL4126661::US11535607, Example 22-8 Histone deacetylase 4 Homo sapiens >1000 US Patent 10.7270/Q2M330NW US11535607 Zheng, X; Martin, MW; Ng, PY; Thomason, JR; Han, B; Rudnitskaya, A; Lancia, Jr., DR Valo Health, Inc. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50273526 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50273526&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 134492522 405256605 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1234626 COC(=O)c1cccc2c1CN(c1cnc(cn1)C(F)(F)F)C2(C)C InChI=1S/C17H16F3N3O2/c1-16(2)12-6-4-5-10(15(24)25-3)11(12)9-23(16)14-8-21-13(7-22-14)17(18,19)20/h4-8H,9H2,1-3H3 PWXDRQNYJNIDEQ-UHFFFAOYSA-N 587537 US11535607, Example 50-1 Histone deacetylase 4 Homo sapiens >1000 US Patent 10.7270/Q2M330NW US11535607 Zheng, X; Martin, MW; Ng, PY; Thomason, JR; Han, B; Rudnitskaya, A; Lancia, Jr., DR Valo Health, Inc. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=587537 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=587537&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51440008 COc1ccc2n(Cc3ccc(cc3)C(=O)NO)cc(CCNC(C)=O)c2c1 InChI=1S/C21H23N3O4/c1-14(25)22-10-9-17-13-24(20-8-7-18(28-2)11-19(17)20)12-15-3-5-16(6-4-15)21(26)23-27/h3-8,11,13,27H,9-10,12H2,1-2H3,(H,22,25)(H,23,26) BLSYXNAYVNGVFA-UHFFFAOYSA-N 50581675 CHEMBL5076794 Histone deacetylase 4 Homo sapiens 3431 ChEMBL 10.1021/acs.jmedchem.0c01940 10.7270/Q2WH2TVR 33769811 He, F; Chou, CJ; Scheiner, M; Poeta, E; Yuan Chen, N; Gunesch, S; Hoffmann, M; Sotriffer, C; Monti, B; Maurice, T; Decker, M Julius Maximilian University of W£rzburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50581675 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50581675&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166627027 476026680 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51440009 COc1ccc2n(Cc3ccc(cc3)C(=O)NO)cc(CCNC(C)=O)c2c1 InChI=1S/C21H23N3O4/c1-14(25)22-10-9-17-13-24(20-8-7-18(28-2)11-19(17)20)12-15-3-5-16(6-4-15)21(26)23-27/h3-8,11,13,27H,9-10,12H2,1-2H3,(H,22,25)(H,23,26) BLSYXNAYVNGVFA-UHFFFAOYSA-N 50581675 CHEMBL5076794 Histone deacetylase 4 Homo sapiens 3388 ChEMBL 10.1021/acs.jmedchem.0c01940 10.7270/Q2WH2TVR 33769811 He, F; Chou, CJ; Scheiner, M; Poeta, E; Yuan Chen, N; Gunesch, S; Hoffmann, M; Sotriffer, C; Monti, B; Maurice, T; Decker, M Julius Maximilian University of W£rzburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50581675 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50581675&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166627027 476026680 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51440010 COc1ccc2[nH]cc(CCN(Cc3ccc(cc3)C(=O)NO)C(=O)\C=C\c3ccc(O)c(OC)c3)c2c1 InChI=1S/C29H29N3O6/c1-37-23-9-10-25-24(16-23)22(17-30-25)13-14-32(18-20-3-7-21(8-4-20)29(35)31-36)28(34)12-6-19-5-11-26(33)27(15-19)38-2/h3-12,15-17,30,33,36H,13-14,18H2,1-2H3,(H,31,35)/b12-6+ BOSHROJUQKKPJB-WUXMJOGZSA-N 50581678 CHEMBL5072502 Histone deacetylase 4 Homo sapiens >10.0 ChEMBL 10.1021/acs.jmedchem.0c01940 10.7270/Q2WH2TVR 33769811 He, F; Chou, CJ; Scheiner, M; Poeta, E; Yuan Chen, N; Gunesch, S; Hoffmann, M; Sotriffer, C; Monti, B; Maurice, T; Decker, M Julius Maximilian University of W£rzburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50581678 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50581678&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166630821 476026683 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51467757 NC(=O)c1ccc(COc2ccc(cc2)-n2cc3cccc(C(N)=O)c3n2)cc1 InChI=1S/C22H18N4O3/c23-21(27)15-6-4-14(5-7-15)13-29-18-10-8-17(9-11-18)26-12-16-2-1-3-19(22(24)28)20(16)25-26/h1-12H,13H2,(H2,23,27)(H2,24,28) IQDRXCXNISQMPH-UHFFFAOYSA-N 50592258 CHEMBL5177616 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.7270/Q22F7SD8 35643262 Chi, Z; Bai, Y; Li, J; Wang, K; Xu, Y; Luan, Y Qingdao University Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50592258 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50592258&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168276619 482603110 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51467758 NC(=O)\C=C\c1ccc(COc2ccc(cc2)-n2cc3cccc(C(N)=O)c3n2)cc1 InChI=1S/C24H20N4O3/c25-22(29)13-8-16-4-6-17(7-5-16)15-31-20-11-9-19(10-12-20)28-14-18-2-1-3-21(24(26)30)23(18)27-28/h1-14H,15H2,(H2,25,29)(H2,26,30)/b13-8+ IPPGXRJXMXVNLN-MDWZMJQESA-N 50592259 CHEMBL5208297 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.7270/Q22F7SD8 35643262 Chi, Z; Bai, Y; Li, J; Wang, K; Xu, Y; Luan, Y Qingdao University Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50592259 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50592259&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168295232 482603111 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51467759 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 1140 ChEMBL 10.7270/Q22F7SD8 35643262 Chi, Z; Bai, Y; Li, J; Wang, K; Xu, Y; Luan, Y Qingdao University Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51467774 COc1ccc(cn1)-c1cc(OCCN(C)c2ncc(cn2)C(=O)NO)c2ncnc(C)c2c1 InChI=1S/C23H23N7O4/c1-14-18-8-16(15-4-5-20(33-3)24-10-15)9-19(21(18)28-13-27-14)34-7-6-30(2)23-25-11-17(12-26-23)22(31)29-32/h4-5,8-13,32H,6-7H2,1-3H3,(H,29,31) GVPYBTYCSMGVJF-UHFFFAOYSA-N 50503947 CHEMBL4462577 Histone deacetylase 4 Homo sapiens 972 ChEMBL 10.7270/Q2XP78WH 35644299 Zhang, K; Huang, L; Lai, F; Lin, S; Tian, H; Wu, D; Chen, X; Xu, H Chinese Academy of Medical Sciences & Peking Union Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503947 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503947&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155529247 440712532 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51467659 CCCNNC(=O)c1ccc(NC(=O)Cc2ccccc2)cc1 InChI=1S/C18H21N3O2/c1-2-12-19-21-18(23)15-8-10-16(11-9-15)20-17(22)13-14-6-4-3-5-7-14/h3-11,19H,2,12-13H2,1H3,(H,20,22)(H,21,23) NWOAWPYSTZJWRK-UHFFFAOYSA-N 50592233 CHEMBL5187930 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.7270/Q2FN1B6D 35635949 Pulya, S; Patel, T; Paul, M; Adhikari, N; Banerjee, S; Routholla, G; Biswas, S; Jha, T; Ghosh, B Birla Institute of Technology and Science-Pilani Hyderabad Campus http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50592233 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50592233&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168278676 482603085 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51467660 CCCNNC(=O)c1ccc(Nc2ccccc2)cc1 InChI=1S/C16H19N3O/c1-2-12-17-19-16(20)13-8-10-15(11-9-13)18-14-6-4-3-5-7-14/h3-11,17-18H,2,12H2,1H3,(H,19,20) PCVNESMTNLXHLQ-UHFFFAOYSA-N 50592234 CHEMBL5209383 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.7270/Q2FN1B6D 35635949 Pulya, S; Patel, T; Paul, M; Adhikari, N; Banerjee, S; Routholla, G; Biswas, S; Jha, T; Ghosh, B Birla Institute of Technology and Science-Pilani Hyderabad Campus http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50592234 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50592234&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168296893 482603086 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51467661 CCCCNNC(=O)c1ccc(Br)cc1 InChI=1S/C11H15BrN2O/c1-2-3-8-13-14-11(15)9-4-6-10(12)7-5-9/h4-7,13H,2-3,8H2,1H3,(H,14,15) BVQCFCYPFJOOAV-UHFFFAOYSA-N 163619 UF010::US10807944, Compound UF010 Histone deacetylase 4 Homo sapiens >50000 ChEMBL 10.7270/Q2FN1B6D 35635949 Pulya, S; Patel, T; Paul, M; Adhikari, N; Banerjee, S; Routholla, G; Biswas, S; Jha, T; Ghosh, B Birla Institute of Technology and Science-Pilani Hyderabad Campus http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=163619 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=163619&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4596836 310305336 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51466220 Cn1c(CCCC(O)=O)nc2cc(ccc12)N(CCCl)CCCl InChI=1S/C16H21Cl2N3O2/c1-20-14-6-5-12(21(9-7-17)10-8-18)11-13(14)19-15(20)3-2-4-16(22)23/h5-6,11H,2-4,7-10H2,1H3,(H,22,23) YTKUWDBFDASYHO-UHFFFAOYSA-N 173621 US9096627, CY190602 Histone deacetylase 4 Homo sapiens 10.0 ChEMBL 10.7270/Q2KK9GTQ 33143937 Vaidya, GN; Rana, P; Venkatesh, A; Chatterjee, DR; Contractor, D; Satpute, DP; Nagpure, M; Jain, A; Kumar, D National Institute of Pharmaceutical Education and Research (NIPER) - Ahmedabad http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=173621 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=173621&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 65628 312810091 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51464746 CC(C)n1ncc2c(cc(cc12)-c1ccc(nc1)N1CCN(CC1)c1ncc(cn1)C(=O)NO)C(=O)NCc1c(C)cc(C)[nH]c1=O InChI=1S/C33H36N10O4/c1-19(2)43-28-13-23(12-25(27(28)18-38-43)31(45)35-17-26-20(3)11-21(4)39-32(26)46)22-5-6-29(34-14-22)41-7-9-42(10-8-41)33-36-15-24(16-37-33)30(44)40-47/h5-6,11-16,18-19,47H,7-10,17H2,1-4H3,(H,35,45)(H,39,46)(H,40,44) DTYUAFQIQYXAKJ-UHFFFAOYSA-N 50591112 CHEMBL5189365 Histone deacetylase 4 Homo sapiens 5640 ChEMBL 10.7270/Q2000620 36153841 Lu, D; Wang, C; Qu, L; Yin, F; Li, S; Luo, H; Zhang, Y; Liu, X; Chen, X; Luo, Z; Cui, N; Kong, L; Wang, X China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50591112 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50591112&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168281629 482601964 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51469432 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 300 ChEMBL 10.7270/Q2ZC86W8 36053318 Jiang, XC; Tu, FH; Wei, LY; Wang, BZ; Yuan, H; Yuan, JM; Rao, Y; Huang, SL; Li, QJ; Ou, TM; Wang, HG; Tan, JH; Chen, SB; Huang, ZS Sun Yat-sen University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51469433 Cl.CN(C)CCCNC(=O)c1ccc(\C=C2/CCn3c2nc2cc(N4CCN(CCCCCCCC(=O)NO)CC4)c(F)cc2c3=O)cc1 InChI=1S/C36H48FN7O4.ClH/c1-41(2)16-8-15-38-35(46)27-12-10-26(11-13-27)23-28-14-18-44-34(28)39-31-25-32(30(37)24-29(31)36(44)47)43-21-19-42(20-22-43)17-7-5-3-4-6-9-33(45)40-48;/h10-13,23-25,48H,3-9,14-22H2,1-2H3,(H,38,46)(H,40,45);1H/b28-23+; LVHIQYGIJSRTAN-XVBNZNTOSA-N 50592935 CHEMBL5192285 Histone deacetylase 4 Homo sapiens 2640 ChEMBL 10.7270/Q2ZC86W8 36053318 Jiang, XC; Tu, FH; Wei, LY; Wang, BZ; Yuan, H; Yuan, JM; Rao, Y; Huang, SL; Li, QJ; Ou, TM; Wang, HG; Tan, JH; Chen, SB; Huang, ZS Sun Yat-sen University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50592935 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50592935&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 165412735 482603787 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51476259 Nc1ccccc1NC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C20H25N3O2/c21-17-12-8-9-13-18(17)23-20(25)15-7-2-1-6-14-19(24)22-16-10-4-3-5-11-16/h3-5,8-13H,1-2,6-7,14-15,21H2,(H,22,24)(H,23,25) RFLHBLWLFUFFDZ-UHFFFAOYSA-N 50222414 BML-210::CHEBI:61077::CHEMBL324053 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.7270/Q2280CN2 35580726 Yue, K; Qin, M; Huang, C; James Chou, C; Jiang, Y; Li, X Ocean University of China http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50222414 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50222414&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 9543540 377008245 CHEMBL324053 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51476260 CCCNNC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C17H27N3O2/c1-2-14-18-20-17(22)13-9-4-3-8-12-16(21)19-15-10-6-5-7-11-15/h5-7,10-11,18H,2-4,8-9,12-14H2,1H3,(H,19,21)(H,20,22) QDBUPYIRFBUJSV-UHFFFAOYSA-N 50595204 CHEMBL4451085 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.7270/Q2280CN2 35580726 Yue, K; Qin, M; Huang, C; James Chou, C; Jiang, Y; Li, X Ocean University of China http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50595204 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50595204&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155521561 482606056 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51476261 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 6860 ChEMBL 10.7270/Q2280CN2 35580726 Yue, K; Qin, M; Huang, C; James Chou, C; Jiang, Y; Li, X Ocean University of China http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51469934 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1 InChI=1S/C24H27N5O3/c30-22(28-32)15-9-1-2-10-16-25-23(31)19-17-26-24(27-18-19)29(20-11-5-3-6-12-20)21-13-7-4-8-14-21/h3-8,11-14,17-18,32H,1-2,9-10,15-16H2,(H,25,31)(H,28,30) QGZYDVAGYRLSKP-UHFFFAOYSA-N 50439674 RICOLINOSTAT::US10858323, Compound 2::US11207431, Example E::US8609678, 2-(diphenylamino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [26] Histone deacetylase 4 Homo sapiens >5000 ChEMBL 10.7270/Q2XD15N3 36073117 Yue, K; Sun, S; Jia, G; Qin, M; Hou, X; Chou, CJ; Huang, C; Li, X Ocean University of China http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50439674 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50439674&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search AH4 5WGL 53340666 175451991 ZINC89630354 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51469935 CN1CCc2c(C1)c1ccccc1n2Cc1ccc(cc1)C(=O)NO InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::Tubastatin A::US10227295, Compound Tubastatin A::US10456394, Tubastatin A::US11207431, Example D::US8748451, 6::US9249087, Tubacin::US9751832, Tubastatin A::US9956192, Compound Tubastatin-A Histone deacetylase 4 Homo sapiens >5000 ChEMBL 10.7270/Q2XD15N3 36073117 Yue, K; Sun, S; Jia, G; Qin, M; Hou, X; Chou, CJ; Huang, C; Li, X Ocean University of China http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 ZINC51951670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51469936 CCNNC(=O)c1ccc(CN2c3ccccc3C=Cc3ccncc23)cc1 InChI=1S/C23H22N4O/c1-2-25-26-23(28)20-9-7-17(8-10-20)16-27-21-6-4-3-5-18(21)11-12-19-13-14-24-15-22(19)27/h3-15,25H,2,16H2,1H3,(H,26,28) ZNRZSMMDQXGEGA-UHFFFAOYSA-N 50593116 CHEMBL5173493 Histone deacetylase 4 Homo sapiens >5000 ChEMBL 10.7270/Q2XD15N3 36073117 Yue, K; Sun, S; Jia, G; Qin, M; Hou, X; Chou, CJ; Huang, C; Li, X Ocean University of China http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593116 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593116&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 165368935 482603968 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51478625 ONC(=O)c1ccc(CN(C2CC2)S(=O)(=O)c2cc(F)c(F)c(F)c2F)cc1 InChI=1S/C17H14F4N2O4S/c18-12-7-13(15(20)16(21)14(12)19)28(26,27)23(11-5-6-11)8-9-1-3-10(4-2-9)17(24)22-25/h1-4,7,11,25H,5-6,8H2,(H,22,24) HYEWQOQZANKATO-UHFFFAOYSA-N 50595960 CHEMBL5192865 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.7270/Q2MP579X 34101461 Toutah, K; Nawar, N; Timonen, S; Sorger, H; Raouf, YS; Bukhari, S; von Jan, J; Ianevski, A; Gawel, JM; Olaoye, OO; Geletu, M; Abdeldayem, A; Israelian, J; Radu, TB; Sedighi, A; Bhatti, MN; Hassan, MM; Manaswiyoungkul, P; Shouksmith, AE; Neubauer, HA; de Araujo, ED; Aittokallio, T; Krämer, OH; Moriggl, R; Mustjoki, S; Herling, M; Gunning, PT University of Toronto Mississauga http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50595960 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50595960&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155155639 482606812 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51478626 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1Cl InChI=1S/C24H26ClN5O3/c25-20-12-7-8-13-21(20)30(19-10-4-3-5-11-19)24-27-16-18(17-28-24)23(32)26-15-9-2-1-6-14-22(31)29-33/h3-5,7-8,10-13,16-17,33H,1-2,6,9,14-15H2,(H,26,32)(H,29,31) VLIUIBXPEDFJRF-UHFFFAOYSA-N 110036 US8609678, 2-((2-chlorophenyl)(phenyl)amino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [89] Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.7270/Q2MP579X 34101461 Toutah, K; Nawar, N; Timonen, S; Sorger, H; Raouf, YS; Bukhari, S; von Jan, J; Ianevski, A; Gawel, JM; Olaoye, OO; Geletu, M; Abdeldayem, A; Israelian, J; Radu, TB; Sedighi, A; Bhatti, MN; Hassan, MM; Manaswiyoungkul, P; Shouksmith, AE; Neubauer, HA; de Araujo, ED; Aittokallio, T; Krämer, OH; Moriggl, R; Mustjoki, S; Herling, M; Gunning, PT University of Toronto Mississauga http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=110036 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=110036&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 53340426 186526906 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51468985 ONC(=O)\C=C\c1ccc(CNc2ccc3nc4CCCCCn4c(=O)c3c2)cc1 InChI=1S/C23H24N4O3/c28-22(26-30)12-9-16-5-7-17(8-6-16)15-24-18-10-11-20-19(14-18)23(29)27-13-3-1-2-4-21(27)25-20/h5-12,14,24,30H,1-4,13,15H2,(H,26,28)/b12-9+ PXSXCOJDFYVRBV-FMIVXFBMSA-N 50592855 CHEMBL5205415 Histone deacetylase 4 Homo sapiens 1630 ChEMBL 10.7270/Q2CJ8JF1 35858522 Sharma, R; Chatterjee, E; Mathew, J; Sharma, S; Rao, NV; Pan, CH; Lee, SB; Dhingra, A; Grewal, AS; Liou, JP; Guru, SK; Nepali, K Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50592855 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50592855&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168294525 482603707 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51468986 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 150 ChEMBL 10.7270/Q2CJ8JF1 35858522 Sharma, R; Chatterjee, E; Mathew, J; Sharma, S; Rao, NV; Pan, CH; Lee, SB; Dhingra, A; Grewal, AS; Liou, JP; Guru, SK; Nepali, K Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51477847 Cc1ncsc1-c1ccc(CNC(=O)[C@@H]2C[C@@H](O)CN2C(=O)[C@@H](NC(=O)COCCOCCOCC(F)(F)c2cnc(nc2)-c2ccc(cc2)C(C(=O)NO)c2ccccc2F)C(C)(C)C)cc1 InChI=1S/C48H54F3N7O9S/c1-29-41(68-28-55-29)32-11-9-30(10-12-32)22-54-44(61)38-21-35(59)25-58(38)46(63)42(47(2,3)4)56-39(60)26-66-19-17-65-18-20-67-27-48(50,51)34-23-52-43(53-24-34)33-15-13-31(14-16-33)40(45(62)57-64)36-7-5-6-8-37(36)49/h5-16,23-24,28,35,38,40,42,59,64H,17-22,25-27H2,1-4H3,(H,54,61)(H,56,60)(H,57,62)/t35-,38+,40?,42-/m1/s1 CUCLIKLMKDOFAE-PELIQRIMSA-N 50595707 CHEMBL5194487 Histone deacetylase 4 Homo sapiens 410 ChEMBL 10.7270/Q2CC14PT 36098485 Macabuag, N; Esmieu, W; Breccia, P; Jarvis, R; Blackaby, W; Lazari, O; Urbonas, L; Eznarriaga, M; Williams, R; Strijbosch, A; Van de Bospoort, R; Matthews, K; Clissold, C; Ladduwahetty, T; Vater, H; Heaphy, P; Stafford, DG; Wang, HJ; Mangette, JE; McAllister, G; Beaumont, V; Vogt, TF; Wilkinson, HA; Doherty, EM; Dominguez, C Charles River Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50595707 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50595707&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168289228 482606559 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51477848 Cc1ncsc1-c1ccc(CNC(=O)[C@@H]2C[C@@H](O)CN2C(=O)[C@@H](NC(=O)COCCOCCOCCOCC(F)(F)c2cnc(nc2)-c2ccc(cc2)C(C(=O)NO)c2ccccc2F)C(C)(C)C)cc1 InChI=1S/C50H58F3N7O10S/c1-31-43(71-30-57-31)34-11-9-32(10-12-34)24-56-46(63)40-23-37(61)27-60(40)48(65)44(49(2,3)4)58-41(62)28-69-21-19-67-17-18-68-20-22-70-29-50(52,53)36-25-54-45(55-26-36)35-15-13-33(14-16-35)42(47(64)59-66)38-7-5-6-8-39(38)51/h5-16,25-26,30,37,40,42,44,61,66H,17-24,27-29H2,1-4H3,(H,56,63)(H,58,62)(H,59,64)/t37-,40+,42?,44-/m1/s1 JCIGJBGCHCAMMB-DGTRGAFGSA-N 50595708 CHEMBL5202426 Histone deacetylase 4 Homo sapiens 560 ChEMBL 10.7270/Q2CC14PT 36098485 Macabuag, N; Esmieu, W; Breccia, P; Jarvis, R; Blackaby, W; Lazari, O; Urbonas, L; Eznarriaga, M; Williams, R; Strijbosch, A; Van de Bospoort, R; Matthews, K; Clissold, C; Ladduwahetty, T; Vater, H; Heaphy, P; Stafford, DG; Wang, HJ; Mangette, JE; McAllister, G; Beaumont, V; Vogt, TF; Wilkinson, HA; Doherty, EM; Dominguez, C Charles River Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50595708 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50595708&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168292645 482606560 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51477849 Cc1ncsc1-c1ccc(CNC(=O)[C@@H]2C[C@@H](O)CN2C(=O)[C@@H](NC(=O)COCCOCCOCCOCCOCC(F)(F)c2cnc(nc2)-c2ccc(cc2)C(C(=O)NO)c2ccccc2F)C(C)(C)C)cc1 InChI=1S/C52H62F3N7O11S/c1-33-45(74-32-59-33)36-11-9-34(10-12-36)26-58-48(65)42-25-39(63)29-62(42)50(67)46(51(2,3)4)60-43(64)30-72-23-21-70-19-17-69-18-20-71-22-24-73-31-52(54,55)38-27-56-47(57-28-38)37-15-13-35(14-16-37)44(49(66)61-68)40-7-5-6-8-41(40)53/h5-16,27-28,32,39,42,44,46,63,68H,17-26,29-31H2,1-4H3,(H,58,65)(H,60,64)(H,61,66)/t39-,42+,44?,46-/m1/s1 HCYVFIZSHJPMGM-BZWIJWRHSA-N 50595709 CHEMBL5181194 Histone deacetylase 4 Homo sapiens 1100 ChEMBL 10.7270/Q2CC14PT 36098485 Macabuag, N; Esmieu, W; Breccia, P; Jarvis, R; Blackaby, W; Lazari, O; Urbonas, L; Eznarriaga, M; Williams, R; Strijbosch, A; Van de Bospoort, R; Matthews, K; Clissold, C; Ladduwahetty, T; Vater, H; Heaphy, P; Stafford, DG; Wang, HJ; Mangette, JE; McAllister, G; Beaumont, V; Vogt, TF; Wilkinson, HA; Doherty, EM; Dominguez, C Charles River Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50595709 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50595709&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168276767 482606561 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51477850 Cc1ncsc1-c1ccc(CNC(=O)[C@@H]2C[C@H](O)CN2C(=O)[C@@H](NC(=O)COCCOCCOCCOCCOCC(F)(F)c2cnc(nc2)-c2ccc(cc2)C(C(=O)NO)c2ccccc2F)C(C)(C)C)cc1 InChI=1S/C52H62F3N7O11S/c1-33-45(74-32-59-33)36-11-9-34(10-12-36)26-58-48(65)42-25-39(63)29-62(42)50(67)46(51(2,3)4)60-43(64)30-72-23-21-70-19-17-69-18-20-71-22-24-73-31-52(54,55)38-27-56-47(57-28-38)37-15-13-35(14-16-37)44(49(66)61-68)40-7-5-6-8-41(40)53/h5-16,27-28,32,39,42,44,46,63,68H,17-26,29-31H2,1-4H3,(H,58,65)(H,60,64)(H,61,66)/t39-,42-,44?,46+/m0/s1 HCYVFIZSHJPMGM-CFCRNHAGSA-N 50595710 CHEMBL5191938 Histone deacetylase 4 Homo sapiens 230 ChEMBL 10.7270/Q2CC14PT 36098485 Macabuag, N; Esmieu, W; Breccia, P; Jarvis, R; Blackaby, W; Lazari, O; Urbonas, L; Eznarriaga, M; Williams, R; Strijbosch, A; Van de Bospoort, R; Matthews, K; Clissold, C; Ladduwahetty, T; Vater, H; Heaphy, P; Stafford, DG; Wang, HJ; Mangette, JE; McAllister, G; Beaumont, V; Vogt, TF; Wilkinson, HA; Doherty, EM; Dominguez, C Charles River Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50595710 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50595710&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168285308 482606562 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51477851 CCCN(CCCCOCCOCCOCC(=O)N[C@H](C(=O)N1C[C@H](O)C[C@H]1C(=O)NCc1ccc(cc1)-c1scnc1C)C(C)(C)C)C[C@@H](C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C48H65F3N8O9S/c1-7-18-58(27-31(2)54-43(62)36-16-14-35(15-17-36)42-56-46(68-57-42)48(49,50)51)19-8-9-20-65-21-22-66-23-24-67-29-39(61)55-41(47(4,5)6)45(64)59-28-37(60)25-38(59)44(63)52-26-33-10-12-34(13-11-33)40-32(3)53-30-69-40/h10-17,30-31,37-38,41,60H,7-9,18-29H2,1-6H3,(H,52,63)(H,54,62)(H,55,61)/t31-,37-,38+,41-/m1/s1 LNVXIMZTYRLPDR-UYNIEJFQSA-N 50595711 CHEMBL5172806 Histone deacetylase 4 Homo sapiens 90 ChEMBL 10.7270/Q2CC14PT 36098485 Macabuag, N; Esmieu, W; Breccia, P; Jarvis, R; Blackaby, W; Lazari, O; Urbonas, L; Eznarriaga, M; Williams, R; Strijbosch, A; Van de Bospoort, R; Matthews, K; Clissold, C; Ladduwahetty, T; Vater, H; Heaphy, P; Stafford, DG; Wang, HJ; Mangette, JE; McAllister, G; Beaumont, V; Vogt, TF; Wilkinson, HA; Doherty, EM; Dominguez, C Charles River Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50595711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50595711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168274795 482606563 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51477852 CCCN(CCCCOCCOCCOCCOCC(=O)N[C@H](C(=O)N1C[C@H](O)C[C@H]1C(=O)NCc1ccc(cc1)-c1scnc1C)C(C)(C)C)C[C@@H](C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C50H69F3N8O10S/c1-7-18-60(29-33(2)56-45(64)38-16-14-37(15-17-38)44-58-48(71-59-44)50(51,52)53)19-8-9-20-67-21-22-68-23-24-69-25-26-70-31-41(63)57-43(49(4,5)6)47(66)61-30-39(62)27-40(61)46(65)54-28-35-10-12-36(13-11-35)42-34(3)55-32-72-42/h10-17,32-33,39-40,43,62H,7-9,18-31H2,1-6H3,(H,54,65)(H,56,64)(H,57,63)/t33-,39-,40+,43-/m1/s1 QONCFSQPRCINOK-WIIHZIRBSA-N 50595712 CHEMBL5199458 Histone deacetylase 4 Homo sapiens 100 ChEMBL 10.7270/Q2CC14PT 36098485 Macabuag, N; Esmieu, W; Breccia, P; Jarvis, R; Blackaby, W; Lazari, O; Urbonas, L; Eznarriaga, M; Williams, R; Strijbosch, A; Van de Bospoort, R; Matthews, K; Clissold, C; Ladduwahetty, T; Vater, H; Heaphy, P; Stafford, DG; Wang, HJ; Mangette, JE; McAllister, G; Beaumont, V; Vogt, TF; Wilkinson, HA; Doherty, EM; Dominguez, C Charles River Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50595712 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50595712&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168292252 482606564 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51477853 CCCN(CCCCOCCOCCOCCOCCOCC(=O)N[C@H](C(=O)N1C[C@H](O)C[C@H]1C(=O)NCc1ccc(cc1)-c1scnc1C)C(C)(C)C)C[C@@H](C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C52H73F3N8O11S/c1-7-18-62(31-35(2)58-47(66)40-16-14-39(15-17-40)46-60-50(74-61-46)52(53,54)55)19-8-9-20-69-21-22-70-23-24-71-25-26-72-27-28-73-33-43(65)59-45(51(4,5)6)49(68)63-32-41(64)29-42(63)48(67)56-30-37-10-12-38(13-11-37)44-36(3)57-34-75-44/h10-17,34-35,41-42,45,64H,7-9,18-33H2,1-6H3,(H,56,67)(H,58,66)(H,59,65)/t35-,41-,42+,45-/m1/s1 KBDZFZJFGKYVBZ-KLSSUPLUSA-N 50595713 CHEMBL5208515 Histone deacetylase 4 Homo sapiens 92 ChEMBL 10.7270/Q2CC14PT 36098485 Macabuag, N; Esmieu, W; Breccia, P; Jarvis, R; Blackaby, W; Lazari, O; Urbonas, L; Eznarriaga, M; Williams, R; Strijbosch, A; Van de Bospoort, R; Matthews, K; Clissold, C; Ladduwahetty, T; Vater, H; Heaphy, P; Stafford, DG; Wang, HJ; Mangette, JE; McAllister, G; Beaumont, V; Vogt, TF; Wilkinson, HA; Doherty, EM; Dominguez, C Charles River Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50595713 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50595713&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168297912 482606565 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51477854 CCCN(CCCCOCCOCCOCCOCCOCC(=O)N[C@@H](C(=O)N1C[C@@H](O)C[C@@H]1C(=O)NCc1ccc(cc1)-c1scnc1C)C(C)(C)C)C[C@@H](C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C52H73F3N8O11S/c1-7-18-62(31-35(2)58-47(66)40-16-14-39(15-17-40)46-60-50(74-61-46)52(53,54)55)19-8-9-20-69-21-22-70-23-24-71-25-26-72-27-28-73-33-43(65)59-45(51(4,5)6)49(68)63-32-41(64)29-42(63)48(67)56-30-37-10-12-38(13-11-37)44-36(3)57-34-75-44/h10-17,34-35,41-42,45,64H,7-9,18-33H2,1-6H3,(H,56,67)(H,58,66)(H,59,65)/t35-,41+,42-,45+/m1/s1 KBDZFZJFGKYVBZ-RBILXPFJSA-N 50595714 CHEMBL5206361 Histone deacetylase 4 Homo sapiens 150 ChEMBL 10.7270/Q2CC14PT 36098485 Macabuag, N; Esmieu, W; Breccia, P; Jarvis, R; Blackaby, W; Lazari, O; Urbonas, L; Eznarriaga, M; Williams, R; Strijbosch, A; Van de Bospoort, R; Matthews, K; Clissold, C; Ladduwahetty, T; Vater, H; Heaphy, P; Stafford, DG; Wang, HJ; Mangette, JE; McAllister, G; Beaumont, V; Vogt, TF; Wilkinson, HA; Doherty, EM; Dominguez, C Charles River Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50595714 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50595714&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168296246 482606566 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51477855 ONC(=O)C(c1ccc(cc1)-c1ncc(cn1)C(F)(F)F)c1ccccc1F InChI=1S/C19H13F4N3O2/c20-15-4-2-1-3-14(15)16(18(27)26-28)11-5-7-12(8-6-11)17-24-9-13(10-25-17)19(21,22)23/h1-10,16,28H,(H,26,27) LMGDHGQJJLEAPQ-UHFFFAOYSA-N 50503690 CHEMBL4456445 Histone deacetylase 4 Homo sapiens 54 ChEMBL 10.7270/Q2CC14PT 36098485 Macabuag, N; Esmieu, W; Breccia, P; Jarvis, R; Blackaby, W; Lazari, O; Urbonas, L; Eznarriaga, M; Williams, R; Strijbosch, A; Van de Bospoort, R; Matthews, K; Clissold, C; Ladduwahetty, T; Vater, H; Heaphy, P; Stafford, DG; Wang, HJ; Mangette, JE; McAllister, G; Beaumont, V; Vogt, TF; Wilkinson, HA; Doherty, EM; Dominguez, C Charles River Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50503690 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50503690&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 81689842 440712275 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51477856 CCCN(CCC)C[C@@H](C)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C19H25F3N4O2/c1-4-10-26(11-5-2)12-13(3)23-17(27)15-8-6-14(7-9-15)16-24-18(28-25-16)19(20,21)22/h6-9,13H,4-5,10-12H2,1-3H3,(H,23,27)/t13-/m1/s1 HMXFCVJIASWKMB-CYBMUJFWSA-N 162846 US9056843, 137 Histone deacetylase 4 Homo sapiens 3.0 ChEMBL 10.7270/Q2CC14PT 36098485 Macabuag, N; Esmieu, W; Breccia, P; Jarvis, R; Blackaby, W; Lazari, O; Urbonas, L; Eznarriaga, M; Williams, R; Strijbosch, A; Van de Bospoort, R; Matthews, K; Clissold, C; Ladduwahetty, T; Vater, H; Heaphy, P; Stafford, DG; Wang, HJ; Mangette, JE; McAllister, G; Beaumont, V; Vogt, TF; Wilkinson, HA; Doherty, EM; Dominguez, C Charles River Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162846 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162846&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230790 310304783 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51455878 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1 InChI=1S/C24H27N5O3/c30-22(28-32)15-9-1-2-10-16-25-23(31)19-17-26-24(27-18-19)29(20-11-5-3-6-12-20)21-13-7-4-8-14-21/h3-8,11-14,17-18,32H,1-2,9-10,15-16H2,(H,25,31)(H,28,30) QGZYDVAGYRLSKP-UHFFFAOYSA-N 50439674 RICOLINOSTAT::US10858323, Compound 2::US11207431, Example E::US8609678, 2-(diphenylamino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [26] Histone deacetylase 4 Homo sapiens 7000 ChEMBL 10.7270/Q2G73JP3 33523672 Zhang, XH; Qin-Ma, na; Wu, HP; Khamis, MY; Li, YH; Ma, LY; Liu, HM Zhengzhou University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50439674 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50439674&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search AH4 5WGL 53340666 175451991 ZINC89630354 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51455879 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1Cl InChI=1S/C24H26ClN5O3/c25-20-12-7-8-13-21(20)30(19-10-4-3-5-11-19)24-27-16-18(17-28-24)23(32)26-15-9-2-1-6-14-22(31)29-33/h3-5,7-8,10-13,16-17,33H,1-2,6,9,14-15H2,(H,26,32)(H,29,31) VLIUIBXPEDFJRF-UHFFFAOYSA-N 110036 US8609678, 2-((2-chlorophenyl)(phenyl)amino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [89] Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.7270/Q2G73JP3 33523672 Zhang, XH; Qin-Ma, na; Wu, HP; Khamis, MY; Li, YH; Ma, LY; Liu, HM Zhengzhou University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=110036 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=110036&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 53340426 186526906 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51455894 ONC(=O)CCCCCCC(=O)N\N=C\c1cnc(nc1)N(c1ccccc1)c1ccccc1 InChI=1S/C25H28N6O3/c32-23(15-9-1-2-10-16-24(33)30-34)29-28-19-20-17-26-25(27-18-20)31(21-11-5-3-6-12-21)22-13-7-4-8-14-22/h3-8,11-14,17-19,34H,1-2,9-10,15-16H2,(H,29,32)(H,30,33)/b28-19+ BBSLRRWTGBLAON-TURZUDJPSA-N 50587716 CHEMBL5188297 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.7270/Q2G73JP3 33523672 Zhang, XH; Qin-Ma, na; Wu, HP; Khamis, MY; Li, YH; Ma, LY; Liu, HM Zhengzhou University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50587716 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50587716&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168278328 482598568 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51455906 OCCN(C(=O)Cc1ccc(cc1)C(=O)NO)c1ccccc1 InChI=1S/C17H18N2O4/c20-11-10-19(15-4-2-1-3-5-15)16(21)12-13-6-8-14(9-7-13)17(22)18-23/h1-9,20,23H,10-12H2,(H,18,22) RFAZNTABYJYOAR-UHFFFAOYSA-N 198121 HPOB Histone deacetylase 4 Homo sapiens 1700 ChEMBL 10.7270/Q2G73JP3 33523672 Zhang, XH; Qin-Ma, na; Wu, HP; Khamis, MY; Li, YH; Ma, LY; Liu, HM Zhengzhou University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=198121 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=198121&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5OJ 5EF7 71532921 318489194 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51455907 OCCN(C(=O)Cc1ccccc1)C(=O)Cc1ccc(cc1)C(=O)NO InChI=1S/C19H20N2O5/c22-11-10-21(17(23)12-14-4-2-1-3-5-14)18(24)13-15-6-8-16(9-7-15)19(25)20-26/h1-9,22,26H,10-13H2,(H,20,25) YKTXZBJZADGNSE-UHFFFAOYSA-N 50587717 CHEMBL5194437 Histone deacetylase 4 Homo sapiens 2199 ChEMBL 10.7270/Q2G73JP3 33523672 Zhang, XH; Qin-Ma, na; Wu, HP; Khamis, MY; Li, YH; Ma, LY; Liu, HM Zhengzhou University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50587717 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50587717&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168287973 482598569 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51455925 CN1CCc2c(C1)c1ccccc1n2Cc1ccc(cc1)C(=O)NO InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::Tubastatin A::US10227295, Compound Tubastatin A::US10456394, Tubastatin A::US11207431, Example D::US8748451, 6::US9249087, Tubacin::US9751832, Tubastatin A::US9956192, Compound Tubastatin-A Histone deacetylase 4 Homo sapiens >30000 ChEMBL 10.7270/Q2G73JP3 33523672 Zhang, XH; Qin-Ma, na; Wu, HP; Khamis, MY; Li, YH; Ma, LY; Liu, HM Zhengzhou University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 ZINC51951670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51455939 ONC(=O)c1ccc(Cn2sc3ccccc3c2=O)cc1 InChI=1S/C15H12N2O3S/c18-14(16-20)11-7-5-10(6-8-11)9-17-15(19)12-3-1-2-4-13(12)21-17/h1-8,20H,9H2,(H,16,18) ZBKIYZUDBOQUME-UHFFFAOYSA-N 50587718 CHEMBL5185889 Histone deacetylase 4 Homo sapiens 5400 ChEMBL 10.7270/Q2G73JP3 33523672 Zhang, XH; Qin-Ma, na; Wu, HP; Khamis, MY; Li, YH; Ma, LY; Liu, HM Zhengzhou University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50587718 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50587718&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 58011595 482598570 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51455963 ONC(=O)c1ccc(CN2CCCc3cc(Cl)ccc23)cc1 InChI=1S/C17H17ClN2O2/c18-15-7-8-16-14(10-15)2-1-9-20(16)11-12-3-5-13(6-4-12)17(21)19-22/h3-8,10,22H,1-2,9,11H2,(H,19,21) MNAYBFFSFQRSIT-UHFFFAOYSA-N 417049 4-((6-chloro-3,4-dihydroquinolin-1(2H)-yl)methyl)-N-hydroxybenzamide::US10456394, Example 2 Histone deacetylase 4 Homo sapiens 10900 ChEMBL 10.7270/Q2G73JP3 33523672 Zhang, XH; Qin-Ma, na; Wu, HP; Khamis, MY; Li, YH; Ma, LY; Liu, HM Zhengzhou University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=417049 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=417049&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 130345472 433916959 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51455986 ONC(=O)\C=C\c1cccc(c1)S(=O)(=O)Nc1ccccc1 InChI=1S/C15H14N2O4S/c18-15(16-19)10-9-12-5-4-8-14(11-12)22(20,21)17-13-6-2-1-3-7-13/h1-11,17,19H,(H,16,18)/b10-9+ NCNRHFGMJRPRSK-MDZDMXLPSA-N 25150 (2E)-N-hydroxy-3-[3-(phenylsulfamoyl)phenyl]prop-2-enamide::Belinosta::Belinostat::PXD-101::PXD101 Histone deacetylase 4 Homo sapiens 115 ChEMBL 10.7270/Q26Q2260 33540228 Lopes, JR; Chiba, DE; Dos Santos, JL S£o Paulo State University (UNESP) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25150 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25150&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5OG 5EEN 6918638 56374291 61076 ZINC03818726 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51458202 ONC(=O)CCCCC\C=C\c1csc(n1)C#C InChI=1S/C13H16N2O2S/c1-2-13-14-11(10-18-13)8-6-4-3-5-7-9-12(16)15-17/h1,6,8,10,17H,3-5,7,9H2,(H,15,16)/b8-6+ KAKCYHAHFMDCRW-SOFGYWHQSA-N 50588568 CHEMBL5186798 Histone deacetylase 4 Homo sapiens 8600 ChEMBL 10.7270/Q2C53QTB 36306372 Karaj, E; Sindi, SH; Kuganesan, N; Koranne, RA; Knoff, JR; James, AW; Fu, Y; Kotsull, LN; Pflum, MK; Shah, Z; Taylor, WR; Tillekeratne, LMV University of Toledo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50588568 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50588568&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168278204 482599420 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51458203 ONC(=O)\C=C\C=C\c1csc(n1)C#C InChI=1S/C10H8N2O2S/c1-2-10-11-8(7-15-10)5-3-4-6-9(13)12-14/h1,3-7,14H,(H,12,13)/b5-3+,6-4+ NHXGMOTURBJIGL-GGWOSOGESA-N 50588569 CHEMBL5170140 Histone deacetylase 4 Homo sapiens 2100 ChEMBL 10.7270/Q2C53QTB 36306372 Karaj, E; Sindi, SH; Kuganesan, N; Koranne, RA; Knoff, JR; James, AW; Fu, Y; Kotsull, LN; Pflum, MK; Shah, Z; Taylor, WR; Tillekeratne, LMV University of Toledo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50588569 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50588569&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168269974 482599421 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51458204 ONC(=O)CCCCC\C=C/c1csc(Br)n1 InChI=1S/C11H15BrN2O2S/c12-11-13-9(8-17-11)6-4-2-1-3-5-7-10(15)14-16/h4,6,8,16H,1-3,5,7H2,(H,14,15)/b6-4- WLRUIAIHXAKVSH-XQRVVYSFSA-N 50588561 CHEMBL5193020 Histone deacetylase 4 Homo sapiens 7200 ChEMBL 10.7270/Q2C53QTB 36306372 Karaj, E; Sindi, SH; Kuganesan, N; Koranne, RA; Knoff, JR; James, AW; Fu, Y; Kotsull, LN; Pflum, MK; Shah, Z; Taylor, WR; Tillekeratne, LMV University of Toledo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50588561 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50588561&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168286586 482599413 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51458205 ONC(=O)\C=C\C=C\c1csc(Br)n1 InChI=1S/C8H7BrN2O2S/c9-8-10-6(5-14-8)3-1-2-4-7(12)11-13/h1-5,13H,(H,11,12)/b3-1+,4-2+ IYHAVTYWOVUBNO-ZPUQHVIOSA-N 50588564 CHEMBL5206154 Histone deacetylase 4 Homo sapiens 34000 ChEMBL 10.7270/Q2C53QTB 36306372 Karaj, E; Sindi, SH; Kuganesan, N; Koranne, RA; Knoff, JR; James, AW; Fu, Y; Kotsull, LN; Pflum, MK; Shah, Z; Taylor, WR; Tillekeratne, LMV University of Toledo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50588564 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50588564&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168295622 482599416 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51458206 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 12000 ChEMBL 10.7270/Q2C53QTB 36306372 Karaj, E; Sindi, SH; Kuganesan, N; Koranne, RA; Knoff, JR; James, AW; Fu, Y; Kotsull, LN; Pflum, MK; Shah, Z; Taylor, WR; Tillekeratne, LMV University of Toledo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51456130 Cn1cc(CNCC2CCN(CC2)c2ncc(cn2)C(=O)NO)c2ccccc12 InChI=1S/C21H26N6O2/c1-26-14-17(18-4-2-3-5-19(18)26)11-22-10-15-6-8-27(9-7-15)21-23-12-16(13-24-21)20(28)25-29/h2-5,12-15,22,29H,6-11H2,1H3,(H,25,28) PAWIYAYFNXQGAP-UHFFFAOYSA-N 50105327 JNJ-26481585::Quisinostat Histone deacetylase 4 Homo sapiens 0.640000 ChEMBL 10.7270/Q2F76HH8 33714914 Gediya, P; Parikh, PK; Vyas, VK; Ghate, MD Nirma University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50105327 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50105327&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search GOK 7Q1B,6HSK,6HSH 11538455 318590494 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51484569 COc1ccccc1CN1C2=NCCN2C2=C(CN(Cc3ccc(cc3)C(=O)Nc3ccccc3N)CC2)C1=O InChI=1S/C31H32N6O3/c1-40-28-9-5-2-6-23(28)19-37-30(39)24-20-35(16-14-27(24)36-17-15-33-31(36)37)18-21-10-12-22(13-11-21)29(38)34-26-8-4-3-7-25(26)32/h2-13H,14-20,32H2,1H3,(H,34,38) JRYSTMMUZUGAAW-UHFFFAOYSA-N 50598259 CHEMBL5194529 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.7270/Q2QR525P 35649291 Cui, H; Hu, Z; Yang, K; Huang, J; Wu, Y; Chen, Q; Wei, R; Wang, P; Wang, H; Li, H; Chen, Y; Lu, T; Yao, Y; Zhu, Y China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50598259 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50598259&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168285020 482609111 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51457507 CCCC(CCC)C(O)=O InChI=1S/C8H16O2/c1-3-5-7(6-4-2)8(9)10/h7H,3-6H2,1-2H3,(H,9,10) NIJJYAXOARWZEE-UHFFFAOYSA-N 50003616 2-n-propyl-n-valeric acid::CHEMBL109::DPA::Di-n-propylessigsaeure::VALPROIC ACID::Valproinsaeure::dipropylacetic acid::n-DPA Histone deacetylase 4 Homo sapiens 1000000 ChEMBL 10.7270/Q25M69NW 34826681 Qiu, X; Zhu, L; Wang, H; Tan, Y; Yang, Z; Yang, L; Wan, L Chengdu University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50003616 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50003616&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 2PP 1DIT 3121 103917584 39867 CHEMBL109 DB00313 7009 C07185 ZINC03008621 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51457508 CCCCCCCC(=O)SCC\C=C\[C@@H]1CC(=O)NCc2nc(cs2)C2=N[C@@](C)(CS2)C(=O)N[C@@H](C(C)C)C(=O)O1 InChI=1S/C29H42N4O5S3/c1-5-6-7-8-9-13-24(35)39-14-11-10-12-20-15-22(34)30-16-23-31-21(17-40-23)26-33-29(4,18-41-26)28(37)32-25(19(2)3)27(36)38-20/h10,12,17,19-20,25H,5-9,11,13-16,18H2,1-4H3,(H,30,34)(H,32,37)/b12-10+/t20-,25+,29+/m1/s1 AXESYCSCGBQJBL-SZPBEECKSA-N 50322422 CHEMBL1173445::Largazole Histone deacetylase 4 Homo sapiens 3000 ChEMBL 10.7270/Q25M69NW 34826681 Qiu, X; Zhu, L; Wang, H; Tan, Y; Yang, Z; Yang, L; Wan, L Chengdu University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50322422 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50322422&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 24757913 104143951 CHEMBL1173445 C05752 ZINC56861395 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51457513 C\C=C1/NC(=O)[C@H]2CSSCC\C=C\[C@@H](CC(=O)N[C@H](C(C)C)C(=O)N2)OC(=O)[C@@H](NC1=O)C(C)C InChI=1S/C24H36N4O6S2/c1-6-16-21(30)28-20(14(4)5)24(33)34-15-9-7-8-10-35-36-12-17(22(31)25-16)26-23(32)19(13(2)3)27-18(29)11-15/h6-7,9,13-15,17,19-20H,8,10-12H2,1-5H3,(H,25,31)(H,26,32)(H,27,29)(H,28,30)/b9-7+,16-6-/t15-,17+,19+,20-/m0/s1 OHRURASPPZQGQM-QSVHVVLASA-N 50048864 CHEMBL3310505 Histone deacetylase 4 Homo sapiens 510 ChEMBL 10.7270/Q25M69NW 34826681 Qiu, X; Zhu, L; Wang, H; Tan, Y; Yang, Z; Yang, L; Wan, L Chengdu University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50048864 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50048864&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11947684 103979245 CHEMBL3310505 ZINC13745305 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51457518 CC[C@]1(C)NC(=O)[C@H](CCCCCC(=O)[C@@H](C)O)NC(=O)[C@H]2CC(C)CN2C(=O)[C@H](Cc2ccccc2)NC1=O InChI=1S/C30H44N4O6/c1-5-30(4)29(40)32-23(17-21-12-8-6-9-13-21)28(39)34-18-19(2)16-24(34)27(38)31-22(26(37)33-30)14-10-7-11-15-25(36)20(3)35/h6,8-9,12-13,19-20,22-24,35H,5,7,10-11,14-18H2,1-4H3,(H,31,38)(H,32,40)(H,33,37)/t19?,20-,22+,23+,24-,30+/m1/s1 NJEYLEUCEPGDMG-ORSGUKHISA-N 50588305 CHEMBL5209235 Histone deacetylase 4 Homo sapiens 60 ChEMBL 10.7270/Q25M69NW 34826681 Qiu, X; Zhu, L; Wang, H; Tan, Y; Yang, Z; Yang, L; Wan, L Chengdu University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50588305 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50588305&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168294741 482599157 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51457519 C[C@@H](O)C(=O)CCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC(=O)C(C)(C)NC1=O InChI=1S/C28H40N4O6/c1-18(33)23(34)15-9-5-8-13-20-24(35)31-28(2,3)27(38)30-21(17-19-11-6-4-7-12-19)26(37)32-16-10-14-22(32)25(36)29-20/h4,6-7,11-12,18,20-22,33H,5,8-10,13-17H2,1-3H3,(H,29,36)(H,30,38)(H,31,35)/t18-,20+,21+,22-/m1/s1 UXOLDMJAFJDQSE-RYFAJOAYSA-N 50588306 CHEMBL474318 Histone deacetylase 4 Homo sapiens 30 ChEMBL 10.7270/Q25M69NW 34826681 Qiu, X; Zhu, L; Wang, H; Tan, Y; Yang, Z; Yang, L; Wan, L Chengdu University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50588306 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50588306&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 10392191 482599158 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51457520 CC[C@]1(C)NC(=O)[C@H](CCCCCC(=O)[C@@H](C)O)NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC1=O InChI=1S/C29H42N4O6/c1-4-29(3)28(39)31-22(18-20-12-7-5-8-13-20)27(38)33-17-11-15-23(33)26(37)30-21(25(36)32-29)14-9-6-10-16-24(35)19(2)34/h5,7-8,12-13,19,21-23,34H,4,6,9-11,14-18H2,1-3H3,(H,30,37)(H,31,39)(H,32,36)/t19-,21+,22+,23-,29+/m1/s1 XQURZRWZWZDDKH-XLSSLVJHSA-N 50531334 CHEMBL472574 Histone deacetylase 4 Homo sapiens 50 ChEMBL 10.7270/Q25M69NW 34826681 Qiu, X; Zhu, L; Wang, H; Tan, Y; Yang, Z; Yang, L; Wan, L Chengdu University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50531334 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50531334&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44563351 440739916 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51457521 C[C@@H](O)C(=O)CCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC(=O)[C@H](Cc2ccccc2)NC1=O InChI=1S/C33H42N4O6/c1-22(38)29(39)18-10-4-9-16-25-30(40)35-26(20-23-12-5-2-6-13-23)31(41)36-27(21-24-14-7-3-8-15-24)33(43)37-19-11-17-28(37)32(42)34-25/h2-3,5-8,12-15,22,25-28,38H,4,9-11,16-21H2,1H3,(H,34,42)(H,35,40)(H,36,41)/t22-,25+,26+,27+,28-/m1/s1 GDHPWFSAGIUMHT-HMZHQOCUSA-N 50588307 CHEMBL451873 Histone deacetylase 4 Homo sapiens 280 ChEMBL 10.7270/Q25M69NW 34826681 Qiu, X; Zhu, L; Wang, H; Tan, Y; Yang, Z; Yang, L; Wan, L Chengdu University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50588307 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50588307&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44563392 482599159 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51457522 C[C@@H](O)C(=O)CCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC(=O)[C@@H](NC1=O)n1ccc2ccccc12 InChI=1S/C34H41N5O6/c1-22(40)29(41)17-7-3-6-14-25-31(42)37-30(38-20-18-24-13-8-9-15-27(24)38)33(44)36-26(21-23-11-4-2-5-12-23)34(45)39-19-10-16-28(39)32(43)35-25/h2,4-5,8-9,11-13,15,18,20,22,25-26,28,30,40H,3,6-7,10,14,16-17,19,21H2,1H3,(H,35,43)(H,36,44)(H,37,42)/t22-,25+,26+,28-,30+/m1/s1 ZTOPZCOUZQXWSK-RLQIRPRCSA-N 50588308 CHEMBL5204304 Histone deacetylase 4 Homo sapiens 20 ChEMBL 10.7270/Q25M69NW 34826681 Qiu, X; Zhu, L; Wang, H; Tan, Y; Yang, Z; Yang, L; Wan, L Chengdu University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50588308 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50588308&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168293660 482599160 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51457523 CC[C@]1(C)NC(=O)[C@H](CCCCCC(=O)[C@@H](C)O)NC(=O)[C@H]2CC(C)(C)CN2C(=O)[C@H](Cc2ccccc2)NC1=O InChI=1S/C31H46N4O6/c1-6-31(5)29(41)33-23(17-21-13-9-7-10-14-21)28(40)35-19-30(3,4)18-24(35)27(39)32-22(26(38)34-31)15-11-8-12-16-25(37)20(2)36/h7,9-10,13-14,20,22-24,36H,6,8,11-12,15-19H2,1-5H3,(H,32,39)(H,33,41)(H,34,38)/t20-,22+,23+,24-,31+/m1/s1 CKZGFFROESMZMH-OHKQVTTLSA-N 50588309 CHEMBL470325 Histone deacetylase 4 Homo sapiens 90 ChEMBL 10.7270/Q25M69NW 34826681 Qiu, X; Zhu, L; Wang, H; Tan, Y; Yang, Z; Yang, L; Wan, L Chengdu University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50588309 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50588309&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44563391 482599161 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51457524 C[C@H](O)C(=O)CCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC(=O)C(C)(C)NC1=O InChI=1S/C28H40N4O6/c1-18(33)23(34)15-9-5-8-13-20-24(35)31-28(2,3)27(38)30-21(17-19-11-6-4-7-12-19)26(37)32-16-10-14-22(32)25(36)29-20/h4,6-7,11-12,18,20-22,33H,5,8-10,13-17H2,1-3H3,(H,29,36)(H,30,38)(H,31,35)/t18-,20-,21-,22+/m0/s1 UXOLDMJAFJDQSE-JKLQHZFJSA-N 50588310 CHEMBL473512 Histone deacetylase 4 Homo sapiens 330 ChEMBL 10.7270/Q25M69NW 34826681 Qiu, X; Zhu, L; Wang, H; Tan, Y; Yang, Z; Yang, L; Wan, L Chengdu University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50588310 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50588310&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44563393 482599162 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51457525 CC[C@@H]1NC(=O)[C@H](CCCCCC(=O)[C@H](C)O)NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC1=O InChI=1S/C28H40N4O6/c1-3-20-25(35)31-22(17-19-11-6-4-7-12-19)28(38)32-16-10-14-23(32)27(37)30-21(26(36)29-20)13-8-5-9-15-24(34)18(2)33/h4,6-7,11-12,18,20-23,33H,3,5,8-10,13-17H2,1-2H3,(H,29,36)(H,30,37)(H,31,35)/t18-,20-,21-,22-,23+/m0/s1 ZQRGLKUISWQUNH-VPSDZCSPSA-N 50588311 CHEMBL489280 Histone deacetylase 4 Homo sapiens 1000 ChEMBL 10.7270/Q25M69NW 34826681 Qiu, X; Zhu, L; Wang, H; Tan, Y; Yang, Z; Yang, L; Wan, L Chengdu University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50588311 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50588311&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44563451 482599163 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51457526 C[C@H](O)C(=O)CCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC(=O)C(NC1=O)(C1CCCCC1)C1CCCCC1 InChI=1S/C38H56N4O6/c1-26(43)33(44)23-13-5-12-21-30-34(45)41-38(28-17-8-3-9-18-28,29-19-10-4-11-20-29)37(48)40-31(25-27-15-6-2-7-16-27)36(47)42-24-14-22-32(42)35(46)39-30/h2,6-7,15-16,26,28-32,43H,3-5,8-14,17-25H2,1H3,(H,39,46)(H,40,48)(H,41,45)/t26-,30-,31-,32+/m0/s1 MUOGWSZZDRMXBO-NKIORRDJSA-N 50588312 CHEMBL5203465 Histone deacetylase 4 Homo sapiens 670 ChEMBL 10.7270/Q25M69NW 34826681 Qiu, X; Zhu, L; Wang, H; Tan, Y; Yang, Z; Yang, L; Wan, L Chengdu University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50588312 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50588312&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168293383 482599164 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51457527 C[C@H](O)C(=O)CCCCC[C@@H]1NC(=O)[C@H]2CCCN2C(=O)[C@H](Cc2ccccc2)NC(=O)[C@@H](NC1=O)c1nc(C)c[nH]1 InChI=1S/C30H40N6O6/c1-18-17-31-26(32-18)25-29(41)34-22(16-20-10-5-3-6-11-20)30(42)36-15-9-13-23(36)28(40)33-21(27(39)35-25)12-7-4-8-14-24(38)19(2)37/h3,5-6,10-11,17,19,21-23,25,37H,4,7-9,12-16H2,1-2H3,(H,31,32)(H,33,40)(H,34,41)(H,35,39)/t19-,21-,22-,23+,25-/m0/s1 CNFXAXJBSTZPSF-LPXUDWAYSA-N 50588313 CHEMBL5179307 Histone deacetylase 4 Homo sapiens 350000 ChEMBL 10.7270/Q25M69NW 34826681 Qiu, X; Zhu, L; Wang, H; Tan, Y; Yang, Z; Yang, L; Wan, L Chengdu University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50588313 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50588313&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168273787 482599165 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51457528 C[C@H](\C=C(/C)\C=C\C(=O)NO)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1 RTKIYFITIVXBLE-QEQCGCAPSA-N 50005711 CHEBI:46024::GNF-Pf-1011::TRICHOSTATIN::Trichostatin A::Trichostatin A (TSA)::US10011611, Trichostatin A::US10722597, Compound Trichostatin::US11535598, Compound Trichostatin A::US9265734, TSA Histone deacetylase 4 Homo sapiens 15 ChEMBL 10.7270/Q25M69NW 34826681 Qiu, X; Zhu, L; Wang, H; Tan, Y; Yang, Z; Yang, L; Wan, L Chengdu University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 444732 242056952 DB04297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51458490 CN(C)c1ccc(cc1)C(=O)N(CC(=O)NCc1ccccc1)Cc1ccc(cc1F)C(=O)NO InChI=1S/C26H27FN4O4/c1-30(2)22-12-10-19(11-13-22)26(34)31(17-24(32)28-15-18-6-4-3-5-7-18)16-21-9-8-20(14-23(21)27)25(33)29-35/h3-14,35H,15-17H2,1-2H3,(H,28,32)(H,29,33) GBIQEYYBFBGNOZ-UHFFFAOYSA-N 50588683 CHEMBL5187433 Histone deacetylase 4 Homo sapiens 1880 ChEMBL 10.7270/Q22N5679 36351184 Reßing, N; Schliehe-Diecks, J; Watson, PR; Sönnichsen, M; Cragin, AD; Schöler, A; Yang, J; Schäker-Hübner, L; Borkhardt, A; Christianson, DW; Bhatia, S; Hansen, FK University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50588683 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50588683&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 0I 165430653 482599535 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51458491 CC(C)c1ccccc1C(=O)N(CC(=O)NC(C)(C)C)Cc1ccc(cc1F)C(=O)NO InChI=1S/C24H30FN3O4/c1-15(2)18-8-6-7-9-19(18)23(31)28(14-21(29)26-24(3,4)5)13-17-11-10-16(12-20(17)25)22(30)27-32/h6-12,15,32H,13-14H2,1-5H3,(H,26,29)(H,27,30) ICGXHGQIMMAKJH-UHFFFAOYSA-N 50588691 CHEMBL5170634 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.7270/Q22N5679 36351184 Reßing, N; Schliehe-Diecks, J; Watson, PR; Sönnichsen, M; Cragin, AD; Schöler, A; Yang, J; Schäker-Hübner, L; Borkhardt, A; Christianson, DW; Bhatia, S; Hansen, FK University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50588691 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50588691&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 166176969 482599543 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51457566 CN(CC#C)Cc1cccc(NC(=O)CCCCCCC(=O)NO)c1 InChI=1S/C19H27N3O3/c1-3-13-22(2)15-16-9-8-10-17(14-16)20-18(23)11-6-4-5-7-12-19(24)21-25/h1,8-10,14,25H,4-7,11-13,15H2,2H3,(H,20,23)(H,21,24) FQVRLKIMFQKGHF-UHFFFAOYSA-N 50588334 CHEMBL5171489 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.7270/Q2X352D4 34908406 Ojha, R; Chen, IC; Hsieh, CM; Nepali, K; Lai, RW; Hsu, KC; Lin, TE; Pan, SL; Chen, MC; Liou, JP Taipei Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50588334 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50588334&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162679302 482599186 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51470664 O=C(COc1ccc(\C=C2\SC(=O)NC2=O)cc1)N1N=C(CC1c1ccccc1)c1ccccc1 InChI=1S/C27H21N3O4S/c31-25(17-34-21-13-11-18(12-14-21)15-24-26(32)28-27(33)35-24)30-23(20-9-5-2-6-10-20)16-22(29-30)19-7-3-1-4-8-19/h1-15,23H,16-17H2,(H,28,32,33)/b24-15+ VLCQEDLNVOGCBZ-BUVRLJJBSA-N 50593352 CHEMBL5208471 Histone deacetylase 4 Homo sapiens 1600 ChEMBL 10.7270/Q22Z19HQ 34671737 Upadhyay, N; Tilekar, K; Safuan, S; Kumar, AP; Schweipert, M; Meyer-Almes, FJ; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593352 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593352&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168297065 482604204 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51470665 Clc1ccccc1C1CC(=NN1C(=O)COc1ccc(\C=C2\SC(=O)NC2=O)cc1)c1ccccc1 InChI=1S/C27H20ClN3O4S/c28-21-9-5-4-8-20(21)23-15-22(18-6-2-1-3-7-18)30-31(23)25(32)16-35-19-12-10-17(11-13-19)14-24-26(33)29-27(34)36-24/h1-14,23H,15-16H2,(H,29,33,34)/b24-14+ LUBGHYJLVUIGOO-ZVHZXABRSA-N 50593353 CHEMBL5188703 Histone deacetylase 4 Homo sapiens 1200 ChEMBL 10.7270/Q22Z19HQ 34671737 Upadhyay, N; Tilekar, K; Safuan, S; Kumar, AP; Schweipert, M; Meyer-Almes, FJ; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593353 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593353&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168278356 482604205 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51470666 FC(F)(F)c1ccc(cc1)C1CC(=NN1C(=O)COc1ccc(\C=C2\SC(=O)NC2=O)cc1)c1ccccc1 InChI=1S/C28H20F3N3O4S/c29-28(30,31)20-10-8-19(9-11-20)23-15-22(18-4-2-1-3-5-18)33-34(23)25(35)16-38-21-12-6-17(7-13-21)14-24-26(36)32-27(37)39-24/h1-14,23H,15-16H2,(H,32,36,37)/b24-14+ WTOASWGWURGURO-ZVHZXABRSA-N 50593354 CHEMBL5192137 Histone deacetylase 4 Homo sapiens 1000 ChEMBL 10.7270/Q22Z19HQ 34671737 Upadhyay, N; Tilekar, K; Safuan, S; Kumar, AP; Schweipert, M; Meyer-Almes, FJ; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593354 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593354&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168286528 482604206 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51470667 Fc1ccc(cc1)C1CC(=NN1C(=O)COc1ccc(\C=C2\SC(=O)NC2=O)cc1)c1ccccc1 InChI=1S/C27H20FN3O4S/c28-20-10-8-19(9-11-20)23-15-22(18-4-2-1-3-5-18)30-31(23)25(32)16-35-21-12-6-17(7-13-21)14-24-26(33)29-27(34)36-24/h1-14,23H,15-16H2,(H,29,33,34)/b24-14+ DYHQWVNUYSHGSV-ZVHZXABRSA-N 50593355 CHEMBL5192370 Histone deacetylase 4 Homo sapiens 1700 ChEMBL 10.7270/Q22Z19HQ 34671737 Upadhyay, N; Tilekar, K; Safuan, S; Kumar, AP; Schweipert, M; Meyer-Almes, FJ; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593355 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593355&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168284923 482604207 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51470668 Fc1ccc(C2CC(=NN2C(=O)COc2ccc(\C=C3\SC(=O)NC3=O)cc2)c2ccccc2)c(F)c1 InChI=1S/C27H19F2N3O4S/c28-18-8-11-20(21(29)13-18)23-14-22(17-4-2-1-3-5-17)31-32(23)25(33)15-36-19-9-6-16(7-10-19)12-24-26(34)30-27(35)37-24/h1-13,23H,14-15H2,(H,30,34,35)/b24-12+ MKNSRMBCTPCUPP-WYMPLXKRSA-N 50593356 CHEMBL5200735 Histone deacetylase 4 Homo sapiens 2200 ChEMBL 10.7270/Q22Z19HQ 34671737 Upadhyay, N; Tilekar, K; Safuan, S; Kumar, AP; Schweipert, M; Meyer-Almes, FJ; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593356 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593356&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168290796 482604208 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51470669 Cc1ccc(cc1)C1CC(=NN1C(=O)COc1ccc(\C=C2\SC(=O)NC2=O)cc1)c1ccccc1 InChI=1S/C28H23N3O4S/c1-18-7-11-21(12-8-18)24-16-23(20-5-3-2-4-6-20)30-31(24)26(32)17-35-22-13-9-19(10-14-22)15-25-27(33)29-28(34)36-25/h2-15,24H,16-17H2,1H3,(H,29,33,34)/b25-15+ RQZTVZAKQUZNLU-MFKUBSTISA-N 50593357 CHEMBL5205473 Histone deacetylase 4 Homo sapiens 1200 ChEMBL 10.7270/Q22Z19HQ 34671737 Upadhyay, N; Tilekar, K; Safuan, S; Kumar, AP; Schweipert, M; Meyer-Almes, FJ; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593357 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593357&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168296206 482604209 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51470670 Clc1ccc(cc1Cl)C1CC(=NN1C(=O)COc1ccc(\C=C2\SC(=O)NC2=O)cc1)c1ccccc1 InChI=1S/C27H19Cl2N3O4S/c28-20-11-8-18(13-21(20)29)23-14-22(17-4-2-1-3-5-17)31-32(23)25(33)15-36-19-9-6-16(7-10-19)12-24-26(34)30-27(35)37-24/h1-13,23H,14-15H2,(H,30,34,35)/b24-12+ JTPZHEMUSATIFE-WYMPLXKRSA-N 50593358 CHEMBL5194067 Histone deacetylase 4 Homo sapiens 700 ChEMBL 10.7270/Q22Z19HQ 34671737 Upadhyay, N; Tilekar, K; Safuan, S; Kumar, AP; Schweipert, M; Meyer-Almes, FJ; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593358 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593358&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168287058 482604210 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51470671 Brc1ccc(cc1)C1CC(=NN1C(=O)COc1ccc(\C=C2\SC(=O)NC2=O)cc1)c1ccccc1 InChI=1S/C27H20BrN3O4S/c28-20-10-8-19(9-11-20)23-15-22(18-4-2-1-3-5-18)30-31(23)25(32)16-35-21-12-6-17(7-13-21)14-24-26(33)29-27(34)36-24/h1-14,23H,15-16H2,(H,29,33,34)/b24-14+ IFJXVWSHPAFIAU-ZVHZXABRSA-N 50593359 CHEMBL5189207 Histone deacetylase 4 Homo sapiens 1200 ChEMBL 10.7270/Q22Z19HQ 34671737 Upadhyay, N; Tilekar, K; Safuan, S; Kumar, AP; Schweipert, M; Meyer-Almes, FJ; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593359 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593359&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168278410 482604211 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51470672 Fc1ccc(cc1)C1=NN(C(C1)c1ccccc1)C(=O)COc1ccc(\C=C2\SC(=O)NC2=O)cc1 InChI=1S/C27H20FN3O4S/c28-20-10-8-18(9-11-20)22-15-23(19-4-2-1-3-5-19)31(30-22)25(32)16-35-21-12-6-17(7-13-21)14-24-26(33)29-27(34)36-24/h1-14,23H,15-16H2,(H,29,33,34)/b24-14+ XZGDQEORMIPPRP-ZVHZXABRSA-N 50593360 CHEMBL5189623 Histone deacetylase 4 Homo sapiens 4200 ChEMBL 10.7270/Q22Z19HQ 34671737 Upadhyay, N; Tilekar, K; Safuan, S; Kumar, AP; Schweipert, M; Meyer-Almes, FJ; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593360 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593360&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168283179 482604212 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51470673 Fc1ccc(cc1)C1=NN(C(C1)c1ccccc1Cl)C(=O)COc1ccc(\C=C2\SC(=O)NC2=O)cc1 InChI=1S/C27H19ClFN3O4S/c28-21-4-2-1-3-20(21)23-14-22(17-7-9-18(29)10-8-17)31-32(23)25(33)15-36-19-11-5-16(6-12-19)13-24-26(34)30-27(35)37-24/h1-13,23H,14-15H2,(H,30,34,35)/b24-13+ DAUNZNGVBFJIKV-ZMOGYAJESA-N 50593361 CHEMBL5203530 Histone deacetylase 4 Homo sapiens 1100 ChEMBL 10.7270/Q22Z19HQ 34671737 Upadhyay, N; Tilekar, K; Safuan, S; Kumar, AP; Schweipert, M; Meyer-Almes, FJ; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593361 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593361&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168293179 482604213 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51470674 Fc1ccc(cc1)C1=NN(C(C1)c1ccco1)C(=O)COc1ccc(\C=C2\SC(=O)NC2=O)cc1 InChI=1S/C25H18FN3O5S/c26-17-7-5-16(6-8-17)19-13-20(21-2-1-11-33-21)29(28-19)23(30)14-34-18-9-3-15(4-10-18)12-22-24(31)27-25(32)35-22/h1-12,20H,13-14H2,(H,27,31,32)/b22-12+ KXAPDKXGXJJUQC-WSDLNYQXSA-N 50593362 CHEMBL5174358 Histone deacetylase 4 Homo sapiens 880 ChEMBL 10.7270/Q22Z19HQ 34671737 Upadhyay, N; Tilekar, K; Safuan, S; Kumar, AP; Schweipert, M; Meyer-Almes, FJ; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593362 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593362&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168274002 482604214 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51470675 Fc1ccc(cc1)C1=NN(C(C1)c1ccc(cc1)C(F)(F)F)C(=O)COc1ccc(\C=C2\SC(=O)NC2=O)cc1 InChI=1S/C28H19F4N3O4S/c29-20-9-5-17(6-10-20)22-14-23(18-3-7-19(8-4-18)28(30,31)32)35(34-22)25(36)15-39-21-11-1-16(2-12-21)13-24-26(37)33-27(38)40-24/h1-13,23H,14-15H2,(H,33,37,38)/b24-13+ KRNQTAXFNJUQTP-ZMOGYAJESA-N 50593363 CHEMBL5203024 Histone deacetylase 4 Homo sapiens 1300 ChEMBL 10.7270/Q22Z19HQ 34671737 Upadhyay, N; Tilekar, K; Safuan, S; Kumar, AP; Schweipert, M; Meyer-Almes, FJ; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593363 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593363&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168292900 482604215 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51470676 Fc1ccc(cc1)C1CC(=NN1C(=O)COc1ccc(\C=C2\SC(=O)NC2=O)cc1)c1ccc(F)cc1 InChI=1S/C27H19F2N3O4S/c28-19-7-3-17(4-8-19)22-14-23(18-5-9-20(29)10-6-18)32(31-22)25(33)15-36-21-11-1-16(2-12-21)13-24-26(34)30-27(35)37-24/h1-13,23H,14-15H2,(H,30,34,35)/b24-13+ WOLHRAFKOJVOHK-ZMOGYAJESA-N 50593364 CHEMBL5196025 Histone deacetylase 4 Homo sapiens 1400 ChEMBL 10.7270/Q22Z19HQ 34671737 Upadhyay, N; Tilekar, K; Safuan, S; Kumar, AP; Schweipert, M; Meyer-Almes, FJ; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593364 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593364&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168284747 482604216 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51470677 Fc1ccc(cc1)C1=NN(C(C1)c1ccc(F)cc1F)C(=O)COc1ccc(\C=C2\SC(=O)NC2=O)cc1 InChI=1S/C27H18F3N3O4S/c28-17-5-3-16(4-6-17)22-13-23(20-10-7-18(29)12-21(20)30)33(32-22)25(34)14-37-19-8-1-15(2-9-19)11-24-26(35)31-27(36)38-24/h1-12,23H,13-14H2,(H,31,35,36)/b24-11+ FBYDUABKHMDYLH-BHGWPJFGSA-N 50593365 CHEMBL5173048 Histone deacetylase 4 Homo sapiens 1600 ChEMBL 10.7270/Q22Z19HQ 34671737 Upadhyay, N; Tilekar, K; Safuan, S; Kumar, AP; Schweipert, M; Meyer-Almes, FJ; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593365 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593365&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168272439 482604217 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51470678 Cc1ccc(cc1)C1CC(=NN1C(=O)COc1ccc(\C=C2\SC(=O)NC2=O)cc1)c1ccc(F)cc1 InChI=1S/C28H22FN3O4S/c1-17-2-6-20(7-3-17)24-15-23(19-8-10-21(29)11-9-19)31-32(24)26(33)16-36-22-12-4-18(5-13-22)14-25-27(34)30-28(35)37-25/h2-14,24H,15-16H2,1H3,(H,30,34,35)/b25-14+ PWHYKDWFJPIARJ-AFUMVMLFSA-N 50593366 CHEMBL5176437 Histone deacetylase 4 Homo sapiens 1800 ChEMBL 10.7270/Q22Z19HQ 34671737 Upadhyay, N; Tilekar, K; Safuan, S; Kumar, AP; Schweipert, M; Meyer-Almes, FJ; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593366 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593366&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168273102 482604218 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51470679 Fc1ccc(cc1)C1=NN(C(C1)c1ccc(Cl)c(Cl)c1)C(=O)COc1ccc(\C=C2\SC(=O)NC2=O)cc1 InChI=1S/C27H18Cl2FN3O4S/c28-20-10-5-17(12-21(20)29)23-13-22(16-3-6-18(30)7-4-16)32-33(23)25(34)14-37-19-8-1-15(2-9-19)11-24-26(35)31-27(36)38-24/h1-12,23H,13-14H2,(H,31,35,36)/b24-11+ DTVNAEHYBVIKTD-BHGWPJFGSA-N 50593367 CHEMBL5183909 Histone deacetylase 4 Homo sapiens 800 ChEMBL 10.7270/Q22Z19HQ 34671737 Upadhyay, N; Tilekar, K; Safuan, S; Kumar, AP; Schweipert, M; Meyer-Almes, FJ; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593367 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593367&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168279831 482604219 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51470680 Fc1ccc(C2=NN(C(C2)c2ccco2)C(=O)COc2ccc(\C=C3\SC(=O)NC3=O)cc2)c(F)c1 InChI=1S/C25H17F2N3O5S/c26-15-5-8-17(18(27)11-15)19-12-20(21-2-1-9-34-21)30(29-19)23(31)13-35-16-6-3-14(4-7-16)10-22-24(32)28-25(33)36-22/h1-11,20H,12-13H2,(H,28,32,33)/b22-10+ UZERPFJICOIUMF-LSHDLFTRSA-N 50593368 CHEMBL5176817 Histone deacetylase 4 Homo sapiens 15000 ChEMBL 10.7270/Q22Z19HQ 34671737 Upadhyay, N; Tilekar, K; Safuan, S; Kumar, AP; Schweipert, M; Meyer-Almes, FJ; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593368 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593368&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168275444 482604220 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51470681 Fc1ccc(cc1)C1CC(=NN1C(=O)COc1ccc(\C=C2\SC(=O)NC2=O)cc1)c1ccc(F)cc1F InChI=1S/C27H18F3N3O4S/c28-17-5-3-16(4-6-17)23-13-22(20-10-7-18(29)12-21(20)30)32-33(23)25(34)14-37-19-8-1-15(2-9-19)11-24-26(35)31-27(36)38-24/h1-12,23H,13-14H2,(H,31,35,36)/b24-11+ VGHMSLZMRYYKFP-BHGWPJFGSA-N 50593369 CHEMBL5170222 Histone deacetylase 4 Homo sapiens 1500 ChEMBL 10.7270/Q22Z19HQ 34671737 Upadhyay, N; Tilekar, K; Safuan, S; Kumar, AP; Schweipert, M; Meyer-Almes, FJ; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593369 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593369&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168268959 482604221 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51470682 Cc1ccc(cc1)C1CC(=NN1C(=O)COc1ccc(\C=C2\SC(=O)NC2=O)cc1)c1ccc(F)cc1F InChI=1S/C28H21F2N3O4S/c1-16-2-6-18(7-3-16)24-14-23(21-11-8-19(29)13-22(21)30)32-33(24)26(34)15-37-20-9-4-17(5-10-20)12-25-27(35)31-28(36)38-25/h2-13,24H,14-15H2,1H3,(H,31,35,36)/b25-12+ SVJZOFSLJQBMFT-BRJLIKDPSA-N 50593370 CHEMBL5199025 Histone deacetylase 4 Homo sapiens 1500 ChEMBL 10.7270/Q22Z19HQ 34671737 Upadhyay, N; Tilekar, K; Safuan, S; Kumar, AP; Schweipert, M; Meyer-Almes, FJ; C S, R Bharati Vidyapeeth's College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50593370 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50593370&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168286858 482604222 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51473190 ONC(=O)c1ccc(CN2CCN(CC2)C(c2ccccc2)c2ccccc2)cc1 InChI=1S/C25H27N3O2/c29-25(26-30)23-13-11-20(12-14-23)19-27-15-17-28(18-16-27)24(21-7-3-1-4-8-21)22-9-5-2-6-10-22/h1-14,24,30H,15-19H2,(H,26,29) WYZGPGZJNOPQLB-UHFFFAOYSA-N 50594395 CHEMBL5189146 Histone deacetylase 4 Homo sapiens 4400 ChEMBL 10.7270/Q2NG4VP5 35859864 Hashimoto, K; Ide, S; Arata, M; Nakata, A; Ito, A; Ito, TK; Kudo, N; Lin, B; Nunomura, K; Tsuganezawa, K; Yoshida, M; Nagaoka, Y; Sumiyoshi, T Kansai University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50594395 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50594395&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168290670 482605247 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51473191 ONC(=O)c1ccc(CCN2CCN(CC2)C(c2ccccc2)c2ccccc2)cc1 InChI=1S/C26H29N3O2/c30-26(27-31)24-13-11-21(12-14-24)15-16-28-17-19-29(20-18-28)25(22-7-3-1-4-8-22)23-9-5-2-6-10-23/h1-14,25,31H,15-20H2,(H,27,30) CJSCFEBBGAGVJI-UHFFFAOYSA-N 50594396 CHEMBL5172611 Histone deacetylase 4 Homo sapiens 3000 ChEMBL 10.7270/Q2NG4VP5 35859864 Hashimoto, K; Ide, S; Arata, M; Nakata, A; Ito, A; Ito, TK; Kudo, N; Lin, B; Nunomura, K; Tsuganezawa, K; Yoshida, M; Nagaoka, Y; Sumiyoshi, T Kansai University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50594396 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50594396&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168271166 482605248 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51473192 ONC(=O)c1ccc(CCCN2CCN(CC2)C(c2ccccc2)c2ccccc2)cc1 InChI=1S/C27H31N3O2/c31-27(28-32)25-15-13-22(14-16-25)8-7-17-29-18-20-30(21-19-29)26(23-9-3-1-4-10-23)24-11-5-2-6-12-24/h1-6,9-16,26,32H,7-8,17-21H2,(H,28,31) SFMNWYGDIXMZNK-UHFFFAOYSA-N 50594397 CHEMBL5193136 Histone deacetylase 4 Homo sapiens 1900 ChEMBL 10.7270/Q2NG4VP5 35859864 Hashimoto, K; Ide, S; Arata, M; Nakata, A; Ito, A; Ito, TK; Kudo, N; Lin, B; Nunomura, K; Tsuganezawa, K; Yoshida, M; Nagaoka, Y; Sumiyoshi, T Kansai University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50594397 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50594397&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168290111 482605249 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51473193 ONC(=O)c1ccc(CCCCN2CCN(CC2)C(c2ccccc2)c2ccccc2)cc1 InChI=1S/C28H33N3O2/c32-28(29-33)26-16-14-23(15-17-26)9-7-8-18-30-19-21-31(22-20-30)27(24-10-3-1-4-11-24)25-12-5-2-6-13-25/h1-6,10-17,27,33H,7-9,18-22H2,(H,29,32) VESYDOZDDMFQMJ-UHFFFAOYSA-N 50594398 CHEMBL5175813 Histone deacetylase 4 Homo sapiens 5000 ChEMBL 10.7270/Q2NG4VP5 35859864 Hashimoto, K; Ide, S; Arata, M; Nakata, A; Ito, A; Ito, TK; Kudo, N; Lin, B; Nunomura, K; Tsuganezawa, K; Yoshida, M; Nagaoka, Y; Sumiyoshi, T Kansai University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50594398 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50594398&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168276122 482605250 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51473194 ONC(=O)c1ccccc1CN1CCN(CC1)C(c1ccccc1)c1ccccc1 InChI=1S/C25H27N3O2/c29-25(26-30)23-14-8-7-13-22(23)19-27-15-17-28(18-16-27)24(20-9-3-1-4-10-20)21-11-5-2-6-12-21/h1-14,24,30H,15-19H2,(H,26,29) SXTFIMHINDWWNJ-UHFFFAOYSA-N 50594399 CHEMBL5198614 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.7270/Q2NG4VP5 35859864 Hashimoto, K; Ide, S; Arata, M; Nakata, A; Ito, A; Ito, TK; Kudo, N; Lin, B; Nunomura, K; Tsuganezawa, K; Yoshida, M; Nagaoka, Y; Sumiyoshi, T Kansai University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50594399 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50594399&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168286000 482605251 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51473195 ONC(=O)c1cccc(CN2CCN(CC2)C(c2ccccc2)c2ccccc2)c1 InChI=1S/C25H27N3O2/c29-25(26-30)23-13-7-8-20(18-23)19-27-14-16-28(17-15-27)24(21-9-3-1-4-10-21)22-11-5-2-6-12-22/h1-13,18,24,30H,14-17,19H2,(H,26,29) AXOOZPHQPAOTFP-UHFFFAOYSA-N 50594400 CHEMBL5205202 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.7270/Q2NG4VP5 35859864 Hashimoto, K; Ide, S; Arata, M; Nakata, A; Ito, A; Ito, TK; Kudo, N; Lin, B; Nunomura, K; Tsuganezawa, K; Yoshida, M; Nagaoka, Y; Sumiyoshi, T Kansai University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50594400 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50594400&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168296918 482605252 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51473196 CC(N1CCN(Cc2ccc(cc2)C(=O)NO)CC1)c1ccccc1 InChI=1S/C20H25N3O2/c1-16(18-5-3-2-4-6-18)23-13-11-22(12-14-23)15-17-7-9-19(10-8-17)20(24)21-25/h2-10,16,25H,11-15H2,1H3,(H,21,24) ZHVQXJZQHWNCES-UHFFFAOYSA-N 50594394 CHEMBL5195750 Histone deacetylase 4 Homo sapiens 12300 ChEMBL 10.7270/Q2NG4VP5 35859864 Hashimoto, K; Ide, S; Arata, M; Nakata, A; Ito, A; Ito, TK; Kudo, N; Lin, B; Nunomura, K; Tsuganezawa, K; Yoshida, M; Nagaoka, Y; Sumiyoshi, T Kansai University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50594394 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50594394&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 164887483 482605246 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51473197 ONC(=O)c1ccc(CN2CCN(Cc3ccccc3)CC2)cc1 InChI=1S/C19H23N3O2/c23-19(20-24)18-8-6-17(7-9-18)15-22-12-10-21(11-13-22)14-16-4-2-1-3-5-16/h1-9,24H,10-15H2,(H,20,23) YUDJFSRXZHYHCF-UHFFFAOYSA-N 50594401 CHEMBL5192796 Histone deacetylase 4 Homo sapiens 9200 ChEMBL 10.7270/Q2NG4VP5 35859864 Hashimoto, K; Ide, S; Arata, M; Nakata, A; Ito, A; Ito, TK; Kudo, N; Lin, B; Nunomura, K; Tsuganezawa, K; Yoshida, M; Nagaoka, Y; Sumiyoshi, T Kansai University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50594401 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50594401&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168287377 482605253 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51483629 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1 InChI=1S/C24H27N5O3/c30-22(28-32)15-9-1-2-10-16-25-23(31)19-17-26-24(27-18-19)29(20-11-5-3-6-12-20)21-13-7-4-8-14-21/h3-8,11-14,17-18,32H,1-2,9-10,15-16H2,(H,25,31)(H,28,30) QGZYDVAGYRLSKP-UHFFFAOYSA-N 50439674 RICOLINOSTAT::US10858323, Compound 2::US11207431, Example E::US8609678, 2-(diphenylamino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [26] Histone deacetylase 4 Homo sapiens 7000 ChEMBL 10.7270/Q2FF3XCC 34992037 Gu, X; Zhang, H; Jiao, M; Han, B; Zhang, Z; Li, J; Zhang, Q Shanghai Institute of Pharmaceutical Industry http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50439674 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50439674&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search AH4 5WGL 53340666 175451991 ZINC89630354 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51483642 OCCN(C(=O)Cc1ccc(cc1)C(=O)NO)c1ccccc1 InChI=1S/C17H18N2O4/c20-11-10-19(15-4-2-1-3-5-15)16(21)12-13-6-8-14(9-7-13)17(22)18-23/h1-9,20,23H,10-12H2,(H,18,22) RFAZNTABYJYOAR-UHFFFAOYSA-N 198121 HPOB Histone deacetylase 4 Homo sapiens 1700 ChEMBL 10.7270/Q2FF3XCC 34992037 Gu, X; Zhang, H; Jiao, M; Han, B; Zhang, Z; Li, J; Zhang, Q Shanghai Institute of Pharmaceutical Industry http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=198121 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=198121&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5OJ 5EF7 71532921 318489194 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51483646 CN(Cc1ccc(cc1F)C(=O)NO)CC12CC3CC(CC(C3)C1)C2 InChI=1S/C20H27FN2O2/c1-23(11-17-3-2-16(7-18(17)21)19(24)22-25)12-20-8-13-4-14(9-20)6-15(5-13)10-20/h2-3,7,13-15,25H,4-6,8-12H2,1H3,(H,22,24) IGZQZELTOHAHNW-UHFFFAOYSA-N 50369345 CHEMBL4165724::US11207431, Example 1 Histone deacetylase 4 Homo sapiens 11300 ChEMBL 10.7270/Q2FF3XCC 34992037 Gu, X; Zhang, H; Jiao, M; Han, B; Zhang, Z; Li, J; Zhang, Q Shanghai Institute of Pharmaceutical Industry http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50369345 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50369345&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search HBV 6DVO 134812690 160848447 ZINC49055016 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51483660 ONC(=O)c1ccc(CN2CCCc3cc(Cl)ccc23)cc1 InChI=1S/C17H17ClN2O2/c18-15-7-8-16-14(10-15)2-1-9-20(16)11-12-3-5-13(6-4-12)17(21)19-22/h3-8,10,22H,1-2,9,11H2,(H,19,21) MNAYBFFSFQRSIT-UHFFFAOYSA-N 417049 4-((6-chloro-3,4-dihydroquinolin-1(2H)-yl)methyl)-N-hydroxybenzamide::US10456394, Example 2 Histone deacetylase 4 Homo sapiens 10900 ChEMBL 10.7270/Q2FF3XCC 34992037 Gu, X; Zhang, H; Jiao, M; Han, B; Zhang, Z; Li, J; Zhang, Q Shanghai Institute of Pharmaceutical Industry http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=417049 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=417049&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 130345472 433916959 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319049 Nc1nc2ccc(cc2s1)-c1cn(Cc2ccc(cn2)-c2nnc(o2)C(F)F)nn1 InChI=1S/C18H12F2N8OS/c19-15(20)17-26-25-16(29-17)10-1-3-11(22-6-10)7-28-8-13(24-27-28)9-2-4-12-14(5-9)30-18(21)23-12/h1-6,8,15H,7H2,(H2,21,23) OMBLFALZRDKBTB-UHFFFAOYSA-N 617829 US20230286970, Compound 1::US20230286970, Compound 376 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=617829 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=617829&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319058 Oc1ccc(cc1NC(=O)N1CCOCC1)-c1nnn(Cc2ccc(cn2)-c2nnc(o2)C(F)F)n1 InChI=1S/C21H19F2N9O4/c22-17(23)20-28-27-19(36-20)13-1-3-14(24-10-13)11-32-29-18(26-30-32)12-2-4-16(33)15(9-12)25-21(34)31-5-7-35-8-6-31/h1-4,9-10,17,33H,5-8,11H2,(H,25,34) PVBHGUJECHBXIV-UHFFFAOYSA-N 617923 US20230286970, Compound 2 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=617923 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=617923&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319067 Nc1nc2cc(ccc2s1)-c1cn(Cc2ccc(cn2)-c2nnc(o2)C(F)F)nn1 InChI=1S/C18H12F2N8OS/c19-15(20)17-26-25-16(29-17)10-1-3-11(22-6-10)7-28-8-13(24-27-28)9-2-4-14-12(5-9)23-18(21)30-14/h1-6,8,15H,7H2,(H2,21,23) XLADEYDEIYUWPJ-UHFFFAOYSA-N 617942 US20230286970, Compound 3 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=617942 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=617942&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319076 FC(F)c1nnc(o1)-c1ccc(Cn2nnc(n2)-c2ccc3CNC(=O)c3c2)nc1 InChI=1S/C18H12F2N8O2/c19-14(20)18-25-24-17(30-18)11-3-4-12(21-7-11)8-28-26-15(23-27-28)9-1-2-10-6-22-16(29)13(10)5-9/h1-5,7,14H,6,8H2,(H,22,29) HUHKHDDDRIDTNY-UHFFFAOYSA-N 617985 US20230286970, Compound 4 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=617985 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=617985&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162722513 484207170 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319085 Nc1ccc(cn1)-c1cn(Cc2ccc(cn2)-c2nnc(o2)C(F)F)nn1 InChI=1S/C16H12F2N8O/c17-14(18)16-24-23-15(27-16)10-1-3-11(20-6-10)7-26-8-12(22-25-26)9-2-4-13(19)21-5-9/h1-6,8,14H,7H2,(H2,19,21) BNODAOHYITZHKT-UHFFFAOYSA-N 617987 5-(1-((5-(5-(difluoromethyl)-1,3,4-oxadiazol-2-yl)pyridin-2-yl)methyl)-1H-1,2,3-triazol-4-yl)pyridin-2-amine::US20230286970, Compound 362::US20230286970, Compound 5 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=617987 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=617987&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162721935 484207172 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319094 FC(F)c1nnc(o1)-c1ccc(Cn2cc(nn2)-c2cccc(NC(=O)N3CCOCC3)c2)nc1 InChI=1S/C22H20F2N8O3/c23-19(24)21-29-28-20(35-21)15-4-5-17(25-11-15)12-32-13-18(27-30-32)14-2-1-3-16(10-14)26-22(33)31-6-8-34-9-7-31/h1-5,10-11,13,19H,6-9,12H2,(H,26,33) UTXOOXKUYRMOQL-UHFFFAOYSA-N 618044 US20230286970, Compound 369::US20230286970, Compound 6 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=618044 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=618044&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168071674 484207210 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319103 Nc1nc2cc(ccc2o1)-c1nnn(Cc2ccc(cn2)-c2nnc(o2)C(F)F)n1 InChI=1S/C17H11F2N9O2/c18-13(19)16-25-24-15(30-16)9-1-3-10(21-6-9)7-28-26-14(23-27-28)8-2-4-12-11(5-8)22-17(20)29-12/h1-6,13H,7H2,(H2,20,22) JDDMBYXSGPQZNS-UHFFFAOYSA-N 618046 5-(2-((5-(5-(difluoromethyl)-1,3,4-oxadiazol-2-yl)pyridin-2-yl)methyl)-2H-tetrazol-5-yl)benzo[d]oxazol-2-amine::US20230286970, Compound 7 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=618046 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=618046&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162722213 484207212 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319112 Nc1nc2cc(ccc2[nH]1)-c1cn(Cc2ccc(cc2)-c2nnc(o2)C(F)F)nn1 InChI=1S/C19H14F2N8O/c20-16(21)18-27-26-17(30-18)11-3-1-10(2-4-11)8-29-9-15(25-28-29)12-5-6-13-14(7-12)24-19(22)23-13/h1-7,9,16H,8H2,(H3,22,23,24) SIIXFWVWBDUVLC-UHFFFAOYSA-N 618048 US20230286970, Compound 8 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=618048 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=618048&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162721877 484207214 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319121 FC(F)c1nnc(o1)-c1ccc(Cn2cc(nn2)-c2ccc3nc(Cl)[nH]c3c2)nc1 InChI=1S/C18H11ClF2N8O/c19-18-23-12-4-2-9(5-13(12)24-18)14-8-29(28-25-14)7-11-3-1-10(6-22-11)16-26-27-17(30-16)15(20)21/h1-6,8,15H,7H2,(H,23,24) XZXKUPHQVYSICW-UHFFFAOYSA-N 618050 US20230286970, Compound 9 Histone deacetylase 4 Homo sapiens 5012 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=618050 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=618050&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162722291 484207216 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319130 FC(F)c1nnc(o1)-c1ccc(Cn2cc(nn2)-c2ccc(NC3=NCCN3)cc2)cc1 InChI=1S/C21H18F2N8O/c22-18(23)20-29-28-19(32-20)15-3-1-13(2-4-15)11-31-12-17(27-30-31)14-5-7-16(8-6-14)26-21-24-9-10-25-21/h1-8,12,18H,9-11H2,(H2,24,25,26) TYHUIOMFTMEPGK-UHFFFAOYSA-N 618052 N-(4-(1-(4-(5-(difluoromethyl)-1,3,4-oxadiazol-2-yl)benzyl)-1H-1,2,3-triazol-4-yl)phenyl)-4,5-dihydro-1H-imidazol-2-amine::US20230286970, Compound 10 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=618052 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=618052&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162722395 484207218 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319139 Cn1c(N)nc2cc(ccc12)-c1nnn(Cc2ccc(cc2)-c2nnc(o2)C(F)F)n1 InChI=1S/C19H15F2N9O/c1-29-14-7-6-12(8-13(14)23-19(29)22)16-24-28-30(27-16)9-10-2-4-11(5-3-10)17-25-26-18(31-17)15(20)21/h2-8,15H,9H2,1H3,(H2,22,23) AVECTCURTFQCOF-UHFFFAOYSA-N 618054 US20230286970, Compound 11 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=618054 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=618054&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162722868 484207220 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319148 Nc1ccc(cn1)-c1cn(Cc2ccc(cn2)-c2nnc(o2)C(F)F)cn1 InChI=1S/C17H13F2N7O/c18-15(19)17-25-24-16(27-17)11-1-3-12(21-6-11)7-26-8-13(23-9-26)10-2-4-14(20)22-5-10/h1-6,8-9,15H,7H2,(H2,20,22) FFJDJXGCLZTXFF-UHFFFAOYSA-N 618056 5-(1-((5-(5-(difluoromethyl)-1,3,4-oxadiazol-2-yl)pyridin-2-yl)methyl)-1H-imidazol-4-yl)pyridin-2-amine::US20230286970, Compound 12 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=618056 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=618056&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162722708 484207222 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319157 Nc1ccc(cn1)-c1cnn(Cc2ccc(cn2)-c2nnc(o2)C(F)F)c1 InChI=1S/C17H13F2N7O/c18-15(19)17-25-24-16(27-17)11-1-3-13(21-6-11)9-26-8-12(7-23-26)10-2-4-14(20)22-5-10/h1-8,15H,9H2,(H2,20,22) JZEOPNVLCLUFDT-UHFFFAOYSA-N 618058 5-(1-((5-(5-(difluoromethyl)-1,3,4-oxadiazol-2-yl)pyridin-2-yl)methyl)-1H-pyrazol-4-yl)pyridin-2-amine::US20230286970, Compound 13 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=618058 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=618058&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162722416 484207224 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319166 Nc1nc2ccc(cc2s1)-c1cn(Cc2ccc(cc2)-c2nnc(o2)C(F)F)nn1 InChI=1S/C19H13F2N7OS/c20-16(21)18-26-25-17(29-18)11-3-1-10(2-4-11)8-28-9-14(24-27-28)12-5-6-13-15(7-12)30-19(22)23-13/h1-7,9,16H,8H2,(H2,22,23) QFNSRVAHUAFRHU-UHFFFAOYSA-N 618060 US20230286970, Compound 14::US20230286970, Compound 351 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=618060 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=618060&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162722044 484207226 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319175 Nc1ccc(cn1)-c1cn(Cc2ccc(-c3nnc(o3)C(F)F)c(F)c2)nn1 InChI=1S/C17H12F3N7O/c18-12-5-9(1-3-11(12)16-24-25-17(28-16)15(19)20)7-27-8-13(23-26-27)10-2-4-14(21)22-6-10/h1-6,8,15H,7H2,(H2,21,22) WAKCHHYREWYBRH-UHFFFAOYSA-N 618062 US20230286970, Compound 15 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=618062 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=618062&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162722319 484207228 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319184 FC(F)c1nnc(o1)-c1ccc(Cn2cc(nn2)-c2cccc(NC(=O)N3CCOCC3)c2)cc1F InChI=1S/C23H20F3N7O3/c24-18-10-14(4-5-17(18)21-29-30-22(36-21)20(25)26)12-33-13-19(28-31-33)15-2-1-3-16(11-15)27-23(34)32-6-8-35-9-7-32/h1-5,10-11,13,20H,6-9,12H2,(H,27,34) BEBPZCLNKBKSSB-UHFFFAOYSA-N 618064 US20230286970, Compound 16 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=618064 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=618064&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162721909 484207230 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319193 Cn1c(N)nc2cc(ccc12)-c1cn(Cc2ccc(cn2)-c2nnc(o2)C(F)F)nn1 InChI=1S/C19H15F2N9O/c1-29-15-5-3-10(6-13(15)24-19(29)22)14-9-30(28-25-14)8-12-4-2-11(7-23-12)17-26-27-18(31-17)16(20)21/h2-7,9,16H,8H2,1H3,(H2,22,24) XPHWMPZXOJFZID-UHFFFAOYSA-N 618066 5-(1-((5-(5-(difluoromethyl)-1,3,4-oxadiazol-2-yl)pyridin-2-yl)methyl)-1H-1,2,3-triazol-4-yl)-1-methyl-1H-benzo[d]imidazol-2-amine::US20230286970, Compound 17 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=618066 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=618066&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162721925 484207232 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319202 CCNc1nc2ccc(cc2[nH]1)-c1cn(Cc2ccc(cn2)-c2nnc(o2)C(F)F)nn1 InChI=1S/C20H17F2N9O/c1-2-23-20-25-14-6-4-11(7-15(14)26-20)16-10-31(30-27-16)9-13-5-3-12(8-24-13)18-28-29-19(32-18)17(21)22/h3-8,10,17H,2,9H2,1H3,(H2,23,25,26) QCIJLXOEDAOJDH-UHFFFAOYSA-N 618068 6-(1-((5-(5-(difluoromethyl)-1,3,4-oxadiazol-2-yl)pyridin-2-yl)methyl)-1H-1,2,3-triazol-4-yl)-N-ethyl-1H-benzo[d]imidazol-2-amine::US20230286970, Compound 18 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=618068 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=618068&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162721960 484207234 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319211 FC(F)c1nnc(o1)-c1ccc(Cn2cc(nn2)-c2ccc3NC(=O)C4(CCNCC4)c3c2)nc1 InChI=1S/C23H20F2N8O2/c24-19(25)21-31-30-20(35-21)14-1-3-15(27-10-14)11-33-12-18(29-32-33)13-2-4-17-16(9-13)23(22(34)28-17)5-7-26-8-6-23/h1-4,9-10,12,19,26H,5-8,11H2,(H,28,34) KZZUQQMAYXHSSP-UHFFFAOYSA-N 618070 US20230286970, Compound 19 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=618070 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=618070&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162722732 484207236 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319220 FC(F)c1nnc(o1)-c1ccc(Cn2cnc(c2)-c2ccc(NC3=NCCN3)cc2)nc1 InChI=1S/C21H18F2N8O/c22-18(23)20-30-29-19(32-20)14-3-6-16(26-9-14)10-31-11-17(27-12-31)13-1-4-15(5-2-13)28-21-24-7-8-25-21/h1-6,9,11-12,18H,7-8,10H2,(H2,24,25,28) IGKXJIIJJSSKNC-UHFFFAOYSA-N 618072 US20230286970, Compound 20 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=618072 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=618072&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162722310 484207238 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319229 Nc1ccc(cn1)-c1cn(Cc2ccc(-c3nnc(o3)C(F)F)c(F)c2F)nn1 InChI=1S/C17H11F4N7O/c18-13-9(1-3-10(14(13)19)16-25-26-17(29-16)15(20)21)6-28-7-11(24-27-28)8-2-4-12(22)23-5-8/h1-5,7,15H,6H2,(H2,22,23) VWMYIUMAPMTYHC-UHFFFAOYSA-N 618074 5-(1-(4-(5-(difluoromethyl)-1,3,4-oxadiazol-2-yl)-2,3-difluorobenzyl)-1H-1,2,3-triazol-4-yl)pyridin-2-amine::US20230286970, Compound 21::US20230286970, Compound 385 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=618074 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=618074&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162721884 484207240 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319238 FC(F)c1nnc(o1)-c1ccc(Cn2cnc(c2)-c2ccc(NC3=NCCN3)cc2)cc1 InChI=1S/C22H19F2N7O/c23-19(24)21-30-29-20(32-21)16-3-1-14(2-4-16)11-31-12-18(27-13-31)15-5-7-17(8-6-15)28-22-25-9-10-26-22/h1-8,12-13,19H,9-11H2,(H2,25,26,28) FHFVNBYDMLGBHU-UHFFFAOYSA-N 618076 N-(4-(1-(4-(5-(difluoromethyl)-1,3,4-oxadiazol-2-yl)benzyl)-1H-imidazol-4-yl)phenyl)-4,5-dihydro-1H-imidazol-2-amine::US20230286970, Compound 22::US20230286970, Compound 368 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=618076 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=618076&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162722379 484207242 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 1319247 Cn1c(N)nc2cc(ccc12)-c1cn(Cc2ccc(cc2)-c2nnc(o2)C(F)F)nn1 InChI=1S/C20H16F2N8O/c1-29-16-7-6-13(8-14(16)24-20(29)23)15-10-30(28-25-15)9-11-2-4-12(5-3-11)18-26-27-19(31-18)17(21)22/h2-8,10,17H,9H2,1H3,(H2,23,24) ZTDYHKPOGGEUGI-UHFFFAOYSA-N 618078 US20230286970, Compound 23 Histone deacetylase 4 Homo sapiens >30000 US Patent 10.7270/Q24T6PHD US20230286970 MARCHINI, M; VERGANI, B; SANDRONE, G; ROCCHIO, I; KACHKOVSKYI, G; CAPRINI, G; FOSSATI, G; STEINKÜHLER, C; STEVENAZZI, A ITALFARMACO S.P.A. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=618078 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=618078&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 162722734 484207244 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51496287 CC(C)(CNC(=O)c1cccc(c1)-c1noc(n1)C(F)(F)F)c1coc(n1)-c1ccccc1 InChI=1S/C23H19F3N4O3/c1-22(2,17-12-32-20(28-17)14-7-4-3-5-8-14)13-27-19(31)16-10-6-9-15(11-16)18-29-21(33-30-18)23(24,25)26/h3-12H,13H2,1-2H3,(H,27,31) QTCSXAUJBQZZSN-UHFFFAOYSA-N 50563276 CHEMBL4751615 Histone deacetylase 4 Homo sapiens 128 ChEMBL 10.7270/Q2WS8Z98 34875522 Turkman, N; Liu, D; Pirola, I Stony Brook University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50563276 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50563276&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 67324851 461683614 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51496288 C[C@H](CN(C)Cc1ccccc1)NC(=O)c1ccc(cc1)-c1noc(n1)C(F)(F)F InChI=1S/C21H21F3N4O2/c1-14(12-28(2)13-15-6-4-3-5-7-15)25-19(29)17-10-8-16(9-11-17)18-26-20(30-27-18)21(22,23)24/h3-11,14H,12-13H2,1-2H3,(H,25,29)/t14-/m1/s1 RESDVUQVZOJNSO-CQSZACIVSA-N 162865 US9056843, 156 Histone deacetylase 4 Homo sapiens 0.080000 ChEMBL 10.7270/Q2WS8Z98 34875522 Turkman, N; Liu, D; Pirola, I Stony Brook University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=162865 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=162865&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71230992 310304802 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51497358 ONC(=O)c1cnc(nc1)N1CCC(CC1)NC(=O)c1cnc(nc1O)-n1cccn1 InChI=1S/C18H19N9O4/c28-14(25-31)11-8-19-17(20-9-11)26-6-2-12(3-7-26)23-15(29)13-10-21-18(24-16(13)30)27-5-1-4-22-27/h1,4-5,8-10,12,31H,2-3,6-7H2,(H,23,29)(H,25,28)(H,21,24,30) WXBFFCPFJFYHFX-UHFFFAOYSA-N 50603205 CHEMBL5172182 Histone deacetylase 4 Homo sapiens 1171 ChEMBL 10.7270/Q22B9344 35033824 Wei, H; Gou, W; Gao, J; Ning, H; Song, Y; Li, D; Qin, Y; Hou, W; Li, Y Peking Union Medical College & Chinese Academy of Medical Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50603205 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50603205&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 163322228 482614056 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51497359 FC(F)(F)c1nc(no1)-c1cccc(c1)C(=O)NCC1(CCOCC1)c1nc(cs1)-c1ccccc1 InChI=1S/C25H21F3N4O3S/c26-25(27,28)22-31-20(32-35-22)17-7-4-8-18(13-17)21(33)29-15-24(9-11-34-12-10-24)23-30-19(14-36-23)16-5-2-1-3-6-16/h1-8,13-14H,9-12,15H2,(H,29,33) HORXBWNTEDOVKN-UHFFFAOYSA-N 50446481 CHEMBL3110004::US10011611, TMP269::US10722597, Compound TMP-269 Histone deacetylase 4 Homo sapiens 318 ChEMBL 10.7270/Q22B9344 35033824 Wei, H; Gou, W; Gao, J; Ning, H; Song, Y; Li, D; Qin, Y; Hou, W; Li, Y Peking Union Medical College & Chinese Academy of Medical Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446481 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446481&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search NU9 3ZNR 53344908 194944377 CHEMBL3110004 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51497474 CNc1nc(Cl)nc2n(Cc3ccc(cc3)C(=O)Nc3ccccc3N)cnc12 InChI=1S/C20H18ClN7O/c1-23-17-16-18(27-20(21)26-17)28(11-24-16)10-12-6-8-13(9-7-12)19(29)25-15-5-3-2-4-14(15)22/h2-9,11H,10,22H2,1H3,(H,25,29)(H,23,26,27) KWLQOVHDALHTOO-UHFFFAOYSA-N 50603230 CHEMBL5186622 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.7270/Q2P27363 35041998 Mao, PT; He, WB; Mai, X; Feng, LH; Li, N; Liao, YJ; Zhu, CS; Li, J; Chen, T; Liu, SH; Zhang, QM; He, L Nanchang University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50603230 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50603230&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 163215942 482614081 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51497475 CCNc1nc(Cl)nc2n(Cc3ccc(cc3)C(=O)Nc3ccccc3N)cnc12 InChI=1S/C21H20ClN7O/c1-2-24-18-17-19(28-21(22)27-18)29(12-25-17)11-13-7-9-14(10-8-13)20(30)26-16-6-4-3-5-15(16)23/h3-10,12H,2,11,23H2,1H3,(H,26,30)(H,24,27,28) NXPXTIKDUKRMJQ-UHFFFAOYSA-N 50603231 CHEMBL5178597 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.7270/Q2P27363 35041998 Mao, PT; He, WB; Mai, X; Feng, LH; Li, N; Liao, YJ; Zhu, CS; Li, J; Chen, T; Liu, SH; Zhang, QM; He, L Nanchang University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50603231 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50603231&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 163215934 482614082 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51497476 CCCNc1nc(Cl)nc2n(Cc3ccc(cc3)C(=O)Nc3ccccc3N)cnc12 InChI=1S/C22H22ClN7O/c1-2-11-25-19-18-20(29-22(23)28-19)30(13-26-18)12-14-7-9-15(10-8-14)21(31)27-17-6-4-3-5-16(17)24/h3-10,13H,2,11-12,24H2,1H3,(H,27,31)(H,25,28,29) FFKCJGZNWZGUOO-UHFFFAOYSA-N 50603232 CHEMBL5179973 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.7270/Q2P27363 35041998 Mao, PT; He, WB; Mai, X; Feng, LH; Li, N; Liao, YJ; Zhu, CS; Li, J; Chen, T; Liu, SH; Zhang, QM; He, L Nanchang University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50603232 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50603232&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 163215944 482614083 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51497477 CCCCNc1nc(Cl)nc2n(Cc3ccc(cc3)C(=O)Nc3ccccc3N)cnc12 InChI=1S/C23H24ClN7O/c1-2-3-12-26-20-19-21(30-23(24)29-20)31(14-27-19)13-15-8-10-16(11-9-15)22(32)28-18-7-5-4-6-17(18)25/h4-11,14H,2-3,12-13,25H2,1H3,(H,28,32)(H,26,29,30) UTSVDUQIDLMZLA-UHFFFAOYSA-N 50603233 CHEMBL5196817 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.7270/Q2P27363 35041998 Mao, PT; He, WB; Mai, X; Feng, LH; Li, N; Liao, YJ; Zhu, CS; Li, J; Chen, T; Liu, SH; Zhang, QM; He, L Nanchang University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50603233 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50603233&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 163215936 482614084 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51497478 C[C@H](\C=C(/C)\C=C\C(=O)NO)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1 RTKIYFITIVXBLE-QEQCGCAPSA-N 50005711 CHEBI:46024::GNF-Pf-1011::TRICHOSTATIN::Trichostatin A::Trichostatin A (TSA)::US10011611, Trichostatin A::US10722597, Compound Trichostatin::US11535598, Compound Trichostatin A::US9265734, TSA Histone deacetylase 4 Homo sapiens 4420 ChEMBL 10.7270/Q2P27363 35041998 Mao, PT; He, WB; Mai, X; Feng, LH; Li, N; Liao, YJ; Zhu, CS; Li, J; Chen, T; Liu, SH; Zhang, QM; He, L Nanchang University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,3F0R,5G0G,5D1B,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 444732 242056952 DB04297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51497484 Nc1ccccc1NC(=O)c1ccc(CNC(=O)OCc2cccnc2)cc1 InChI=1S/C21H20N4O3/c22-18-5-1-2-6-19(18)25-20(26)17-9-7-15(8-10-17)13-24-21(27)28-14-16-4-3-11-23-12-16/h1-12H,13-14,22H2,(H,24,27)(H,25,26) INVTYAOGFAGBOE-UHFFFAOYSA-N 19410 CHEMBL27759::MS-275::US11377423, MS-275::US11672788, Compound Entinostat::US9265734, MS-275::US9796664, Compound MS-275::benzamide-type inhibitor, 3::pyridin-3-ylmethyl N-({4-[(2-aminophenyl)carbamoyl]phenyl}methyl)carbamate Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.7270/Q2P27363 35041998 Mao, PT; He, WB; Mai, X; Feng, LH; Li, N; Liao, YJ; Zhu, CS; Li, J; Chen, T; Liu, SH; Zhang, QM; He, L Nanchang University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19410 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19410&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4261 46519433 CHEMBL27759 7007 ZINC01488870 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51497485 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.7270/Q2P27363 35041998 Mao, PT; He, WB; Mai, X; Feng, LH; Li, N; Liao, YJ; Zhu, CS; Li, J; Chen, T; Liu, SH; Zhang, QM; He, L Nanchang University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51505011 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.7270/Q2XP791Q 33077264 Bass, AKA; El-Zoghbi, MS; Nageeb, EM; Mohamed, MFA; Badr, M; Abuo-Rahma, GEA Menoufia University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51505012 ONC(=O)CCCCCOc1no[n+]([O-])c1S(=O)(=O)c1ccccc1 InChI=1S/C14H17N3O7S/c18-12(15-19)9-5-2-6-10-23-13-14(17(20)24-16-13)25(21,22)11-7-3-1-4-8-11/h1,3-4,7-8,19H,2,5-6,9-10H2,(H,15,18) AGDGTFUFKSHWRN-UHFFFAOYSA-N 50087853 CHEMBL3426906 Histone deacetylase 4 Homo sapiens 30000 ChEMBL 10.7270/Q2XP791Q 33077264 Bass, AKA; El-Zoghbi, MS; Nageeb, EM; Mohamed, MFA; Badr, M; Abuo-Rahma, GEA Menoufia University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50087853 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50087853&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118737455 103986881 CHEMBL3426906 ZINC29479440 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51505013 Cc1cc(C(=O)NCc2c(C)cc(C)[nH]c2=O)c(C)n1-c1cccc(NC(=O)CCCCCCC(=O)NO)c1 InChI=1S/C29H37N5O5/c1-18-14-19(2)31-29(38)25(18)17-30-28(37)24-15-20(3)34(21(24)4)23-11-9-10-22(16-23)32-26(35)12-7-5-6-8-13-27(36)33-39/h9-11,14-16,39H,5-8,12-13,17H2,1-4H3,(H,30,37)(H,31,38)(H,32,35)(H,33,36) HQAHZUWVVKNTRB-UHFFFAOYSA-N 50540803 CHEMBL4633299 Histone deacetylase 4 Homo sapiens 36800 ChEMBL 10.7270/Q2XP791Q 33077264 Bass, AKA; El-Zoghbi, MS; Nageeb, EM; Mohamed, MFA; Badr, M; Abuo-Rahma, GEA Menoufia University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50540803 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50540803&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 156010365 442142366 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51495002 COc1ccc(Cn2ccc3cc(ccc23)C(=O)NO)cc1 InChI=1S/C17H16N2O3/c1-22-15-5-2-12(3-6-15)11-19-9-8-13-10-14(17(20)18-21)4-7-16(13)19/h2-10,21H,11H2,1H3,(H,18,20) BQOSUTIJKDOCIO-UHFFFAOYSA-N 50602213 CHEMBL5203725 Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.7270/Q2959NMG 36449385 Sun, P; Wang, J; Khan, KS; Yang, W; Ng, BW; Ilment, N; Zessin, M; Bülbül, EF; Robaa, D; Erdmann, F; Schmidt, M; Romier, C; Schutkowski, M; Cheng, AS; Sippl, W Martin-Luther University of Halle-Wittenberg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50602213 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50602213&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168293537 482613064 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51495003 CCCNNC(=O)c1ccc(cc1)-c1ccc(CNC(C)=O)cc1 InChI=1S/C19H23N3O2/c1-3-12-21-22-19(24)18-10-8-17(9-11-18)16-6-4-15(5-7-16)13-20-14(2)23/h4-11,21H,3,12-13H2,1-2H3,(H,20,23)(H,22,24) QASVOZNRTMBUBO-UHFFFAOYSA-N 50602189 CHEMBL5194907 Histone deacetylase 4 Homo sapiens 990 ChEMBL 10.7270/Q2959NMG 36449385 Sun, P; Wang, J; Khan, KS; Yang, W; Ng, BW; Ilment, N; Zessin, M; Bülbül, EF; Robaa, D; Erdmann, F; Schmidt, M; Romier, C; Schutkowski, M; Cheng, AS; Sippl, W Martin-Luther University of Halle-Wittenberg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50602189 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50602189&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168285410 482613040 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51495004 CCCCCCNNC(=O)c1ccc(cc1)-c1ccc(CNC(C)=O)cc1 InChI=1S/C22H29N3O2/c1-3-4-5-6-15-24-25-22(27)21-13-11-20(12-14-21)19-9-7-18(8-10-19)16-23-17(2)26/h7-14,24H,3-6,15-16H2,1-2H3,(H,23,26)(H,25,27) TYHZHMRYNRDNRX-UHFFFAOYSA-N 50602192 CHEMBL5174998 Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.7270/Q2959NMG 36449385 Sun, P; Wang, J; Khan, KS; Yang, W; Ng, BW; Ilment, N; Zessin, M; Bülbül, EF; Robaa, D; Erdmann, F; Schmidt, M; Romier, C; Schutkowski, M; Cheng, AS; Sippl, W Martin-Luther University of Halle-Wittenberg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50602192 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50602192&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168273030 482613043 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51495005 CCCCCCNNC(=O)c1cccc(NCc2ccccc2)c1 InChI=1S/C20H27N3O/c1-2-3-4-8-14-22-23-20(24)18-12-9-13-19(15-18)21-16-17-10-6-5-7-11-17/h5-7,9-13,15,21-22H,2-4,8,14,16H2,1H3,(H,23,24) AMGYYKOEOSUCFG-UHFFFAOYSA-N 50602195 CHEMBL5206011 Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.7270/Q2959NMG 36449385 Sun, P; Wang, J; Khan, KS; Yang, W; Ng, BW; Ilment, N; Zessin, M; Bülbül, EF; Robaa, D; Erdmann, F; Schmidt, M; Romier, C; Schutkowski, M; Cheng, AS; Sippl, W Martin-Luther University of Halle-Wittenberg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50602195 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50602195&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168296502 482613046 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51495006 CCCNNC(=O)c1cnc(NCc2ccccc2)nc1 InChI=1S/C15H19N5O/c1-2-8-19-20-14(21)13-10-17-15(18-11-13)16-9-12-6-4-3-5-7-12/h3-7,10-11,19H,2,8-9H2,1H3,(H,20,21)(H,16,17,18) ZNFWUEMVXRQJAR-UHFFFAOYSA-N 50602196 CHEMBL5171850 Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.7270/Q2959NMG 36449385 Sun, P; Wang, J; Khan, KS; Yang, W; Ng, BW; Ilment, N; Zessin, M; Bülbül, EF; Robaa, D; Erdmann, F; Schmidt, M; Romier, C; Schutkowski, M; Cheng, AS; Sippl, W Martin-Luther University of Halle-Wittenberg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50602196 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50602196&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168270492 482613047 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51495007 CCCNNC(=O)c1cnc(nc1)N1CCN(Cc2c[nH]c3ccccc23)CC1 InChI=1S/C21H27N7O/c1-2-7-25-26-20(29)16-12-23-21(24-13-16)28-10-8-27(9-11-28)15-17-14-22-19-6-4-3-5-18(17)19/h3-6,12-14,22,25H,2,7-11,15H2,1H3,(H,26,29) MAEKVVCEBJELGT-UHFFFAOYSA-N 50602203 CHEMBL5171086 Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.7270/Q2959NMG 36449385 Sun, P; Wang, J; Khan, KS; Yang, W; Ng, BW; Ilment, N; Zessin, M; Bülbül, EF; Robaa, D; Erdmann, F; Schmidt, M; Romier, C; Schutkowski, M; Cheng, AS; Sippl, W Martin-Luther University of Halle-Wittenberg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50602203 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50602203&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168270171 482613054 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51495008 CCCCCCNNC(=O)c1cnc(nc1)N1CCN(Cc2c[nH]c3ccccc23)CC1 InChI=1S/C24H33N7O/c1-2-3-4-7-10-28-29-23(32)19-15-26-24(27-16-19)31-13-11-30(12-14-31)18-20-17-25-22-9-6-5-8-21(20)22/h5-6,8-9,15-17,25,28H,2-4,7,10-14,18H2,1H3,(H,29,32) MMZYGJCCLIZGBV-UHFFFAOYSA-N 50602204 CHEMBL5195676 Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.7270/Q2959NMG 36449385 Sun, P; Wang, J; Khan, KS; Yang, W; Ng, BW; Ilment, N; Zessin, M; Bülbül, EF; Robaa, D; Erdmann, F; Schmidt, M; Romier, C; Schutkowski, M; Cheng, AS; Sippl, W Martin-Luther University of Halle-Wittenberg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50602204 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50602204&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 168287165 482613055 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51493983 COc1cccc2n(C)c(=O)c(C(=O)N(C)c3ccc(cc3)C(F)(F)F)c(O)c12 InChI=1S/C20H17F3N2O4/c1-24(12-9-7-11(8-10-12)20(21,22)23)18(27)16-17(26)15-13(25(2)19(16)28)5-4-6-14(15)29-3/h4-10,26H,1-3H3 ONDYALNGTUAJDX-UHFFFAOYSA-N 50565139 Tasquinimod Histone deacetylase 4 Homo sapiens 10.0 ChEMBL 10.7270/Q2PK0M78 34624823 Hou, R; He, Y; Yan, G; Hou, S; Xie, Z; Liao, C Hefei University of Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50565139 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50565139&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 54682876 461685477 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51498076 ONC(=O)c1ccc(CN(C2CC2)S(=O)(=O)c2cc(F)c(F)c(F)c2F)cc1 InChI=1S/C17H14F4N2O4S/c18-12-7-13(15(20)16(21)14(12)19)28(26,27)23(11-5-6-11)8-9-1-3-10(4-2-9)17(24)22-25/h1-4,7,11,25H,5-6,8H2,(H,22,24) HYEWQOQZANKATO-UHFFFAOYSA-N 50595960 CHEMBL5192865 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.7270/Q2QV3RKM 35119267 Nawar, N; Bukhari, S; Adile, AA; Suk, Y; Manaswiyoungkul, P; Toutah, K; Olaoye, OO; Raouf, YS; Sedighi, A; Garcha, HK; Hassan, MM; Gwynne, W; Israelian, J; Radu, TB; Geletu, M; Abdeldayem, A; Gawel, JM; Cabral, AD; Venugopal, C; de Araujo, ED; Singh, SK; Gunning, PT University of Toronto Mississauga http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50595960 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50595960&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155155639 482606812 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51498077 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1Cl InChI=1S/C24H26ClN5O3/c25-20-12-7-8-13-21(20)30(19-10-4-3-5-11-19)24-27-16-18(17-28-24)23(32)26-15-9-2-1-6-14-22(31)29-33/h3-5,7-8,10-13,16-17,33H,1-2,6,9,14-15H2,(H,26,32)(H,29,31) VLIUIBXPEDFJRF-UHFFFAOYSA-N 110036 US8609678, 2-((2-chlorophenyl)(phenyl)amino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [89] Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.7270/Q2QV3RKM 35119267 Nawar, N; Bukhari, S; Adile, AA; Suk, Y; Manaswiyoungkul, P; Toutah, K; Olaoye, OO; Raouf, YS; Sedighi, A; Garcha, HK; Hassan, MM; Gwynne, W; Israelian, J; Radu, TB; Geletu, M; Abdeldayem, A; Gawel, JM; Cabral, AD; Venugopal, C; de Araujo, ED; Singh, SK; Gunning, PT University of Toronto Mississauga http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=110036 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=110036&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 53340426 186526906 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51498078 CC(C)N(Cc1ccc(cc1)C(=O)NO)S(=O)(=O)c1cc(F)c(F)c(F)c1F InChI=1S/C17H16F4N2O4S/c1-9(2)23(8-10-3-5-11(6-4-10)17(24)22-25)28(26,27)13-7-12(18)14(19)16(21)15(13)20/h3-7,9,25H,8H2,1-2H3,(H,22,24) SJWJGLIJTRUXIZ-UHFFFAOYSA-N 50603512 CHEMBL5177475 Histone deacetylase 4 Homo sapiens >4000 ChEMBL 10.7270/Q2QV3RKM 35119267 Nawar, N; Bukhari, S; Adile, AA; Suk, Y; Manaswiyoungkul, P; Toutah, K; Olaoye, OO; Raouf, YS; Sedighi, A; Garcha, HK; Hassan, MM; Gwynne, W; Israelian, J; Radu, TB; Geletu, M; Abdeldayem, A; Gawel, JM; Cabral, AD; Venugopal, C; de Araujo, ED; Singh, SK; Gunning, PT University of Toronto Mississauga http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50603512 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50603512&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search O2L 155699554 482614363 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51514179 Oc1cc2O\C(=C/c3ccc(O)c(O)c3)C(=O)c2c(O)c1 InChI=1S/C15H10O6/c16-8-5-11(19)14-12(6-8)21-13(15(14)20)4-7-1-2-9(17)10(18)3-7/h1-6,16-19H/b13-4- WBEFUVAYFSOUEA-PQMHYQBVSA-N 50439491 AUREUSIDIN Histone deacetylase 4 Homo sapiens 800 ChEMBL 10.7270/Q2QR52BX 36126323 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50439491 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50439491&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5281220 175451808 18149 C08576 ZINC00897612 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51513096 COc1ccc(cc1)-c1nc(cc2c3ccccc3[nH]c12)C(=O)NCc1ccc(cc1)C(=O)NO InChI=1S/C27H22N4O4/c1-35-19-12-10-17(11-13-19)24-25-21(20-4-2-3-5-22(20)29-25)14-23(30-24)27(33)28-15-16-6-8-18(9-7-16)26(32)31-34/h2-14,29,34H,15H2,1H3,(H,28,33)(H,31,32) UZUJYNLQQVVLGQ-UHFFFAOYSA-N 50608961 CHEMBL5275259 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.7270/Q2GF0ZQF 33528252 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50608961 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50608961&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 171353942 494498709 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51521521 COc1ccc(NC(=O)CCCCCCNC(=O)C(O)(O)C(F)(F)F)cc1 InChI=1S/C17H23F3N2O5/c1-27-13-9-7-12(8-10-13)22-14(23)6-4-2-3-5-11-21-15(24)16(25,26)17(18,19)20/h7-10,25-26H,2-6,11H2,1H3,(H,21,24)(H,22,23) QYAUSNMYLJZYSM-UHFFFAOYSA-N 50612575 CHEMBL5266902 Histone deacetylase 4 Homo sapiens 1600000 ChEMBL 10.7270/Q25X2F69 36244186 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50612575 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50612575&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 171349274 494502323 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51521522 OC(O)(C(=O)NCCCCCCC(=O)Nc1ncc(s1)-c1ccccc1)C(F)(F)F InChI=1S/C19H22F3N3O4S/c20-19(21,22)18(28,29)16(27)23-11-7-2-1-6-10-15(26)25-17-24-12-14(30-17)13-8-4-3-5-9-13/h3-5,8-9,12,28-29H,1-2,6-7,10-11H2,(H,23,27)(H,24,25,26) HMBQXLWLFWBPTA-UHFFFAOYSA-N 50612576 CHEMBL5272159 Histone deacetylase 4 Homo sapiens 2500000 ChEMBL 10.7270/Q25X2F69 36244186 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50612576 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50612576&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 171342760 494502324 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51521523 OC(O)(C(=O)NCCCCCCC(=O)Nc1nc2ccccc2s1)C(F)(F)F InChI=1S/C17H20F3N3O4S/c18-17(19,20)16(26,27)14(25)21-10-6-2-1-3-9-13(24)23-15-22-11-7-4-5-8-12(11)28-15/h4-5,7-8,26-27H,1-3,6,9-10H2,(H,21,25)(H,22,23,24) VCBKMQANWHYGLM-UHFFFAOYSA-N 50612577 CHEMBL5267343 Histone deacetylase 4 Homo sapiens 430000 ChEMBL 10.7270/Q25X2F69 36244186 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50612577 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50612577&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 171350058 494502325 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51521524 COc1ccc2sc(NC(=O)CCCCCCNC(=O)C(O)(O)C(F)(F)F)nc2c1 InChI=1S/C18H22F3N3O5S/c1-29-11-7-8-13-12(10-11)23-16(30-13)24-14(25)6-4-2-3-5-9-22-15(26)17(27,28)18(19,20)21/h7-8,10,27-28H,2-6,9H2,1H3,(H,22,26)(H,23,24,25) DBJGGOAPOFCPMT-UHFFFAOYSA-N 50612578 CHEMBL5281058 Histone deacetylase 4 Homo sapiens 1900000 ChEMBL 10.7270/Q25X2F69 36244186 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50612578 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50612578&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 171356047 494502326 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51521525 Oc1ccc(cc1)-c1cnc(NC(=O)CCCCCCNC(=O)C(O)(O)C(F)(F)F)s1 InChI=1S/C19H22F3N3O5S/c20-19(21,22)18(29,30)16(28)23-10-4-2-1-3-5-15(27)25-17-24-11-14(31-17)12-6-8-13(26)9-7-12/h6-9,11,26,29-30H,1-5,10H2,(H,23,28)(H,24,25,27) CXOZDYPHTOUBCX-UHFFFAOYSA-N 50612579 CHEMBL5278407 Histone deacetylase 4 Homo sapiens 2300000 ChEMBL 10.7270/Q25X2F69 36244186 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50612579 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50612579&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 171354881 494502327 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51521526 OC(O)(C(=O)NCCCCCCC(=O)Nc1ccc(Cl)cc1)C(F)(F)F InChI=1S/C16H20ClF3N2O4/c17-11-6-8-12(9-7-11)22-13(23)5-3-1-2-4-10-21-14(24)15(25,26)16(18,19)20/h6-9,25-26H,1-5,10H2,(H,21,24)(H,22,23) ZVDUSHBFRJPLNJ-UHFFFAOYSA-N 50612580 CHEMBL5269393 Histone deacetylase 4 Homo sapiens 2700000 ChEMBL 10.7270/Q25X2F69 36244186 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50612580 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50612580&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 171342273 494502328 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51521527 OC(O)(C(=O)NCCCCCCC(=O)Nc1ccc(Br)cc1)C(F)(F)F InChI=1S/C16H20BrF3N2O4/c17-11-6-8-12(9-7-11)22-13(23)5-3-1-2-4-10-21-14(24)15(25,26)16(18,19)20/h6-9,25-26H,1-5,10H2,(H,21,24)(H,22,23) LGDVXYJRPBFZAJ-UHFFFAOYSA-N 50612581 CHEMBL5270636 Histone deacetylase 4 Homo sapiens 2600000 ChEMBL 10.7270/Q25X2F69 36244186 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50612581 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50612581&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 171344163 494502329 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51521528 OC(O)(C(=O)NCCCCCCC(=O)Nc1ccc(cc1)-c1ccccc1)C(F)(F)F InChI=1S/C22H25F3N2O4/c23-22(24,25)21(30,31)20(29)26-15-7-2-1-6-10-19(28)27-18-13-11-17(12-14-18)16-8-4-3-5-9-16/h3-5,8-9,11-14,30-31H,1-2,6-7,10,15H2,(H,26,29)(H,27,28) ALWAFPQKUFSFNP-UHFFFAOYSA-N 50612582 CHEMBL5280772 Histone deacetylase 4 Homo sapiens 1100000 ChEMBL 10.7270/Q25X2F69 36244186 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50612582 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50612582&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 171357084 494502330 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51521529 COc1ccc(cc1)-c1cnc(NC(=O)CCCCCCNC(=O)C(O)(O)C(F)(F)F)s1 InChI=1S/C20H24F3N3O5S/c1-31-14-9-7-13(8-10-14)15-12-25-18(32-15)26-16(27)6-4-2-3-5-11-24-17(28)19(29,30)20(21,22)23/h7-10,12,29-30H,2-6,11H2,1H3,(H,24,28)(H,25,26,27) LBYUKUIOYGHLJO-UHFFFAOYSA-N 50612583 CHEMBL5269265 Histone deacetylase 4 Homo sapiens 2500000 ChEMBL 10.7270/Q25X2F69 36244186 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50612583 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50612583&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 171342508 494502331 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51521530 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 12000000 ChEMBL 10.7270/Q25X2F69 36244186 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51521531 OC(O)(C(=O)NCCCCCCC(=O)Nc1ncc(s1)-c1ccc(Br)cc1)C(F)(F)F InChI=1S/C19H21BrF3N3O4S/c20-13-8-6-12(7-9-13)14-11-25-17(31-14)26-15(27)5-3-1-2-4-10-24-16(28)18(29,30)19(21,22)23/h6-9,11,29-30H,1-5,10H2,(H,24,28)(H,25,26,27) XFFMCHUCKPYGQZ-UHFFFAOYSA-N 50612584 CHEMBL5280060 Histone deacetylase 4 Homo sapiens 1700000 ChEMBL 10.7270/Q25X2F69 36244186 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50612584 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50612584&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 171352366 494502332 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51508890 COc1cc(Cc2cnc(N)nc2N)cc2C(C)CCN(CCO)c12 InChI=1S/C18H25N5O2/c1-11-3-4-23(5-6-24)16-14(11)8-12(9-15(16)25-2)7-13-10-21-18(20)22-17(13)19/h8-11,24H,3-7H2,1-2H3,(H4,19,20,21,22) IZJHXNMVMRCLAW-UHFFFAOYSA-N 50421842 CHEMBL5268638 Histone deacetylase 4 Homo sapiens 5620 ChEMBL 10.7270/Q2V98D82 31865013 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50421842 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50421842&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44300858 164150717 CHEMBL58074 ZINC29569380 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51509102 O=C(C[N+]12CCC(CC1)[C@H](C2)OC(=O)C1(CCCCCC1)C1=CC=CC1)Nc1ccccn1 InChI=1S/C27H35N3O3/c31-25(29-24-11-5-8-16-28-24)20-30-17-12-21(13-18-30)23(19-30)33-26(32)27(22-9-3-4-10-22)14-6-1-2-7-15-27/h3-5,8-9,11,16,21,23H,1-2,6-7,10,12-15,17-20H2/p+1/t21?,23-,30?/m0/s1 UYYIYNBXGLEYLK-WITHESGTSA-O 50443271 CHEMBL5277234 Histone deacetylase 4 Homo sapiens 5.0 ChEMBL 10.7270/Q22V2MBJ 32688198 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50443271 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50443271&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 72546496 194941167 CHEMBL3087362 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51525020 CN(CCc1ccccc1)S(=O)(=O)c1cccc(\C=C\C(=O)NO)c1 InChI=1S/C18H20N2O4S/c1-20(13-12-15-6-3-2-4-7-15)25(23,24)17-9-5-8-16(14-17)10-11-18(21)19-22/h2-11,14,22H,12-13H2,1H3,(H,19,21)/b11-10+ VLCXJLKMJMKPJC-ZHACJKMWSA-N 323702 US10188756, Compound CN89 Histone deacetylase 4 Homo sapiens 500 ChEMBL 10.7270/Q2NK3K9K 27318122 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=323702 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=323702&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 122548372 384578781 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51525021 CCN(Cc1ccc(\C=C\C(=O)NO)o1)Cc1ccccc1 InChI=1S/C17H20N2O3/c1-2-19(12-14-6-4-3-5-7-14)13-16-9-8-15(22-16)10-11-17(20)18-21/h3-11,21H,2,12-13H2,1H3,(H,18,20)/b11-10+ YSHAULCJPNNZNY-ZHACJKMWSA-N 50492835 CHEMBL2413316 Histone deacetylase 4 Homo sapiens 10730 ChEMBL 10.7270/Q2NK3K9K 27318122 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50492835 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50492835&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 71769925 433960100 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51525022 CN(C)c1cccc2c(SNCCCCCC(=O)NO)cccc12 InChI=1S/C18H25N3O2S/c1-21(2)16-10-6-9-15-14(16)8-7-11-17(15)24-19-13-5-3-4-12-18(22)20-23/h6-11,19,23H,3-5,12-13H2,1-2H3,(H,20,22) IOJSHUPVMUJFRE-UHFFFAOYSA-N 50613613 CHEMBL5271192 Histone deacetylase 4 Homo sapiens 670 ChEMBL 10.7270/Q2NK3K9K 27318122 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50613613 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50613613&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 171342559 494503361 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51525023 CC(=O)Nc1ccc(cc1)C(=O)CSc1nc(C)cc(=O)[nH]1 InChI=1S/C15H15N3O3S/c1-9-7-14(21)18-15(16-9)22-8-13(20)11-3-5-12(6-4-11)17-10(2)19/h3-7H,8H2,1-2H3,(H,17,19)(H,16,18,21) NZVOKXQPGIDGBV-UHFFFAOYSA-N 50348388 CHEMBL1800241 Histone deacetylase 4 Homo sapiens 32500 ChEMBL 10.7270/Q2NK3K9K 27318122 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50348388 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50348388&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 784998 136355074 CHEMBL1800241 ZINC18155397 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51525024 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 1600 ChEMBL 10.7270/Q2NK3K9K 27318122 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51525025 OCc1ccc(cc1)[C@@H]1C[C@H](CSc2nc(c(o2)-c2ccccc2)-c2ccccc2)O[C@@H](O1)c1ccc(NC(=O)CCCCCCC(=O)NO)cc1 InChI=1S/C41H43N3O7S/c45-26-28-17-19-29(20-18-28)35-25-34(27-52-41-43-38(30-11-5-3-6-12-30)39(51-41)31-13-7-4-8-14-31)49-40(50-35)32-21-23-33(24-22-32)42-36(46)15-9-1-2-10-16-37(47)44-48/h3-8,11-14,17-24,34-35,40,45,48H,1-2,9-10,15-16,25-27H2,(H,42,46)(H,44,47)/t34-,35+,40+/m1/s1 BHUZLJOUHMBZQY-YXQOSMAKSA-N 22449 CHEMBL356769::N-(4-{(2R,4R,6S)-4-{[(4,5-diphenyl-1,3-oxazol-2-yl)sulfanyl]methyl}-6-[4-(hydroxymethyl)phenyl]-1,3-dioxan-2-yl}phenyl)-N -hydroxyoctanediamide::Tubacin::US9249087, Tubastatin A Histone deacetylase 4 Homo sapiens 17300 ChEMBL 10.7270/Q2NK3K9K 27318122 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=22449 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=22449&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 6675804 49846263 CHEMBL356769 7374 ZINC27551136 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51525026 OCCN(C(=O)Cc1ccc(cc1)C(=O)NO)c1ccccc1 InChI=1S/C17H18N2O4/c20-11-10-19(15-4-2-1-3-5-15)16(21)12-13-6-8-14(9-7-13)17(22)18-23/h1-9,20,23H,10-12H2,(H,18,22) RFAZNTABYJYOAR-UHFFFAOYSA-N 198121 HPOB Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.7270/Q2NK3K9K 27318122 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=198121 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=198121&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5OJ 5EF7 71532921 318489194 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51525027 CN1CCc2c(C1)c1ccccc1n2Cc1ccc(cc1)C(=O)NO InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::Tubastatin A::US10227295, Compound Tubastatin A::US10456394, Tubastatin A::US11207431, Example D::US8748451, 6::US9249087, Tubacin::US9751832, Tubastatin A::US9956192, Compound Tubastatin-A Histone deacetylase 4 Homo sapiens >30000 ChEMBL 10.7270/Q2NK3K9K 27318122 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 ZINC51951670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51525028 Cn1cc(CCNCc2ccc(\C=C\C(=O)NO)cc2)c2ccccc12 InChI=1S/C21H23N3O2/c1-24-15-18(19-4-2-3-5-20(19)24)12-13-22-14-17-8-6-16(7-9-17)10-11-21(25)23-26/h2-11,15,22,26H,12-14H2,1H3,(H,23,25)/b11-10+ AEDUBEGTPWKDCX-ZHACJKMWSA-N 323704 US10188756, Compound CN107 Histone deacetylase 4 Homo sapiens 655 ChEMBL 10.7270/Q2NK3K9K 27318122 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=323704 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=323704&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11024529 384578783 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51527956 ONC(=O)CCCCCCNc1nc2ccccc2nc1-c1nc2ccccc2o1 InChI=1S/C22H23N5O3/c28-19(27-29)13-3-1-2-8-14-23-21-20(24-15-9-4-5-10-16(15)25-21)22-26-17-11-6-7-12-18(17)30-22/h4-7,9-12,29H,1-3,8,13-14H2,(H,23,25)(H,27,28) UPTYYNWPPBPUMA-UHFFFAOYSA-N 50614780 CHEMBL5269112 Histone deacetylase 4 Homo sapiens 15 ChEMBL 10.7270/Q2183BTQ 37116762 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50614780 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50614780&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 171344205 494504528 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51527957 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 18 ChEMBL 10.7270/Q2183BTQ 37116762 Yang, Y; Liu, Q; Wang, X; Gou, S Southeast University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50988906 ONC(=O)[C@@H]1[C@@H]([C@H]1c1ccc(cc1)-c1cnco1)c1ccccc1 InChI=1S/C19H16N2O3/c22-19(21-23)18-16(13-4-2-1-3-5-13)17(18)14-8-6-12(7-9-14)15-10-20-11-24-15/h1-11,16-18,23H,(H,21,22)/t16-,17-,18-/m1/s1 PYWCXCBMYMFPTR-KZNAEPCWSA-N 50446472 CHEMBL3110021::US9765054, Compound 41B Histone deacetylase 4 Homo sapiens 200 ChEMBL 10.7270/Q28056T7 36490325 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446472 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446472&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search KEE 4CBY 60148693 194944368 CHEMBL3110021 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50988907 ONC(=O)[C@]1(F)[C@@H]([C@H]1c1ccc(cc1)-c1ncc(F)cn1)c1ccccc1 InChI=1S/C20H15F2N3O2/c21-15-10-23-18(24-11-15)14-8-6-13(7-9-14)17-16(12-4-2-1-3-5-12)20(17,22)19(26)25-27/h1-11,16-17,27H,(H,25,26)/t16-,17-,20+/m1/s1 MREATSZIGJDNKB-HLIPFELVSA-N 50160879 CHEMBL3793392::US9505736, (1S,2S,3S)-1-Fluoro-2-(4-(5- fluoropyrimidin-2-yl)phenyl)-N-hydroxy-3- phenylcyclopropanecarboxamide Histone deacetylase 4 Homo sapiens 100 ChEMBL 10.7270/Q28056T7 36490325 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50160879 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50160879&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search OTF 5A2S 72722126 340134793 CHEMBL3793392 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50988908 O[C@H](COCc1ccccc1)[C@H]1CCCCN1 InChI=1S/C14H21NO2/c16-14(13-8-4-5-9-15-13)11-17-10-12-6-2-1-3-7-12/h1-3,6-7,13-16H,4-5,8-11H2/t13-,14-/m1/s1 DCJOWWMUIMVZHV-ZIAGYGMSSA-N 50405617 CHEMBL5269131 Histone deacetylase 4 Homo sapiens 54 ChEMBL 10.7270/Q28056T7 36490325 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50405617 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50405617&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 14201547 163354641 CHEMBL66702 ZINC26263749 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50988909 CC(C)NCC(O)COCCCc1ccccc1 InChI=1S/C15H25NO2/c1-13(2)16-11-15(17)12-18-10-6-9-14-7-4-3-5-8-14/h3-5,7-8,13,15-17H,6,9-12H2,1-2H3 ABSFOXWUNVUMLQ-UHFFFAOYSA-N 50405618 CHEMBL5286810 Histone deacetylase 4 Homo sapiens 40 ChEMBL 10.7270/Q28056T7 36490325 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50405618 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50405618&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 12797747 163354642 CHEMBL66449 ZINC26260307 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50989460 CN1CCc2c(C1)c1ccccc1n2Cc1ccc(cc1)C(=O)NO InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::Tubastatin A::US10227295, Compound Tubastatin A::US10456394, Tubastatin A::US11207431, Example D::US8748451, 6::US9249087, Tubacin::US9751832, Tubastatin A::US9956192, Compound Tubastatin-A Histone deacetylase 4 Homo sapiens 4270 ChEMBL 10.7270/Q2M90DVG 36645952 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 ZINC51951670 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50989461 Clc1ccc(CNCCCCCCNCCCCCCCCNCCCCCCNCc2ccc(Cl)cc2)cc1 InChI=1S/C34H56Cl2N4/c35-33-19-15-31(16-20-33)29-39-27-13-7-5-11-25-37-23-9-3-1-2-4-10-24-38-26-12-6-8-14-28-40-30-32-17-21-34(36)22-18-32/h15-22,37-40H,1-14,23-30H2 RKXRKRPDZVBZTI-UHFFFAOYSA-N 50405753 CHEMBL5274634 Histone deacetylase 4 Homo sapiens 4040 ChEMBL 10.7270/Q2M90DVG 36645952 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50405753 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50405753&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 44380612 163354777 CHEMBL170113 ZINC27980924 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50993398 Cc1[nH]c2ccccc2c1CCNCc1ccc(\C=C\C(=O)NO)cc1 InChI=1S/C21H23N3O2/c1-15-18(19-4-2-3-5-20(19)23-15)12-13-22-14-17-8-6-16(7-9-17)10-11-21(25)24-26/h2-11,22-23,26H,12-14H2,1H3,(H,24,25)/b11-10+ FPOHNWQLNRZRFC-ZHACJKMWSA-N 29589 Faridak::LBH-589::LBH-589B::Panobinostat::US10722597, Compound Panobinostat Histone deacetylase 4 Homo sapiens 203 ChEMBL 10.7270/Q27S7SZF 33035922 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=29589 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=29589&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search LBH 5EF8 6918837 81055018 ZINC22010649 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50993399 ONC(=O)\C=C\c1cccc(c1)S(=O)(=O)Nc1ccccc1 InChI=1S/C15H14N2O4S/c18-15(16-19)10-9-12-5-4-8-14(11-12)22(20,21)17-13-6-2-1-3-7-13/h1-11,17,19H,(H,16,18)/b10-9+ NCNRHFGMJRPRSK-MDZDMXLPSA-N 25150 (2E)-N-hydroxy-3-[3-(phenylsulfamoyl)phenyl]prop-2-enamide::Belinosta::Belinostat::PXD-101::PXD101 Histone deacetylase 4 Homo sapiens 1236 ChEMBL 10.7270/Q27S7SZF 33035922 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25150 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25150&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 5OG 5EEN 6918638 56374291 61076 ZINC03818726 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50993400 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 15056 ChEMBL 10.7270/Q27S7SZF 33035922 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50993401 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1 InChI=1S/C24H27N5O3/c30-22(28-32)15-9-1-2-10-16-25-23(31)19-17-26-24(27-18-19)29(20-11-5-3-6-12-20)21-13-7-4-8-14-21/h3-8,11-14,17-18,32H,1-2,9-10,15-16H2,(H,25,31)(H,28,30) QGZYDVAGYRLSKP-UHFFFAOYSA-N 50439674 RICOLINOSTAT::US10858323, Compound 2::US11207431, Example E::US20230414581, Compound 43::US8609678, 2-(diphenylamino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [26] Histone deacetylase 4 Homo sapiens 7000 ChEMBL 10.7270/Q27S7SZF 33035922 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50439674 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50439674&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search AH4 5WGL 53340666 175451991 ZINC89630354 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50993402 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1Cl InChI=1S/C24H26ClN5O3/c25-20-12-7-8-13-21(20)30(19-10-4-3-5-11-19)24-27-16-18(17-28-24)23(32)26-15-9-2-1-6-14-22(31)29-33/h3-5,7-8,10-13,16-17,33H,1-2,6,9,14-15H2,(H,26,32)(H,29,31) VLIUIBXPEDFJRF-UHFFFAOYSA-N 110036 US8609678, 2-((2-chlorophenyl)(phenyl)amino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [89] Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.7270/Q27S7SZF 33035922 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=110036 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=110036&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search X4U 8SZU 53340426 186526906 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 50994417 Nc1ccc(F)cc1NC(=O)c1ccc(CNC(=O)\C=C\c2cccnc2)cc1 InChI=1S/C22H19FN4O2/c23-18-8-9-19(24)20(12-18)27-22(29)17-6-3-16(4-7-17)14-26-21(28)10-5-15-2-1-11-25-13-15/h1-13H,14,24H2,(H,26,28)(H,27,29)/b10-5+ WXHHICFWKXDFOW-BJMVGYQFSA-N 50242817 CHEMBL4087968 Histone deacetylase 4 Homo sapiens >30000 ChEMBL 10.7270/Q27S7SZF 33035922 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50242817 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50242817&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 9800555 104099245 CHEMBL4087968 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51521272 CNC(=O)CCCCC[C@H](NC(=O)Cn1ccc2cc(ccc12)C#N)c1ncc([nH]1)-c1ccc(CN(C)C)cc1 InChI=1S/C31H37N7O2/c1-33-29(39)8-6-4-5-7-26(31-34-19-27(36-31)24-12-9-22(10-13-24)20-37(2)3)35-30(40)21-38-16-15-25-17-23(18-32)11-14-28(25)38/h9-17,19,26H,4-8,20-21H2,1-3H3,(H,33,39)(H,34,36)(H,35,40)/t26-/m0/s1 WNBJBSFSPKVIPC-SANMLTNESA-N 50612441 CHEMBL5268555 Histone deacetylase 4 Homo sapiens >15000 ChEMBL 10.7270/Q2VM4HH1 30996783 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50612441 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50612441&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 171342340 494502189 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQJ,2VQM,4CBT,6FYZ,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51548500 [I-].C[n+]1ccc(NC(=O)CC(=O)N2Cc3ccccc3C2)c(c1)C#C InChI=1S/C19H17N3O2.HI/c1-3-14-11-21(2)9-8-17(14)20-18(23)10-19(24)22-12-15-6-4-5-7-16(15)13-22;/h1,4-9,11H,10,12-13H2,2H3;1H FGQPRQWRACRCSI-UHFFFAOYSA-N 50622893 CHEMBL5439733 Histone deacetylase 4 Homo sapiens 23100 ChEMBL 10.1021/acs.jmedchem.3c01779 10.7270/Q2B280PD 38113354 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50622893 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50622893&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51551554 ONC(=O)c1ccc(COc2no[n+]([O-])c2S(=O)(=O)c2ccccc2)cc1 InChI=1S/C16H13N3O7S/c20-14(17-21)12-8-6-11(7-9-12)10-25-15-16(19(22)26-18-15)27(23,24)13-4-2-1-3-5-13/h1-9,21H,10H2,(H,17,20) CKHUIFFTCIFDOH-UHFFFAOYSA-N 50624233 CHEMBL5410802 Histone deacetylase 4 Homo sapiens >40000 ChEMBL 10.1021/acs.jmedchem.3c00977 10.7270/Q24X5D6Q 37463038 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50624233 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50624233&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51546874 C[C@@H](c1ccc(cc1)C(=O)Nc1ccc(F)cc1N)n1nc(ccc1=O)-c1ccc(CN(C)C)cc1 InChI=1S/C28H28FN5O2/c1-18(20-8-10-22(11-9-20)28(36)31-26-13-12-23(29)16-24(26)30)34-27(35)15-14-25(32-34)21-6-4-19(5-7-21)17-33(2)3/h4-16,18H,17,30H2,1-3H3,(H,31,36)/t18-/m0/s1 LYXJJUVABRQDQS-SFHVURJKSA-N 673763 US20240150300, Compound I-1 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.3c00525 10.7270/Q24M98ZB 37184921 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=673763 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=673763&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 167225891 497643211 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51546875 Nc1ccccc1NC(=O)c1ccc(CNC(=O)OCc2cccnc2)cc1 InChI=1S/C21H20N4O3/c22-18-5-1-2-6-19(18)25-20(26)17-9-7-15(8-10-17)13-24-21(27)28-14-16-4-3-11-23-12-16/h1-12H,13-14,22H2,(H,24,27)(H,25,26) INVTYAOGFAGBOE-UHFFFAOYSA-N 19410 CHEMBL27759::MS-275::US11377423, MS-275::US11672788, Compound Entinostat::US20240150300, Compound MS-275::US9265734, MS-275::US9796664, Compound MS-275::benzamide-type inhibitor, 3::pyridin-3-ylmethyl N-({4-[(2-aminophenyl)carbamoyl]phenyl}methyl)carbamate Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.3c00525 10.7270/Q24M98ZB 37184921 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19410 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19410&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4261 46519433 CHEMBL27759 7007 ZINC01488870 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51551636 ONC(=O)c1ccc(Cn2c3c(Cl)cccc3c(=O)[nH]c2=O)cc1 InChI=1S/C16H12ClN3O4/c17-12-3-1-2-11-13(12)20(16(23)18-15(11)22)8-9-4-6-10(7-5-9)14(21)19-24/h1-7,24H,8H2,(H,19,21)(H,18,22,23) OWMZGLVMABQUAQ-UHFFFAOYSA-N 50624246 CHEMBL5438457 Histone deacetylase 4 Homo sapiens 516 ChEMBL 10.1021/acs.jmedchem.3c00644 10.7270/Q2154NFV 37463500 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50624246 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50624246&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51551637 Cc1nc2cc(\C=C\C(=O)NO)ccc2c(=O)n1-c1ccccc1 InChI=1S/C18H15N3O3/c1-12-19-16-11-13(8-10-17(22)20-24)7-9-15(16)18(23)21(12)14-5-3-2-4-6-14/h2-11,24H,1H3,(H,20,22)/b10-8+ MDTWRJDWPUJHKT-CSKARUKUSA-N 50624251 CHEMBL2425955 Histone deacetylase 4 Homo sapiens 30000 ChEMBL 10.1021/acs.jmedchem.3c00644 10.7270/Q2154NFV 37463500 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50624251 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50624251&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51553932 ONC(=O)\C=C\c1ccc(NC(=O)Cc2ccccc2)cn1 InChI=1S/C16H15N3O3/c20-15(19-22)9-8-13-6-7-14(11-17-13)18-16(21)10-12-4-2-1-3-5-12/h1-9,11,22H,10H2,(H,18,21)(H,19,20)/b9-8+ TUTLONWPIGDEGH-CMDGGOBGSA-N 50625238 CHEMBL5429873 Histone deacetylase 4 Homo sapiens 19300 ChEMBL 10.1016/j.ejmech.2022.115022 10.7270/Q2NK3KFC 36549114 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50625238 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50625238&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51553933 CCC(C(=O)Nc1ccc(\C=C\C(=O)NO)nc1)c1ccccc1 InChI=1S/C18H19N3O3/c1-2-16(13-6-4-3-5-7-13)18(23)20-15-9-8-14(19-12-15)10-11-17(22)21-24/h3-12,16,24H,2H2,1H3,(H,20,23)(H,21,22)/b11-10+ PGHNCIMZMFKLQY-ZHACJKMWSA-N 50625239 CHEMBL5408688 Histone deacetylase 4 Homo sapiens 17100 ChEMBL 10.1016/j.ejmech.2022.115022 10.7270/Q2NK3KFC 36549114 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50625239 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50625239&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51553934 CC(C)C(C(=O)Nc1ccc(\C=C\C(=O)NO)nc1)c1ccccc1 InChI=1S/C19H21N3O3/c1-13(2)18(14-6-4-3-5-7-14)19(24)21-16-9-8-15(20-12-16)10-11-17(23)22-25/h3-13,18,25H,1-2H3,(H,21,24)(H,22,23)/b11-10+ JGIUFXLFKQTSTL-ZHACJKMWSA-N 50625240 CHEMBL5400896 Histone deacetylase 4 Homo sapiens 16000 ChEMBL 10.1016/j.ejmech.2022.115022 10.7270/Q2NK3KFC 36549114 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50625240 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50625240&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51553935 ONC(=O)\C=C\c1ccc(NC(=O)Cc2ccc3ccccc3c2)cn1 InChI=1S/C20H17N3O3/c24-19(23-26)10-9-17-7-8-18(13-21-17)22-20(25)12-14-5-6-15-3-1-2-4-16(15)11-14/h1-11,13,26H,12H2,(H,22,25)(H,23,24)/b10-9+ PRWNDWJOZUOTNQ-MDZDMXLPSA-N 50625241 CHEMBL5401106 Histone deacetylase 4 Homo sapiens 17600 ChEMBL 10.1016/j.ejmech.2022.115022 10.7270/Q2NK3KFC 36549114 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50625241 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50625241&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51553936 ONC(=O)c1ccc(NC(=O)Cc2ccccc2)cn1 InChI=1S/C14H13N3O3/c18-13(8-10-4-2-1-3-5-10)16-11-6-7-12(15-9-11)14(19)17-20/h1-7,9,20H,8H2,(H,16,18)(H,17,19) KHCGDOSZEMWAGW-UHFFFAOYSA-N 50506781 CHEMBL4435005 Histone deacetylase 4 Homo sapiens 82400 ChEMBL 10.1016/j.ejmech.2022.115022 10.7270/Q2NK3KFC 36549114 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50506781 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50506781&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155510915 440715366 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51553937 CCC(C(=O)Nc1ccc(nc1)C(=O)NO)c1ccccc1 InChI=1S/C16H17N3O3/c1-2-13(11-6-4-3-5-7-11)15(20)18-12-8-9-14(17-10-12)16(21)19-22/h3-10,13,22H,2H2,1H3,(H,18,20)(H,19,21) CVBCVVCMLWNQKF-UHFFFAOYSA-N 50625248 CHEMBL5418060 Histone deacetylase 4 Homo sapiens 77900 ChEMBL 10.1016/j.ejmech.2022.115022 10.7270/Q2NK3KFC 36549114 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50625248 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50625248&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51553938 CC(C)C(C(=O)Nc1ccc(nc1)C(=O)NO)c1ccccc1 InChI=1S/C17H19N3O3/c1-11(2)15(12-6-4-3-5-7-12)17(22)19-13-8-9-14(18-10-13)16(21)20-23/h3-11,15,23H,1-2H3,(H,19,22)(H,20,21) DJUWADUNXSFHSV-UHFFFAOYSA-N 50625249 CHEMBL5425559 Histone deacetylase 4 Homo sapiens 63200 ChEMBL 10.1016/j.ejmech.2022.115022 10.7270/Q2NK3KFC 36549114 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50625249 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50625249&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51553939 ONC(=O)c1ccc(NC(=O)C(Cc2ccccc2)c2ccccc2)cn1 InChI=1S/C21H19N3O3/c25-20(23-17-11-12-19(22-14-17)21(26)24-27)18(16-9-5-2-6-10-16)13-15-7-3-1-4-8-15/h1-12,14,18,27H,13H2,(H,23,25)(H,24,26) LFAILFCZRLHSBV-UHFFFAOYSA-N 50625250 CHEMBL5411948 Histone deacetylase 4 Homo sapiens 39200 ChEMBL 10.1016/j.ejmech.2022.115022 10.7270/Q2NK3KFC 36549114 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50625250 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50625250&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51553940 ONC(=O)c1ccc(NC(=O)Cc2cccc3ccccc23)cn1 InChI=1S/C18H15N3O3/c22-17(20-14-8-9-16(19-11-14)18(23)21-24)10-13-6-3-5-12-4-1-2-7-15(12)13/h1-9,11,24H,10H2,(H,20,22)(H,21,23) JLCBQKQIFFSMTN-UHFFFAOYSA-N 50506779 CHEMBL4521590 Histone deacetylase 4 Homo sapiens 30700 ChEMBL 10.1016/j.ejmech.2022.115022 10.7270/Q2NK3KFC 36549114 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50506779 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50506779&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155542755 440715364 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51553941 ONC(=O)c1ccc(NC(=O)Cc2ccc3ccccc3c2)cn1 InChI=1S/C18H15N3O3/c22-17(20-15-7-8-16(19-11-15)18(23)21-24)10-12-5-6-13-3-1-2-4-14(13)9-12/h1-9,11,24H,10H2,(H,20,22)(H,21,23) USXBFTGGZAUGDB-UHFFFAOYSA-N 50625251 CHEMBL5426896 Histone deacetylase 4 Homo sapiens 15800 ChEMBL 10.1016/j.ejmech.2022.115022 10.7270/Q2NK3KFC 36549114 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50625251 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50625251&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51553942 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 76000 ChEMBL 10.1016/j.ejmech.2022.115022 10.7270/Q2NK3KFC 36549114 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,9GKX,9GKV,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,9GN6,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51553943 ONC(=O)\C=C\c1ccc(NC(=O)C(Cc2ccccc2)c2ccccc2)cn1 InChI=1S/C23H21N3O3/c27-22(26-29)14-13-19-11-12-20(16-24-19)25-23(28)21(18-9-5-2-6-10-18)15-17-7-3-1-4-8-17/h1-14,16,21,29H,15H2,(H,25,28)(H,26,27)/b14-13+ UQSIPNLHOWORHA-BUHFOSPRSA-N 50087841 CHEMBL3426804 Histone deacetylase 4 Homo sapiens 11700 ChEMBL 10.1016/j.ejmech.2022.115022 10.7270/Q2NK3KFC 36549114 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50087841 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50087841&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 118737400 103986869 CHEMBL3426804 ZINC13493926 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51553944 ONC(=O)\C=C\c1ccc(NC(=O)Cc2cccc3ccccc23)cn1 InChI=1S/C20H17N3O3/c24-19(23-26)11-10-16-8-9-17(13-21-16)22-20(25)12-15-6-3-5-14-4-1-2-7-18(14)15/h1-11,13,26H,12H2,(H,22,25)(H,23,24)/b11-10+ DTNVLAIWDVXDJR-ZHACJKMWSA-N 50506780 CHEMBL4550522 Histone deacetylase 4 Homo sapiens 2730 ChEMBL 10.1016/j.ejmech.2022.115022 10.7270/Q2NK3KFC 36549114 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50506780 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50506780&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 155555345 440715365 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51551971 COc1ccc2c3CCN(Cc3oc2c1)[C@@H](Cc1ccccc1)C(=O)Nc1ccc(cc1)C(=O)NO InChI=1S/C28H27N3O5/c1-35-21-11-12-22-23-13-14-31(17-26(23)36-25(22)16-21)24(15-18-5-3-2-4-6-18)28(33)29-20-9-7-19(8-10-20)27(32)30-34/h2-12,16,24,34H,13-15,17H2,1H3,(H,29,33)(H,30,32)/t24-/m0/s1 KRBROHHVEWJNNM-DEOSSOPVSA-N 50624387 CHEMBL5419989 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acs.jmedchem.3c01008 10.7270/Q2H41WTJ 37498552 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50624387 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50624387&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51551972 CN(C)Cc1c(oc2ccccc12)C(=O)NCCOc1ccc(cc1)C(=O)NO InChI=1S/C21H23N3O5/c1-24(2)13-17-16-5-3-4-6-18(16)29-19(17)21(26)22-11-12-28-15-9-7-14(8-10-15)20(25)23-27/h3-10,27H,11-13H2,1-2H3,(H,22,26)(H,23,25) MAUCONCHVWBMHK-UHFFFAOYSA-N 24622 3-[(dimethylamino)methyl]-N-{2-[4-(hydroxycarbamoyl)phenoxy]ethyl}-1-benzofuran-2-carboxamide::CRA-024781 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1021/acs.jmedchem.3c01008 10.7270/Q2H41WTJ 37498552 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=24622 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=24622&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11749858 56269573 ZINC06716700 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51549916 Nc1cc(F)ccc1NC(=O)c1ccc(CNC(=O)\C=C\c2cccnc2)cc1 InChI=1S/C22H19FN4O2/c23-18-8-9-20(19(24)12-18)27-22(29)17-6-3-16(4-7-17)14-26-21(28)10-5-15-2-1-11-25-13-15/h1-13H,14,24H2,(H,26,28)(H,27,29)/b10-5+ SZMJVTADHFNAIS-BJMVGYQFSA-N 50457079 CS-055::CS055::Chidamide::Epidaza in China::HBI-8000::Tucidinostat::US11377423, HUYA::US11672788, Compound Chidamide Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1016/j.ejmech.2023.115140 10.7270/Q2GH9PB9 36736154 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50457079 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50457079&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 12136798 433924346 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51549917 Nc1ccccc1NC(=O)c1ccc(NC(=O)c2n[nH]cc2NC(=O)c2c(Cl)cccc2Cl)cc1 InChI=1S/C24H18Cl2N6O3/c25-15-4-3-5-16(26)20(15)23(34)31-19-12-28-32-21(19)24(35)29-14-10-8-13(9-11-14)22(33)30-18-7-2-1-6-17(18)27/h1-12H,27H2,(H,28,32)(H,29,35)(H,30,33)(H,31,34) DMHUURDTAWQEKB-UHFFFAOYSA-N 50623515 CHEMBL5417235 Histone deacetylase 4 Homo sapiens >1000 ChEMBL 10.1016/j.ejmech.2023.115140 10.7270/Q2GH9PB9 36736154 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50623515 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50623515&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51548128 ONC(=O)CCCCCCNC(=O)c1cnc(nc1)N(c1ccccc1)c1ccccc1 InChI=1S/C24H27N5O3/c30-22(28-32)15-9-1-2-10-16-25-23(31)19-17-26-24(27-18-19)29(20-11-5-3-6-12-20)21-13-7-4-8-14-21/h3-8,11-14,17-18,32H,1-2,9-10,15-16H2,(H,25,31)(H,28,30) QGZYDVAGYRLSKP-UHFFFAOYSA-N 50439674 RICOLINOSTAT::US10858323, Compound 2::US11207431, Example E::US20230414581, Compound 43::US8609678, 2-(diphenylamino)-N-(7-(hydroxyamino)-7-oxoheptyl)pyrimidine-5-carboxamide [26] Histone deacetylase 4 Homo sapiens 7000 ChEMBL 10.1016/j.ejmech.2022.114920 10.7270/Q2W09B98 36399875 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50439674 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50439674&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search AH4 5WGL 53340666 175451991 ZINC89630354 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51548141 C\C=C1/NC(=O)[C@H]2CSSCC\C=C\[C@@H](CC(=O)N[C@H](C(C)C)C(=O)N2)OC(=O)[C@@H](NC1=O)C(C)C InChI=1S/C24H36N4O6S2/c1-6-16-21(30)28-20(14(4)5)24(33)34-15-9-7-8-10-35-36-12-17(22(31)25-16)26-23(32)19(13(2)3)27-18(29)11-15/h6-7,9,13-15,17,19-20H,8,10-12H2,1-5H3,(H,25,31)(H,26,32)(H,27,29)(H,28,30)/b9-7+,16-6-/t15-,17+,19+,20-/m0/s1 OHRURASPPZQGQM-QSVHVVLASA-N 50048864 CHEMBL3310505 Histone deacetylase 4 Homo sapiens 510 ChEMBL 10.1016/j.ejmech.2022.114920 10.7270/Q2W09B98 36399875 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50048864 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50048864&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 11947684 103979245 CHEMBL3310505 ZINC13745305 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51570098 Nc1ccccc1NC(=O)c1ccc(CNC(=O)OCc2cccnc2)cc1 InChI=1S/C21H20N4O3/c22-18-5-1-2-6-19(18)25-20(26)17-9-7-15(8-10-17)13-24-21(27)28-14-16-4-3-11-23-12-16/h1-12H,13-14,22H2,(H,24,27)(H,25,26) INVTYAOGFAGBOE-UHFFFAOYSA-N 19410 CHEMBL27759::MS-275::US11377423, MS-275::US11672788, Compound Entinostat::US20240150300, Compound MS-275::US9265734, MS-275::US9796664, Compound MS-275::benzamide-type inhibitor, 3::pyridin-3-ylmethyl N-({4-[(2-aminophenyl)carbamoyl]phenyl}methyl)carbamate Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.3c01236 10.7270/Q2BZ6BHH 38060537 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19410 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19410&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 4261 46519433 CHEMBL27759 7007 ZINC01488870 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51570099 Nc1ccccc1NC(=O)c1ccc(CNC(=O)OC2CCN(CC2)S(=O)(=O)c2c(F)c(F)c(F)c(F)c2F)cc1 InChI=1S/C26H23F5N4O5S/c27-19-20(28)22(30)24(23(31)21(19)29)41(38,39)35-11-9-16(10-12-35)40-26(37)33-13-14-5-7-15(8-6-14)25(36)34-18-4-2-1-3-17(18)32/h1-8,16H,9-13,32H2,(H,33,37)(H,34,36) JGJZNWDPKNHILY-UHFFFAOYSA-N 50631442 CHEMBL5411315 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.3c01236 10.7270/Q2BZ6BHH 38060537 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50631442 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50631442&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51572438 Nc1nn(nc1C(=O)NCc1ccc(cc1)C(=O)NO)-c1ccccc1 InChI=1S/C17H16N6O3/c18-15-14(20-23(21-15)13-4-2-1-3-5-13)17(25)19-10-11-6-8-12(9-7-11)16(24)22-26/h1-9,26H,10H2,(H2,18,21)(H,19,25)(H,22,24) NRYKLRJVRBXJSZ-UHFFFAOYSA-N 50632395 CHEMBL5415232 Histone deacetylase 4 Homo sapiens 2056 ChEMBL 10.1021/acs.jmedchem.2c01985 10.7270/Q2445RZS 36934335 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50632395 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50632395&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51572439 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.2c01985 10.7270/Q2445RZS 36934335 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,9GKX,9GKV,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,9GN6,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51572440 Nc1ccccc1NC(=O)c1ccc(CNc2nccc(n2)-c2cccnc2)cc1 InChI=1S/C23H20N6O/c24-19-5-1-2-6-21(19)28-22(30)17-9-7-16(8-10-17)14-27-23-26-13-11-20(29-23)18-4-3-12-25-15-18/h1-13,15H,14,24H2,(H,28,30)(H,26,27,29) HRNLUBSXIHFDHP-UHFFFAOYSA-N 24624 CHEMBL272980::MGCD-0103::MGCD0103::N-(2-aminophenyl)-4-({[4-(pyridin-3-yl)pyrimidin-2-yl]amino}methyl)benzamide::US10227295, Compound MGCD0103::US11377423, MGCD-0103::US9409858, MGCD0103::US9751832, MGCD0103::US9956192, Compound MGCD0103 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.2c01985 10.7270/Q2445RZS 36934335 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=24624 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=24624&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 9865515 56269575 CHEMBL272980 7008 ZINC13986811 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51572441 Nc1cc(F)ccc1NC(=O)c1ccc(CNC(=O)\C=C\c2cccnc2)cc1 InChI=1S/C22H19FN4O2/c23-18-8-9-20(19(24)12-18)27-22(29)17-6-3-16(4-7-17)14-26-21(28)10-5-15-2-1-11-25-13-15/h1-13H,14,24H2,(H,26,28)(H,27,29)/b10-5+ SZMJVTADHFNAIS-BJMVGYQFSA-N 50457079 CS-055::CS055::Chidamide::Epidaza in China::HBI-8000::Tucidinostat::US11377423, HUYA::US11672788, Compound Chidamide Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.2c01985 10.7270/Q2445RZS 36934335 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50457079 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50457079&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 12136798 433924346 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51572442 Nc1nn(nc1C(=O)NCc1ccc(cc1)C(=O)Nc1ccccc1N)-c1ccccc1Cl InChI=1S/C23H20ClN7O2/c24-16-5-1-4-8-19(16)31-29-20(21(26)30-31)23(33)27-13-14-9-11-15(12-10-14)22(32)28-18-7-3-2-6-17(18)25/h1-12H,13,25H2,(H2,26,30)(H,27,33)(H,28,32) BPVZRJLWWCCMKG-UHFFFAOYSA-N 50632430 CHEMBL5431071 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.2c01985 10.7270/Q2445RZS 36934335 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50632430 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50632430&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51573469 Cc1cnc(Nc2ccc(OCCCCCCC(=O)NO)cc2)nc1Nc1cccc(c1)S(=O)(=O)NC(C)(C)C InChI=1S/C28H38N6O5S/c1-20-19-29-27(31-21-13-15-23(16-14-21)39-17-8-6-5-7-12-25(35)33-36)32-26(20)30-22-10-9-11-24(18-22)40(37,38)34-28(2,3)4/h9-11,13-16,18-19,34,36H,5-8,12,17H2,1-4H3,(H,33,35)(H2,29,30,31,32) YJVWRVUQZNYKON-UHFFFAOYSA-N 50632923 CHEMBL5433552 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.3c00036 10.7270/Q2WH2VG7 37057760 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50632923 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50632923&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51573470 Cc1cnc(Nc2ccc(OCCCCCCC(=O)NO)c(F)c2)nc1Nc1cccc(c1)S(=O)(=O)NC(C)(C)C InChI=1S/C28H37FN6O5S/c1-19-18-30-27(33-26(19)31-20-10-9-11-22(16-20)41(38,39)35-28(2,3)4)32-21-13-14-24(23(29)17-21)40-15-8-6-5-7-12-25(36)34-37/h9-11,13-14,16-18,35,37H,5-8,12,15H2,1-4H3,(H,34,36)(H2,30,31,32,33) XQYXAGOVMRYFIS-UHFFFAOYSA-N 50632924 CHEMBL5395502 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.3c00036 10.7270/Q2WH2VG7 37057760 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50632924 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50632924&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51573471 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.3c00036 10.7270/Q2WH2VG7 37057760 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,9GKX,9GKV,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,9GN6,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51568758 ONC(=O)c1ccc(Cn2ccc3cc(ccc23)C(=O)NCC23C[C@H]4C[C@H](C[C@H](C4)C2)C3)cc1 InChI=1S/C28H31N3O3/c32-26(29-17-28-13-19-9-20(14-28)11-21(10-19)15-28)24-5-6-25-23(12-24)7-8-31(25)16-18-1-3-22(4-2-18)27(33)30-34/h1-8,12,19-21,34H,9-11,13-17H2,(H,29,32)(H,30,33)/t19-,20+,21-,28? OGOUVFOKYOKPNY-XMURTRJZSA-N 50630951 CHEMBL5424224 Histone deacetylase 4 Homo sapiens 1090 ChEMBL 10.1021/acs.jmedchem.3c01491 10.7270/Q2FX7FZJ 37972387 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630951 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630951&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51568759 ONC(=O)c1ccc(Cn2ccc3cc(ccc23)C(=O)NCC23C[C@H]4C[C@H](C[C@H](C4)C2)C3)c(F)c1 InChI=1S/C28H30FN3O3/c29-24-11-22(27(34)31-35)1-2-23(24)15-32-6-5-20-10-21(3-4-25(20)32)26(33)30-16-28-12-17-7-18(13-28)9-19(8-17)14-28/h1-6,10-11,17-19,35H,7-9,12-16H2,(H,30,33)(H,31,34)/t17-,18+,19-,28? AWLCTQDMWMZSKS-UGQIIZBGSA-N 50630952 CHEMBL5430740 Histone deacetylase 4 Homo sapiens 1120 ChEMBL 10.1021/acs.jmedchem.3c01491 10.7270/Q2FX7FZJ 37972387 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630952 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630952&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51568760 ONC(=O)c1ccc(Cn2ccc3cc(ccc23)C(=O)NCC23C[C@H]4C[C@H](C[C@H](C4)C2)C3)cc1F InChI=1S/C28H30FN3O3/c29-24-10-17(1-3-23(24)27(34)31-35)15-32-6-5-21-11-22(2-4-25(21)32)26(33)30-16-28-12-18-7-19(13-28)9-20(8-18)14-28/h1-6,10-11,18-20,35H,7-9,12-16H2,(H,30,33)(H,31,34)/t18-,19+,20-,28? XBNPUOXMQUEWOS-DMHOEKEMSA-N 50630953 CHEMBL5436104 Histone deacetylase 4 Homo sapiens 110 ChEMBL 10.1021/acs.jmedchem.3c01491 10.7270/Q2FX7FZJ 37972387 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630953 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630953&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51568761 COc1cc(ccc1Cn1ccc2cc(ccc12)C(=O)NCC12C[C@H]3C[C@H](C[C@H](C3)C1)C2)C(=O)NO InChI=1S/C29H33N3O4/c1-36-26-12-23(28(34)31-35)2-3-24(26)16-32-7-6-21-11-22(4-5-25(21)32)27(33)30-17-29-13-18-8-19(14-29)10-20(9-18)15-29/h2-7,11-12,18-20,35H,8-10,13-17H2,1H3,(H,30,33)(H,31,34)/t18-,19+,20-,29? WYYYPNVABFUNGR-VIBOSYLXSA-N 50630954 CHEMBL5405871 Histone deacetylase 4 Homo sapiens 3040 ChEMBL 10.1021/acs.jmedchem.3c01491 10.7270/Q2FX7FZJ 37972387 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630954 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630954&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51568762 COc1cc(Cn2ccc3cc(ccc23)C(=O)NCC23C[C@H]4C[C@H](C[C@H](C4)C2)C3)ccc1C(=O)NO InChI=1S/C29H33N3O4/c1-36-26-11-18(2-4-24(26)28(34)31-35)16-32-7-6-22-12-23(3-5-25(22)32)27(33)30-17-29-13-19-8-20(14-29)10-21(9-19)15-29/h2-7,11-12,19-21,35H,8-10,13-17H2,1H3,(H,30,33)(H,31,34)/t19-,20+,21-,29? JJMWRKOHPNUEJN-CTZVOZSRSA-N 50630955 CHEMBL5415287 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.3c01491 10.7270/Q2FX7FZJ 37972387 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630955 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630955&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51568763 Cc1cc(Cn2ccc3cc(ccc23)C(=O)NCC23C[C@H]4C[C@H](C[C@H](C4)C2)C3)ccc1C(=O)NO InChI=1S/C29H33N3O3/c1-18-8-19(2-4-25(18)28(34)31-35)16-32-7-6-23-12-24(3-5-26(23)32)27(33)30-17-29-13-20-9-21(14-29)11-22(10-20)15-29/h2-8,12,20-22,35H,9-11,13-17H2,1H3,(H,30,33)(H,31,34)/t20-,21+,22-,29? ZCTKVIDJFYSUSK-GZVDNEBNSA-N 50630956 CHEMBL5415394 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.3c01491 10.7270/Q2FX7FZJ 37972387 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630956 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630956&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51568764 ONC(=O)c1ccc(Cn2ccc3cc(ccc23)C(=O)NCC23C[C@H]4C[C@H](C[C@H](C4)C2)C3)cc1O InChI=1S/C28H31N3O4/c32-25-10-17(1-3-23(25)27(34)30-35)15-31-6-5-21-11-22(2-4-24(21)31)26(33)29-16-28-12-18-7-19(13-28)9-20(8-18)14-28/h1-6,10-11,18-20,32,35H,7-9,12-16H2,(H,29,33)(H,30,34)/t18-,19+,20-,28? CSCWEEIJBZSOPY-DMHOEKEMSA-N 50630957 CHEMBL5395395 Histone deacetylase 4 Homo sapiens 1600 ChEMBL 10.1021/acs.jmedchem.3c01491 10.7270/Q2FX7FZJ 37972387 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630957 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630957&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51568765 CCOc1cc(Cn2ccc3cc(ccc23)C(=O)NCC23C[C@H]4C[C@H](C[C@H](C4)C2)C3)ccc1C(=O)NO InChI=1S/C30H35N3O4/c1-2-37-27-12-19(3-5-25(27)29(35)32-36)17-33-8-7-23-13-24(4-6-26(23)33)28(34)31-18-30-14-20-9-21(15-30)11-22(10-20)16-30/h3-8,12-13,20-22,36H,2,9-11,14-18H2,1H3,(H,31,34)(H,32,35)/t20-,21+,22-,30? JZTMEOJBADVKCP-UPLOIYFPSA-N 50630958 CHEMBL5421030 Histone deacetylase 4 Homo sapiens >10000 ChEMBL 10.1021/acs.jmedchem.3c01491 10.7270/Q2FX7FZJ 37972387 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630958 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630958&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51568766 ONC(=O)c1ccc(Cn2ccc3cc(ccc23)C(=O)NCC23C[C@H]4C[C@H](C[C@H](C4)C2)C3)cc1Cl InChI=1S/C28H30ClN3O3/c29-24-10-17(1-3-23(24)27(34)31-35)15-32-6-5-21-11-22(2-4-25(21)32)26(33)30-16-28-12-18-7-19(13-28)9-20(8-18)14-28/h1-6,10-11,18-20,35H,7-9,12-16H2,(H,30,33)(H,31,34)/t18-,19+,20-,28? SALUDWMRYYZYRA-DMHOEKEMSA-N 50630959 CHEMBL5415658 Histone deacetylase 4 Homo sapiens 1200 ChEMBL 10.1021/acs.jmedchem.3c01491 10.7270/Q2FX7FZJ 37972387 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630959 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630959&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51568767 ONC(=O)c1ccc(Cn2ccc3cc(ccc23)C(=O)NCC23C[C@H]4C[C@H](C[C@H](C4)C2)C3)cc1Br InChI=1S/C28H30BrN3O3/c29-24-10-17(1-3-23(24)27(34)31-35)15-32-6-5-21-11-22(2-4-25(21)32)26(33)30-16-28-12-18-7-19(13-28)9-20(8-18)14-28/h1-6,10-11,18-20,35H,7-9,12-16H2,(H,30,33)(H,31,34)/t18-,19+,20-,28? JGJNFFIWMLTLRX-DMHOEKEMSA-N 50630960 CHEMBL5399941 Histone deacetylase 4 Homo sapiens 1370 ChEMBL 10.1021/acs.jmedchem.3c01491 10.7270/Q2FX7FZJ 37972387 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630960 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630960&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51568768 C[C@H](\C=C(/C)\C=C\C(=O)NO)C(=O)c1ccc(cc1)N(C)C InChI=1S/C17H22N2O3/c1-12(5-10-16(20)18-22)11-13(2)17(21)14-6-8-15(9-7-14)19(3)4/h5-11,13,22H,1-4H3,(H,18,20)/b10-5+,12-11+/t13-/m1/s1 RTKIYFITIVXBLE-QEQCGCAPSA-N 50005711 CHEBI:46024::GNF-Pf-1011::TRICHOSTATIN::Trichostatin A::Trichostatin A (TSA)::US10011611, Trichostatin A::US10722597, Compound Trichostatin::US11535598, Compound Trichostatin A::US20230322747, Compound trichostatin A::US9265734, TSA Histone deacetylase 4 Homo sapiens 1210 ChEMBL 10.1021/acs.jmedchem.3c01491 10.7270/Q2FX7FZJ 37972387 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005711 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005711&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search TSN 5WGI,6UO2,6UO4,5EDU,5EEF,1T64,5G0G,5D1B,9GN7,1C3R,4QA3,6HOY,5EEK,6WYO,3C10 444732 242056952 DB04297 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51566858 Nc1ccccc1NC(=O)c1ccc(COc2ccc(CNC(=O)[C@@H]3CCC(=O)N3Cc3ccccc3)cc2)cc1 InChI=1S/C33H32N4O4/c34-28-8-4-5-9-29(28)36-32(39)26-14-10-25(11-15-26)22-41-27-16-12-23(13-17-27)20-35-33(40)30-18-19-31(38)37(30)21-24-6-2-1-3-7-24/h1-17,30H,18-22,34H2,(H,35,40)(H,36,39)/t30-/m0/s1 QGJOQSWDMMVMFK-PMERELPUSA-N 50630096 CHEMBL5399337 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.3c01422 10.7270/Q2K078Q8 37795958 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630096 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630096&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51566859 Nc1ccccc1NC(=O)c1ccc(COc2ccc(CNC(=O)[C@H]3CCC(=O)N3Cc3ccccc3)cc2)cc1 InChI=1S/C33H32N4O4/c34-28-8-4-5-9-29(28)36-32(39)26-14-10-25(11-15-26)22-41-27-16-12-23(13-17-27)20-35-33(40)30-18-19-31(38)37(30)21-24-6-2-1-3-7-24/h1-17,30H,18-22,34H2,(H,35,40)(H,36,39)/t30-/m1/s1 QGJOQSWDMMVMFK-SSEXGKCCSA-N 50630097 CHEMBL5433049 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.3c01422 10.7270/Q2K078Q8 37795958 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630097 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630097&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51566860 Nc1ccccc1NC(=O)c1ccc(COc2ccc(CNC(=O)[C@@H]3CCCN3Cc3ccccc3)cc2)cc1 InChI=1S/C33H34N4O3/c34-29-9-4-5-10-30(29)36-32(38)27-16-12-26(13-17-27)23-40-28-18-14-24(15-19-28)21-35-33(39)31-11-6-20-37(31)22-25-7-2-1-3-8-25/h1-5,7-10,12-19,31H,6,11,20-23,34H2,(H,35,39)(H,36,38)/t31-/m0/s1 FWWZNWCRXJQHCP-HKBQPEDESA-N 50630102 CHEMBL5403777 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.3c01422 10.7270/Q2K078Q8 37795958 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630102 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630102&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51566861 Cl.Cl.Nc1ccccc1NC(=O)c1ccc(COc2ccc(CNC(=O)[C@@H]3CCCN3)cc2)cc1 InChI=1S/C26H28N4O3.2ClH/c27-22-4-1-2-5-23(22)30-25(31)20-11-7-19(8-12-20)17-33-21-13-9-18(10-14-21)16-29-26(32)24-6-3-15-28-24;;/h1-2,4-5,7-14,24,28H,3,6,15-17,27H2,(H,29,32)(H,30,31);2*1H/t24-;;/m0../s1 UFARUDAPUKLDQM-ASMAMLKCSA-N 50630104 CHEMBL5407714 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.3c01422 10.7270/Q2K078Q8 37795958 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630104 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630104&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51566862 Cl.Cl.Nc1ccccc1NC(=O)c1ccc(COc2ccc(CNC(=O)[C@H]3CCCN3)cc2)cc1 InChI=1S/C26H28N4O3.2ClH/c27-22-4-1-2-5-23(22)30-25(31)20-11-7-19(8-12-20)17-33-21-13-9-18(10-14-21)16-29-26(32)24-6-3-15-28-24;;/h1-2,4-5,7-14,24,28H,3,6,15-17,27H2,(H,29,32)(H,30,31);2*1H/t24-;;/m1../s1 UFARUDAPUKLDQM-PPLJNSMQSA-N 50630105 CHEMBL5436682 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.3c01422 10.7270/Q2K078Q8 37795958 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630105 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630105&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51566863 Cl.Cl.NCc1ccc(OCc2ccc(cc2)C(=O)Nc2ccccc2N)cc1 InChI=1S/C21H21N3O2.2ClH/c22-13-15-7-11-18(12-8-15)26-14-16-5-9-17(10-6-16)21(25)24-20-4-2-1-3-19(20)23;;/h1-12H,13-14,22-23H2,(H,24,25);2*1H SKUYZAGCVBEGSS-UHFFFAOYSA-N 50630115 CHEMBL5415256 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.3c01422 10.7270/Q2K078Q8 37795958 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630115 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630115&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51566907 Cc1cnc(Nc2ccc(OCCN3CCCC3)cc2)nc1Nc1ccc(cc1)C(=O)NO InChI=1S/C24H28N6O3/c1-17-16-25-24(28-22(17)26-19-6-4-18(5-7-19)23(31)29-32)27-20-8-10-21(11-9-20)33-15-14-30-12-2-3-13-30/h4-11,16,32H,2-3,12-15H2,1H3,(H,29,31)(H2,25,26,27,28) JUIHREVFVXLZPR-UHFFFAOYSA-N 50630116 CHEMBL5408198 Histone deacetylase 4 Homo sapiens >5000 ChEMBL 10.1021/acs.jmedchem.3c01242 10.7270/Q2F76J0Z 37796543 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630116 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630116&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51566908 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >5000 ChEMBL 10.1021/acs.jmedchem.3c01242 10.7270/Q2F76J0Z 37796543 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,9GKX,9GKV,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,9GN6,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51566968 ONC(=O)c1cnc(NC2(CCC(F)(F)CC2)c2ccccc2)nc1 InChI=1S/C17H18F2N4O2/c18-17(19)8-6-16(7-9-17,13-4-2-1-3-5-13)22-15-20-10-12(11-21-15)14(24)23-25/h1-5,10-11,25H,6-9H2,(H,23,24)(H,20,21,22) MRWCVKLVSWYIFO-UHFFFAOYSA-N 249366 US9464073, 003::US9884850, Compound 3 Histone deacetylase 4 Homo sapiens 12000 ChEMBL 10.1021/acs.jmedchem.3c01269 10.7270/Q21Z48VM 37797307 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=249366 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=249366&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search AH7 5WGM 91844718 346543867 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51566969 FC(F)c1nnc(o1)-c1ccc(Cn2nnc(n2)-c2ccccn2)nc1 InChI=1S/C15H10F2N8O/c16-12(17)15-22-21-14(26-15)9-4-5-10(19-7-9)8-25-23-13(20-24-25)11-3-1-2-6-18-11/h1-7,12H,8H2 ZTVLPDLCENUSAG-UHFFFAOYSA-N 50630153 CHEMBL5429808 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.3c01269 10.7270/Q21Z48VM 37797307 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630153 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630153&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51566970 COc1ccccc1-c1nnn(Cc2ccc(cn2)-c2nnc(o2)C(F)F)n1 InChI=1S/C17H13F2N7O2/c1-27-13-5-3-2-4-12(13)15-21-25-26(24-15)9-11-7-6-10(8-20-11)16-22-23-17(28-16)14(18)19/h2-8,14H,9H2,1H3 YNZZZGZGZGBKPB-UHFFFAOYSA-N 50630154 CHEMBL5425061 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.3c01269 10.7270/Q21Z48VM 37797307 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630154 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630154&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51566971 CS(=O)(=O)NCC(Nc1ncc(cn1)-c1nnc(o1)C(F)F)c1ccc(OC(F)(F)F)cc1 InChI=1S/C17H15F5N6O4S/c1-33(29,30)25-8-12(9-2-4-11(5-3-9)32-17(20,21)22)26-16-23-6-10(7-24-16)14-27-28-15(31-14)13(18)19/h2-7,12-13,25H,8H2,1H3,(H,23,24,26) RJVSECRBBVXPCQ-UHFFFAOYSA-N 50630155 CHEMBL5410192 Histone deacetylase 4 Homo sapiens 14000 ChEMBL 10.1021/acs.jmedchem.3c01269 10.7270/Q21Z48VM 37797307 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50630155 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50630155&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51565434 FC(F)(F)c1nc(no1)-c1cccc(c1)C(=O)NCC1(CCOCC1)c1nc(cs1)-c1ccccc1 InChI=1S/C25H21F3N4O3S/c26-25(27,28)22-31-20(32-35-22)17-7-4-8-18(13-17)21(33)29-15-24(9-11-34-12-10-24)23-30-19(14-36-23)16-5-2-1-3-6-16/h1-8,13-14H,9-12,15H2,(H,29,33) HORXBWNTEDOVKN-UHFFFAOYSA-N 50446481 CHEMBL3110004::US10011611, TMP269::US10722597, Compound TMP-269 Histone deacetylase 4 Homo sapiens 753 ChEMBL 10.1021/acs.jmedchem.3c01345 10.7270/Q2ST7V92 37782298 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50446481 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50446481&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search NU9 3ZNR 53344908 194944377 CHEMBL3110004 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51563448 CCCNNC(=O)c1cnc(NCc2ccc(OC)cc2)cn1 InChI=1S/C16H21N5O2/c1-3-8-20-21-16(22)14-10-19-15(11-17-14)18-9-12-4-6-13(23-2)7-5-12/h4-7,10-11,20H,3,8-9H2,1-2H3,(H,18,19)(H,21,22) UNXQXLFIXZKRCS-UHFFFAOYSA-N 50628633 CHEMBL5435277 Histone deacetylase 4 Homo sapiens >20000 ChEMBL 10.1021/acs.jmedchem.3c00614 10.7270/Q2S46XFD 37660352 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50628633 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50628633&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51554533 FC(F)(F)C(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C15H18F3NO2/c16-15(17,18)13(20)10-6-1-2-7-11-14(21)19-12-8-4-3-5-9-12/h3-5,8-9H,1-2,6-7,10-11H2,(H,19,21) KRCXZGYVOZSCSF-UHFFFAOYSA-N 50121062 9,9,9-TRIFLUORO-8-OXO-N-PHENYLNONANAMIDE::9,9,9-Trifluoro-8-oxo-nonanoic acid phenylamide::CHEMBL113537 Histone deacetylase 4 Homo sapiens 40 ChEMBL 10.1021/acs.jmedchem.3c00226 10.7270/Q2FX7FWN 37276138 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50121062 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50121062&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search CF3 2GH6 9882812 104013979 CHEMBL113537 DB07553 ZINC01553046 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51554534 FC(F)(F)C(=O)c1ccc(s1)C(=O)N1CCc2ccccc12 InChI=1S/C15H10F3NO2S/c16-15(17,18)13(20)11-5-6-12(22-11)14(21)19-8-7-9-3-1-2-4-10(9)19/h1-6H,7-8H2 FPQZFCVFBLEELM-UHFFFAOYSA-N 25162 1-[5-(2,3-dihydro-1H-indol-1-ylcarbonyl)thiophen-2-yl]-2,2,2-trifluoroethan-1-one::CHEMBL525529::thiophene derivative, 3h Histone deacetylase 4 Homo sapiens 130 ChEMBL 10.1021/acs.jmedchem.3c00226 10.7270/Q2FX7FWN 37276138 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25162 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25162&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023801 56374303 CHEMBL525529 ZINC29069755 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51554535 FC(F)C(=O)c1ccc(s1)C(=O)N1CCc2ccccc12 InChI=1S/C15H11F2NO2S/c16-14(17)13(19)11-5-6-12(21-11)15(20)18-8-7-9-3-1-2-4-10(9)18/h1-6,14H,7-8H2 WZGNPOPOCGTSMZ-UHFFFAOYSA-N 25172 1-[5-(2,3-dihydro-1H-indol-1-ylcarbonyl)thiophen-2-yl]-2,2-difluoroethan-1-one::thiophene derivative, 15h Histone deacetylase 4 Homo sapiens 7600 ChEMBL 10.1021/acs.jmedchem.3c00226 10.7270/Q2FX7FWN 37276138 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=25172 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=25172&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 25023808 56374313 ZINC29069581 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51554536 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens 24000 ChEMBL 10.1021/acs.jmedchem.3c00226 10.7270/Q2FX7FWN 37276138 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,9GKX,9GKV,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,9GN6,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51554537 C[Si](O)(O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H23NO3Si/c1-19(17,18)12-8-3-2-7-11-14(16)15-13-9-5-4-6-10-13/h4-6,9-10,17-18H,2-3,7-8,11-12H2,1H3,(H,15,16) SYOJIQXYKCJISC-UHFFFAOYSA-N 50462116 CHEMBL4250582 Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.1021/acs.jmedchem.3c00226 10.7270/Q2FX7FWN 37276138 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50462116 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50462116&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 145983639 433929381 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51554635 ON1C[C@@H](CCCCCC(=O)Nc2ccccc2)C1=O InChI=1S/C15H20N2O3/c18-14(16-13-8-4-2-5-9-13)10-6-1-3-7-12-11-17(20)15(12)19/h2,4-5,8-9,12,20H,1,3,6-7,10-11H2,(H,16,18)/t12-/m1/s1 UGQFBCMVKWECOS-GFCCVEGCSA-N 50625524 CHEMBL5415357 Histone deacetylase 4 Homo sapiens >1000000 ChEMBL 10.1021/acs.jmedchem.3c00226 10.7270/Q2FX7FWN 37276138 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50625524 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50625524&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51554636 ON1C[C@H](CCCCCC(=O)Nc2ccccc2)C1=O InChI=1S/C15H20N2O3/c18-14(16-13-8-4-2-5-9-13)10-6-1-3-7-12-11-17(20)15(12)19/h2,4-5,8-9,12,20H,1,3,6-7,10-11H2,(H,16,18)/t12-/m0/s1 UGQFBCMVKWECOS-LBPRGKRZSA-N 50625525 CHEMBL5436129 Histone deacetylase 4 Homo sapiens >1000000 ChEMBL 10.1021/acs.jmedchem.3c00226 10.7270/Q2FX7FWN 37276138 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50625525 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50625525&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51554637 O=C(CCCCCC1CNC1=O)Nc1ccccc1 InChI=1S/C15H20N2O2/c18-14(17-13-8-4-2-5-9-13)10-6-1-3-7-12-11-16-15(12)19/h2,4-5,8-9,12H,1,3,6-7,10-11H2,(H,16,19)(H,17,18) XRLJWKLIQWQEOG-UHFFFAOYSA-N 50625526 CHEMBL5402508 Histone deacetylase 4 Homo sapiens >1000000 ChEMBL 10.1021/acs.jmedchem.3c00226 10.7270/Q2FX7FWN 37276138 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50625526 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50625526&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51554638 Nc1ccccc1N1CC(CCCCCC(=O)Nc2ccccc2)C1=O InChI=1S/C21H25N3O2/c22-18-12-7-8-13-19(18)24-15-16(21(24)26)9-3-1-6-14-20(25)23-17-10-4-2-5-11-17/h2,4-5,7-8,10-13,16H,1,3,6,9,14-15,22H2,(H,23,25) LILAXEOHZMQNKW-UHFFFAOYSA-N 50625527 CHEMBL5425781 Histone deacetylase 4 Homo sapiens >1000000 ChEMBL 10.1021/acs.jmedchem.3c00226 10.7270/Q2FX7FWN 37276138 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50625527 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50625527&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51554677 CNC(=O)C(CCCCCCC(=O)Nc1ccccc1)N=O InChI=1S/C16H23N3O3/c1-17-16(21)14(19-22)11-7-2-3-8-12-15(20)18-13-9-5-4-6-10-13/h4-6,9-10,14H,2-3,7-8,11-12H2,1H3,(H,17,21)(H,18,20) LEVQYUXQSVPMMA-UHFFFAOYSA-N 50341844 2-(Hydroxyimino)-N1-methyl-N9-phenylnonanediamide::CHEMBL1767029 Histone deacetylase 4 Homo sapiens 22000 ChEMBL 10.1021/acs.jmedchem.3c00226 10.7270/Q2FX7FWN 37276138 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50341844 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50341844&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 91932411 131344780 CHEMBL1767029 ZINC71318447 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51537852 ONC(=O)c1ccc(CN2CCCc3cccnc23)c(F)c1 InChI=1S/C16H16FN3O2/c17-14-9-12(16(21)19-22)5-6-13(14)10-20-8-2-4-11-3-1-7-18-15(11)20/h1,3,5-7,9,22H,2,4,8,10H2,(H,19,21) IRALAZOBAVZSHO-UHFFFAOYSA-N 50618629 CHEMBL5401750 Histone deacetylase 4 Homo sapiens 578 ChEMBL 10.1016/j.ejmech.2023.115327 10.7270/Q2183BWM 37098307 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50618629 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50618629&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51540970 ONC(=O)CCCCCCNC(=O)c1ncc(o1)-c1ccccc1 InChI=1S/C17H21N3O4/c21-15(20-23)10-6-1-2-7-11-18-16(22)17-19-12-14(24-17)13-8-4-3-5-9-13/h3-5,8-9,12,23H,1-2,6-7,10-11H2,(H,18,22)(H,20,21) YWUJXZMRSZVDMK-UHFFFAOYSA-N 50619768 CHEMBL5416448 Histone deacetylase 4 Homo sapiens >5000 ChEMBL 10.1016/j.ejmech.2022.114705 10.7270/Q2QC07WG 36215854 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50619768 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50619768&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51540971 ONC(=O)CCCCCCNC(=O)c1ncc(o1)-c1ccc(Br)cc1 InChI=1S/C17H20BrN3O4/c18-13-8-6-12(7-9-13)14-11-20-17(25-14)16(23)19-10-4-2-1-3-5-15(22)21-24/h6-9,11,24H,1-5,10H2,(H,19,23)(H,21,22) YNWLMVWHXKRQRH-UHFFFAOYSA-N 50619780 CHEMBL5399106 Histone deacetylase 4 Homo sapiens >5000 ChEMBL 10.1016/j.ejmech.2022.114705 10.7270/Q2QC07WG 36215854 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50619780 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50619780&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51540972 COc1ccccc1-c1cnc(s1)C(=O)NCCCCCCC(=O)NO InChI=1S/C18H23N3O4S/c1-25-14-9-6-5-8-13(14)15-12-20-18(26-15)17(23)19-11-7-3-2-4-10-16(22)21-24/h5-6,8-9,12,24H,2-4,7,10-11H2,1H3,(H,19,23)(H,21,22) UQAUKCBFWYIVMU-UHFFFAOYSA-N 50619804 CHEMBL5413000 Histone deacetylase 4 Homo sapiens >5000 ChEMBL 10.1016/j.ejmech.2022.114705 10.7270/Q2QC07WG 36215854 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50619804 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50619804&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51540973 ONC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 CHEMBL98::N-hydroxy-N'-phenyloctanediamide::SAHA::US10011611, SAHA::US10188756, Compound SAHA::US11207431, SAHA::US11505523, Compound SAHA::US9115116, SAHA::US9353061, SAHA::US9428447, SAHA::US9695181, Vorinostat::Vorinostat::Zolinza::cid_5311::suberoylanilide hydroxamic acid Histone deacetylase 4 Homo sapiens >5000 ChEMBL 10.1016/j.ejmech.2022.114705 10.7270/Q2QC07WG 36215854 n/a n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,9GKX,9GKV,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,9GN6,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 45716 CHEMBL98 DB02546 6852 ZINC01543873 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6