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 Date of publication Date in BindingDB 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 PubChem SID 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 1 PDB ID(s) of Target Chain 1 UniProt (SwissProt) Recommended Name of Target Chain 1 UniProt (SwissProt) Entry Name of Target Chain 1 UniProt (SwissProt) Primary ID of Target Chain 1 UniProt (SwissProt) Secondary ID(s) of Target Chain 1 UniProt (SwissProt) Alternative ID(s) of Target Chain 1 UniProt (TrEMBL) Submitted Name of Target Chain 1 UniProt (TrEMBL) Entry Name of Target Chain 1 UniProt (TrEMBL) Primary ID of Target Chain 1 UniProt (TrEMBL) Secondary ID(s) of Target Chain 1 UniProt (TrEMBL) Alternative ID(s) of Target Chain 1 BindingDB Target Chain Sequence 2 PDB ID(s) of Target Chain 2 UniProt (SwissProt) Recommended Name of Target Chain 2 UniProt (SwissProt) Entry Name of Target Chain 2 UniProt (SwissProt) Primary ID of Target Chain 2 UniProt (SwissProt) Secondary ID(s) of Target Chain 2 UniProt (SwissProt) Alternative ID(s) of Target Chain 2 UniProt (TrEMBL) Submitted Name of Target Chain 2 UniProt (TrEMBL) Entry Name of Target Chain 2 UniProt (TrEMBL) Primary ID of Target Chain 2 UniProt (TrEMBL) Secondary ID(s) of Target Chain 2 UniProt (TrEMBL) Alternative ID(s) of Target Chain 2 BindingDB Target Chain Sequence 3 PDB ID(s) of Target Chain 3 UniProt (SwissProt) Recommended Name of Target Chain 3 UniProt (SwissProt) Entry Name of Target Chain 3 UniProt (SwissProt) Primary ID of Target Chain 3 UniProt (SwissProt) Secondary ID(s) of Target Chain 3 UniProt (SwissProt) Alternative ID(s) of Target Chain 3 UniProt (TrEMBL) Submitted Name of Target Chain 3 UniProt (TrEMBL) Entry Name of Target Chain 3 UniProt (TrEMBL) Primary ID of Target Chain 3 UniProt (TrEMBL) Secondary ID(s) of Target Chain 3 UniProt (TrEMBL) Alternative ID(s) of Target Chain 3 BindingDB Target Chain Sequence 4 PDB ID(s) of Target Chain 4 UniProt (SwissProt) Recommended Name of Target Chain 4 UniProt (SwissProt) Entry Name of Target Chain 4 UniProt (SwissProt) Primary ID of Target Chain 4 UniProt (SwissProt) Secondary ID(s) of Target Chain 4 UniProt (SwissProt) Alternative ID(s) of Target Chain 4 UniProt (TrEMBL) Submitted Name of Target Chain 4 UniProt (TrEMBL) Entry Name of Target Chain 4 UniProt (TrEMBL) Primary ID of Target Chain 4 UniProt (TrEMBL) Secondary ID(s) of Target Chain 4 UniProt (TrEMBL) Alternative ID(s) of Target Chain 4 BindingDB Target Chain Sequence 5 PDB ID(s) of Target Chain 5 UniProt (SwissProt) Recommended Name of Target Chain 5 UniProt (SwissProt) Entry Name of Target Chain 5 UniProt (SwissProt) Primary ID of Target Chain 5 UniProt (SwissProt) Secondary ID(s) of Target Chain 5 UniProt (SwissProt) Alternative ID(s) of Target Chain 5 UniProt (TrEMBL) Submitted Name of Target Chain 5 UniProt (TrEMBL) Entry Name of Target Chain 5 UniProt (TrEMBL) Primary ID of Target Chain 5 UniProt (TrEMBL) Secondary ID(s) of Target Chain 5 UniProt (TrEMBL) Alternative ID(s) of Target Chain 5 BindingDB Target Chain Sequence 6 PDB ID(s) of Target Chain 6 UniProt (SwissProt) Recommended Name of Target Chain 6 UniProt (SwissProt) Entry Name of Target Chain 6 UniProt (SwissProt) Primary ID of Target Chain 6 UniProt (SwissProt) Secondary ID(s) of Target Chain 6 UniProt (SwissProt) Alternative ID(s) of Target Chain 6 UniProt (TrEMBL) Submitted Name of Target Chain 6 UniProt (TrEMBL) Entry Name of Target Chain 6 UniProt (TrEMBL) Primary ID of Target Chain 6 UniProt (TrEMBL) Secondary ID(s) of Target Chain 6 UniProt (TrEMBL) Alternative ID(s) of Target Chain 6 BindingDB Target Chain Sequence 7 PDB ID(s) of Target Chain 7 UniProt (SwissProt) Recommended Name of Target Chain 7 UniProt (SwissProt) Entry Name of Target Chain 7 UniProt (SwissProt) Primary ID of Target Chain 7 UniProt (SwissProt) Secondary ID(s) of Target Chain 7 UniProt (SwissProt) Alternative ID(s) of Target Chain 7 UniProt (TrEMBL) Submitted Name of Target Chain 7 UniProt (TrEMBL) Entry Name of Target Chain 7 UniProt (TrEMBL) Primary ID of Target Chain 7 UniProt (TrEMBL) Secondary ID(s) of Target Chain 7 UniProt (TrEMBL) Alternative ID(s) of Target Chain 7 BindingDB Target Chain Sequence 8 PDB ID(s) of Target Chain 8 UniProt (SwissProt) Recommended Name of Target Chain 8 UniProt (SwissProt) Entry Name of Target Chain 8 UniProt (SwissProt) Primary ID of Target Chain 8 UniProt (SwissProt) Secondary ID(s) of Target Chain 8 UniProt (SwissProt) Alternative ID(s) of Target Chain 8 UniProt (TrEMBL) Submitted Name of Target Chain 8 UniProt (TrEMBL) Entry Name of Target Chain 8 UniProt (TrEMBL) Primary ID of Target Chain 8 UniProt (TrEMBL) Secondary ID(s) of Target Chain 8 UniProt (TrEMBL) Alternative ID(s) of Target Chain 8 BindingDB Target Chain Sequence 9 PDB ID(s) of Target Chain 9 UniProt (SwissProt) Recommended Name of Target Chain 9 UniProt (SwissProt) Entry Name of Target Chain 9 UniProt (SwissProt) Primary ID of Target Chain 9 UniProt (SwissProt) Secondary ID(s) of Target Chain 9 UniProt (SwissProt) Alternative ID(s) of Target Chain 9 UniProt (TrEMBL) Submitted Name of Target Chain 9 UniProt (TrEMBL) Entry Name of Target Chain 9 UniProt (TrEMBL) Primary ID of Target Chain 9 UniProt (TrEMBL) Secondary ID(s) of Target Chain 9 UniProt (TrEMBL) Alternative ID(s) of Target Chain 9 BindingDB Target Chain Sequence 10 PDB ID(s) of Target Chain 10 UniProt (SwissProt) Recommended Name of Target Chain 10 UniProt (SwissProt) Entry Name of Target Chain 10 UniProt (SwissProt) Primary ID of Target Chain 10 UniProt (SwissProt) Secondary ID(s) of Target Chain 10 UniProt (SwissProt) Alternative ID(s) of Target Chain 10 UniProt (TrEMBL) Submitted Name of Target Chain 10 UniProt (TrEMBL) Entry Name of Target Chain 10 UniProt (TrEMBL) Primary ID of Target Chain 10 UniProt (TrEMBL) Secondary ID(s) of Target Chain 10 UniProt (TrEMBL) Alternative ID(s) of Target Chain 10 BindingDB Target Chain Sequence 11 PDB ID(s) of Target Chain 11 UniProt (SwissProt) Recommended Name of Target Chain 11 UniProt (SwissProt) Entry Name of Target Chain 11 UniProt (SwissProt) Primary ID of Target Chain 11 UniProt (SwissProt) Secondary ID(s) of Target Chain 11 UniProt (SwissProt) Alternative ID(s) of Target Chain 11 UniProt (TrEMBL) Submitted Name of Target Chain 11 UniProt (TrEMBL) Entry Name of Target Chain 11 UniProt (TrEMBL) Primary ID of Target Chain 11 UniProt (TrEMBL) Secondary ID(s) of Target Chain 11 UniProt (TrEMBL) Alternative ID(s) of Target Chain 11 BindingDB Target Chain Sequence 12 PDB ID(s) of Target Chain 12 UniProt (SwissProt) Recommended Name of Target Chain 12 UniProt (SwissProt) Entry Name of Target Chain 12 UniProt (SwissProt) Primary ID of Target Chain 12 UniProt (SwissProt) Secondary ID(s) of Target Chain 12 UniProt (SwissProt) Alternative ID(s) of Target Chain 12 UniProt (TrEMBL) Submitted Name of Target Chain 12 UniProt (TrEMBL) Entry Name of Target Chain 12 UniProt (TrEMBL) Primary ID of Target Chain 12 UniProt (TrEMBL) Secondary ID(s) of Target Chain 12 UniProt (TrEMBL) Alternative ID(s) of Target Chain 12 BindingDB Target Chain Sequence 13 PDB ID(s) of Target Chain 13 UniProt (SwissProt) Recommended Name of Target Chain 13 UniProt (SwissProt) Entry Name of Target Chain 13 UniProt (SwissProt) Primary ID of Target Chain 13 UniProt (SwissProt) Secondary ID(s) of Target Chain 13 UniProt (SwissProt) Alternative ID(s) of Target Chain 13 UniProt (TrEMBL) Submitted Name of Target Chain 13 UniProt (TrEMBL) Entry Name of Target Chain 13 UniProt (TrEMBL) Primary ID of Target Chain 13 UniProt (TrEMBL) Secondary ID(s) of Target Chain 13 UniProt (TrEMBL) Alternative ID(s) of Target Chain 13 BindingDB Target Chain Sequence 14 PDB ID(s) of Target Chain 14 UniProt (SwissProt) Recommended Name of Target Chain 14 UniProt (SwissProt) Entry Name of Target Chain 14 UniProt (SwissProt) Primary ID of Target Chain 14 UniProt (SwissProt) Secondary ID(s) of Target Chain 14 UniProt (SwissProt) Alternative ID(s) of Target Chain 14 UniProt (TrEMBL) Submitted Name of Target Chain 14 UniProt (TrEMBL) Entry Name of Target Chain 14 UniProt (TrEMBL) Primary ID of Target Chain 14 UniProt (TrEMBL) Secondary ID(s) of Target Chain 14 UniProt (TrEMBL) Alternative ID(s) of Target Chain 14 BindingDB Target Chain Sequence 15 PDB ID(s) of Target Chain 15 UniProt (SwissProt) Recommended Name of Target Chain 15 UniProt (SwissProt) Entry Name of Target Chain 15 UniProt (SwissProt) Primary ID of Target Chain 15 UniProt (SwissProt) Secondary ID(s) of Target Chain 15 UniProt (SwissProt) Alternative ID(s) of Target Chain 15 UniProt (TrEMBL) Submitted Name of Target Chain 15 UniProt (TrEMBL) Entry Name of Target Chain 15 UniProt (TrEMBL) Primary ID of Target Chain 15 UniProt (TrEMBL) Secondary ID(s) of Target Chain 15 UniProt (TrEMBL) Alternative ID(s) of Target Chain 15 BindingDB Target Chain Sequence 16 PDB ID(s) of Target Chain 16 UniProt (SwissProt) Recommended Name of Target Chain 16 UniProt (SwissProt) Entry Name of Target Chain 16 UniProt (SwissProt) Primary ID of Target Chain 16 UniProt (SwissProt) Secondary ID(s) of Target Chain 16 UniProt (SwissProt) Alternative ID(s) of Target Chain 16 UniProt (TrEMBL) Submitted Name of Target Chain 16 UniProt (TrEMBL) Entry Name of Target Chain 16 UniProt (TrEMBL) Primary ID of Target Chain 16 UniProt (TrEMBL) Secondary ID(s) of Target Chain 16 UniProt (TrEMBL) Alternative ID(s) of Target Chain 16 BindingDB Target Chain Sequence 17 PDB ID(s) of Target Chain 17 UniProt (SwissProt) Recommended Name of Target Chain 17 UniProt (SwissProt) Entry Name of Target Chain 17 UniProt (SwissProt) Primary ID of Target Chain 17 UniProt (SwissProt) Secondary ID(s) of Target Chain 17 UniProt (SwissProt) Alternative ID(s) of Target Chain 17 UniProt (TrEMBL) Submitted Name of Target Chain 17 UniProt (TrEMBL) Entry Name of Target Chain 17 UniProt (TrEMBL) Primary ID of Target Chain 17 UniProt (TrEMBL) Secondary ID(s) of Target Chain 17 UniProt (TrEMBL) Alternative ID(s) of Target Chain 17 BindingDB Target Chain Sequence 18 PDB ID(s) of Target Chain 18 UniProt (SwissProt) Recommended Name of Target Chain 18 UniProt (SwissProt) Entry Name of Target Chain 18 UniProt (SwissProt) Primary ID of Target Chain 18 UniProt (SwissProt) Secondary ID(s) of Target Chain 18 UniProt (SwissProt) Alternative ID(s) of Target Chain 18 UniProt (TrEMBL) Submitted Name of Target Chain 18 UniProt (TrEMBL) Entry Name of Target Chain 18 UniProt (TrEMBL) Primary ID of Target Chain 18 UniProt (TrEMBL) Secondary ID(s) of Target Chain 18 UniProt (TrEMBL) Alternative ID(s) of Target Chain 18 BindingDB Target Chain Sequence 19 PDB ID(s) of Target Chain 19 UniProt (SwissProt) Recommended Name of Target Chain 19 UniProt (SwissProt) Entry Name of Target Chain 19 UniProt (SwissProt) Primary ID of Target Chain 19 UniProt (SwissProt) Secondary ID(s) of Target Chain 19 UniProt (SwissProt) Alternative ID(s) of Target Chain 19 UniProt (TrEMBL) Submitted Name of Target Chain 19 UniProt (TrEMBL) Entry Name of Target Chain 19 UniProt (TrEMBL) Primary ID of Target Chain 19 UniProt (TrEMBL) Secondary ID(s) of Target Chain 19 UniProt (TrEMBL) Alternative ID(s) of Target Chain 19 BindingDB Target Chain Sequence 20 PDB ID(s) of Target Chain 20 UniProt (SwissProt) Recommended Name of Target Chain 20 UniProt (SwissProt) Entry Name of Target Chain 20 UniProt (SwissProt) Primary ID of Target Chain 20 UniProt (SwissProt) Secondary ID(s) of Target Chain 20 UniProt (SwissProt) Alternative ID(s) of Target Chain 20 UniProt (TrEMBL) Submitted Name of Target Chain 20 UniProt (TrEMBL) Entry Name of Target Chain 20 UniProt (TrEMBL) Primary ID of Target Chain 20 UniProt (TrEMBL) Secondary ID(s) of Target Chain 20 UniProt (TrEMBL) Alternative ID(s) of Target Chain 20 BindingDB Target Chain Sequence 21 PDB ID(s) of Target Chain 21 UniProt (SwissProt) Recommended Name of Target Chain 21 UniProt (SwissProt) Entry Name of Target Chain 21 UniProt (SwissProt) Primary ID of Target Chain 21 UniProt (SwissProt) Secondary ID(s) of Target Chain 21 UniProt (SwissProt) Alternative ID(s) of Target Chain 21 UniProt (TrEMBL) Submitted Name of Target Chain 21 UniProt (TrEMBL) Entry Name of Target Chain 21 UniProt (TrEMBL) Primary ID of Target Chain 21 UniProt (TrEMBL) Secondary ID(s) of Target Chain 21 UniProt (TrEMBL) Alternative ID(s) of Target Chain 21 BindingDB Target Chain Sequence 22 PDB ID(s) of Target Chain 22 UniProt (SwissProt) Recommended Name of Target Chain 22 UniProt (SwissProt) Entry Name of Target Chain 22 UniProt (SwissProt) Primary ID of Target Chain 22 UniProt (SwissProt) Secondary ID(s) of Target Chain 22 UniProt (SwissProt) Alternative ID(s) of Target Chain 22 UniProt (TrEMBL) Submitted Name of Target Chain 22 UniProt (TrEMBL) Entry Name of Target Chain 22 UniProt (TrEMBL) Primary ID of Target Chain 22 UniProt (TrEMBL) Secondary ID(s) of Target Chain 22 UniProt (TrEMBL) Alternative ID(s) of Target Chain 22 BindingDB Target Chain Sequence 23 PDB ID(s) of Target Chain 23 UniProt (SwissProt) Recommended Name of Target Chain 23 UniProt (SwissProt) Entry Name of Target Chain 23 UniProt (SwissProt) Primary ID of Target Chain 23 UniProt (SwissProt) Secondary ID(s) of Target Chain 23 UniProt (SwissProt) Alternative ID(s) of Target Chain 23 UniProt (TrEMBL) Submitted Name of Target Chain 23 UniProt (TrEMBL) Entry Name of Target Chain 23 UniProt (TrEMBL) Primary ID of Target Chain 23 UniProt (TrEMBL) Secondary ID(s) of Target Chain 23 UniProt (TrEMBL) Alternative ID(s) of Target Chain 23 BindingDB Target Chain Sequence 24 PDB ID(s) of Target Chain 24 UniProt (SwissProt) Recommended Name of Target Chain 24 UniProt (SwissProt) Entry Name of Target Chain 24 UniProt (SwissProt) Primary ID of Target Chain 24 UniProt (SwissProt) Secondary ID(s) of Target Chain 24 UniProt (SwissProt) Alternative ID(s) of Target Chain 24 UniProt (TrEMBL) Submitted Name of Target Chain 24 UniProt (TrEMBL) Entry Name of Target Chain 24 UniProt (TrEMBL) Primary ID of Target Chain 24 UniProt (TrEMBL) Secondary ID(s) of Target Chain 24 UniProt (TrEMBL) Alternative ID(s) of Target Chain 24 BindingDB Target Chain Sequence 25 PDB ID(s) of Target Chain 25 UniProt (SwissProt) Recommended Name of Target Chain 25 UniProt (SwissProt) Entry Name of Target Chain 25 UniProt (SwissProt) Primary ID of Target Chain 25 UniProt (SwissProt) Secondary ID(s) of Target Chain 25 UniProt (SwissProt) Alternative ID(s) of Target Chain 25 UniProt (TrEMBL) Submitted Name of Target Chain 25 UniProt (TrEMBL) Entry Name of Target Chain 25 UniProt (TrEMBL) Primary ID of Target Chain 25 UniProt (TrEMBL) Secondary ID(s) of Target Chain 25 UniProt (TrEMBL) Alternative ID(s) of Target Chain 25 BindingDB Target Chain Sequence 26 PDB ID(s) of Target Chain 26 UniProt (SwissProt) Recommended Name of Target Chain 26 UniProt (SwissProt) Entry Name of Target Chain 26 UniProt (SwissProt) Primary ID of Target Chain 26 UniProt (SwissProt) Secondary ID(s) of Target Chain 26 UniProt (SwissProt) Alternative ID(s) of Target Chain 26 UniProt (TrEMBL) Submitted Name of Target Chain 26 UniProt (TrEMBL) Entry Name of Target Chain 26 UniProt (TrEMBL) Primary ID of Target Chain 26 UniProt (TrEMBL) Secondary ID(s) of Target Chain 26 UniProt (TrEMBL) Alternative ID(s) of Target Chain 26 BindingDB Target Chain Sequence 27 PDB ID(s) of Target Chain 27 UniProt (SwissProt) Recommended Name of Target Chain 27 UniProt (SwissProt) Entry Name of Target Chain 27 UniProt (SwissProt) Primary ID of Target Chain 27 UniProt (SwissProt) Secondary ID(s) of Target Chain 27 UniProt (SwissProt) Alternative ID(s) of Target Chain 27 UniProt (TrEMBL) Submitted Name of Target Chain 27 UniProt (TrEMBL) Entry Name of Target Chain 27 UniProt (TrEMBL) Primary ID of Target Chain 27 UniProt (TrEMBL) Secondary ID(s) of Target Chain 27 UniProt (TrEMBL) Alternative ID(s) of Target Chain 27 BindingDB Target Chain Sequence 28 PDB ID(s) of Target Chain 28 UniProt (SwissProt) Recommended Name of Target Chain 28 UniProt (SwissProt) Entry Name of Target Chain 28 UniProt (SwissProt) Primary ID of Target Chain 28 UniProt (SwissProt) Secondary ID(s) of Target Chain 28 UniProt (SwissProt) Alternative ID(s) of Target Chain 28 UniProt (TrEMBL) Submitted Name of Target Chain 28 UniProt (TrEMBL) Entry Name of Target Chain 28 UniProt (TrEMBL) Primary ID of Target Chain 28 UniProt (TrEMBL) Secondary ID(s) of Target Chain 28 UniProt (TrEMBL) Alternative ID(s) of Target Chain 28 BindingDB Target Chain Sequence 29 PDB ID(s) of Target Chain 29 UniProt (SwissProt) Recommended Name of Target Chain 29 UniProt (SwissProt) Entry Name of Target Chain 29 UniProt (SwissProt) Primary ID of Target Chain 29 UniProt (SwissProt) Secondary ID(s) of Target Chain 29 UniProt (SwissProt) Alternative ID(s) of Target Chain 29 UniProt (TrEMBL) Submitted Name of Target Chain 29 UniProt (TrEMBL) Entry Name of Target Chain 29 UniProt (TrEMBL) Primary ID of Target Chain 29 UniProt (TrEMBL) Secondary ID(s) of Target Chain 29 UniProt (TrEMBL) Alternative ID(s) of Target Chain 29 BindingDB Target Chain Sequence 30 PDB ID(s) of Target Chain 30 UniProt (SwissProt) Recommended Name of Target Chain 30 UniProt (SwissProt) Entry Name of Target Chain 30 UniProt (SwissProt) Primary ID of Target Chain 30 UniProt (SwissProt) Secondary ID(s) of Target Chain 30 UniProt (SwissProt) Alternative ID(s) of Target Chain 30 UniProt (TrEMBL) Submitted Name of Target Chain 30 UniProt (TrEMBL) Entry Name of Target Chain 30 UniProt (TrEMBL) Primary ID of Target Chain 30 UniProt (TrEMBL) Secondary ID(s) of Target Chain 30 UniProt (TrEMBL) Alternative ID(s) of Target Chain 30 BindingDB Target Chain Sequence 31 PDB ID(s) of Target Chain 31 UniProt (SwissProt) Recommended Name of Target Chain 31 UniProt (SwissProt) Entry Name of Target Chain 31 UniProt (SwissProt) Primary ID of Target Chain 31 UniProt (SwissProt) Secondary ID(s) of Target Chain 31 UniProt (SwissProt) Alternative ID(s) of Target Chain 31 UniProt (TrEMBL) Submitted Name of Target Chain 31 UniProt (TrEMBL) Entry Name of Target Chain 31 UniProt (TrEMBL) Primary ID of Target Chain 31 UniProt (TrEMBL) Secondary ID(s) of Target Chain 31 UniProt (TrEMBL) Alternative ID(s) of Target Chain 31 BindingDB Target Chain Sequence 32 PDB ID(s) of Target Chain 32 UniProt (SwissProt) Recommended Name of Target Chain 32 UniProt (SwissProt) Entry Name of Target Chain 32 UniProt (SwissProt) Primary ID of Target Chain 32 UniProt (SwissProt) Secondary ID(s) of Target Chain 32 UniProt (SwissProt) Alternative ID(s) of Target Chain 32 UniProt (TrEMBL) Submitted Name of Target Chain 32 UniProt (TrEMBL) Entry Name of Target Chain 32 UniProt (TrEMBL) Primary ID of Target Chain 32 UniProt (TrEMBL) Secondary ID(s) of Target Chain 32 UniProt (TrEMBL) Alternative ID(s) of Target Chain 32 BindingDB Target Chain Sequence 33 PDB ID(s) of Target Chain 33 UniProt (SwissProt) Recommended Name of Target Chain 33 UniProt (SwissProt) Entry Name of Target Chain 33 UniProt (SwissProt) Primary ID of Target Chain 33 UniProt (SwissProt) Secondary ID(s) of Target Chain 33 UniProt (SwissProt) Alternative ID(s) of Target Chain 33 UniProt (TrEMBL) Submitted Name of Target Chain 33 UniProt (TrEMBL) Entry Name of Target Chain 33 UniProt (TrEMBL) Primary ID of Target Chain 33 UniProt (TrEMBL) Secondary ID(s) of Target Chain 33 UniProt (TrEMBL) Alternative ID(s) of Target Chain 33 BindingDB Target Chain Sequence 34 PDB ID(s) of Target Chain 34 UniProt (SwissProt) Recommended Name of Target Chain 34 UniProt (SwissProt) Entry Name of Target Chain 34 UniProt (SwissProt) Primary ID of Target Chain 34 UniProt (SwissProt) Secondary ID(s) of Target Chain 34 UniProt (SwissProt) Alternative ID(s) of Target Chain 34 UniProt (TrEMBL) Submitted Name of Target Chain 34 UniProt (TrEMBL) Entry Name of Target Chain 34 UniProt (TrEMBL) Primary ID of Target Chain 34 UniProt (TrEMBL) Secondary ID(s) of Target Chain 34 UniProt (TrEMBL) Alternative ID(s) of Target Chain 34 BindingDB Target Chain Sequence 35 PDB ID(s) of Target Chain 35 UniProt (SwissProt) Recommended Name of Target Chain 35 UniProt (SwissProt) Entry Name of Target Chain 35 UniProt (SwissProt) Primary ID of Target Chain 35 UniProt (SwissProt) Secondary ID(s) of Target Chain 35 UniProt (SwissProt) Alternative ID(s) of Target Chain 35 UniProt (TrEMBL) Submitted Name of Target Chain 35 UniProt (TrEMBL) Entry Name of Target Chain 35 UniProt (TrEMBL) Primary ID of Target Chain 35 UniProt (TrEMBL) Secondary ID(s) of Target Chain 35 UniProt (TrEMBL) Alternative ID(s) of Target Chain 35 BindingDB Target Chain Sequence 36 PDB ID(s) of Target Chain 36 UniProt (SwissProt) Recommended Name of Target Chain 36 UniProt (SwissProt) Entry Name of Target Chain 36 UniProt (SwissProt) Primary ID of Target Chain 36 UniProt (SwissProt) Secondary ID(s) of Target Chain 36 UniProt (SwissProt) Alternative ID(s) of Target Chain 36 UniProt (TrEMBL) Submitted Name of Target Chain 36 UniProt (TrEMBL) Entry Name of Target Chain 36 UniProt (TrEMBL) Primary ID of Target Chain 36 UniProt (TrEMBL) Secondary ID(s) of Target Chain 36 UniProt (TrEMBL) Alternative ID(s) of Target Chain 36 BindingDB Target Chain Sequence 37 PDB ID(s) of Target Chain 37 UniProt (SwissProt) Recommended Name of Target Chain 37 UniProt (SwissProt) Entry Name of Target Chain 37 UniProt (SwissProt) Primary ID of Target Chain 37 UniProt (SwissProt) Secondary ID(s) of Target Chain 37 UniProt (SwissProt) Alternative ID(s) of Target Chain 37 UniProt (TrEMBL) Submitted Name of Target Chain 37 UniProt (TrEMBL) Entry Name of Target Chain 37 UniProt (TrEMBL) Primary ID of Target Chain 37 UniProt (TrEMBL) Secondary ID(s) of Target Chain 37 UniProt (TrEMBL) Alternative ID(s) of Target Chain 37 BindingDB Target Chain Sequence 38 PDB ID(s) of Target Chain 38 UniProt (SwissProt) Recommended Name of Target Chain 38 UniProt (SwissProt) Entry Name of Target Chain 38 UniProt (SwissProt) Primary ID of Target Chain 38 UniProt (SwissProt) Secondary ID(s) of Target Chain 38 UniProt (SwissProt) Alternative ID(s) of Target Chain 38 UniProt (TrEMBL) Submitted Name of Target Chain 38 UniProt (TrEMBL) Entry Name of Target Chain 38 UniProt (TrEMBL) Primary ID of Target Chain 38 UniProt (TrEMBL) Secondary ID(s) of Target Chain 38 UniProt (TrEMBL) Alternative ID(s) of Target Chain 38 BindingDB Target Chain Sequence 39 PDB ID(s) of Target Chain 39 UniProt (SwissProt) Recommended Name of Target Chain 39 UniProt (SwissProt) Entry Name of Target Chain 39 UniProt (SwissProt) Primary ID of Target Chain 39 UniProt (SwissProt) Secondary ID(s) of Target Chain 39 UniProt (SwissProt) Alternative ID(s) of Target Chain 39 UniProt (TrEMBL) Submitted Name of Target Chain 39 UniProt (TrEMBL) Entry Name of Target Chain 39 UniProt (TrEMBL) Primary ID of Target Chain 39 UniProt (TrEMBL) Secondary ID(s) of Target Chain 39 UniProt (TrEMBL) Alternative ID(s) of Target Chain 39 BindingDB Target Chain Sequence 40 PDB ID(s) of Target Chain 40 UniProt (SwissProt) Recommended Name of Target Chain 40 UniProt (SwissProt) Entry Name of Target Chain 40 UniProt (SwissProt) Primary ID of Target Chain 40 UniProt (SwissProt) Secondary ID(s) of Target Chain 40 UniProt (SwissProt) Alternative ID(s) of Target Chain 40 UniProt (TrEMBL) Submitted Name of Target Chain 40 UniProt (TrEMBL) Entry Name of Target Chain 40 UniProt (TrEMBL) Primary ID of Target Chain 40 UniProt (TrEMBL) Secondary ID(s) of Target Chain 40 UniProt (TrEMBL) Alternative ID(s) of Target Chain 40 BindingDB Target Chain Sequence 41 PDB ID(s) of Target Chain 41 UniProt (SwissProt) Recommended Name of Target Chain 41 UniProt (SwissProt) Entry Name of Target Chain 41 UniProt (SwissProt) Primary ID of Target Chain 41 UniProt (SwissProt) Secondary ID(s) of Target Chain 41 UniProt (SwissProt) Alternative ID(s) of Target Chain 41 UniProt (TrEMBL) Submitted Name of Target Chain 41 UniProt (TrEMBL) Entry Name of Target Chain 41 UniProt (TrEMBL) Primary ID of Target Chain 41 UniProt (TrEMBL) Secondary ID(s) of Target Chain 41 UniProt (TrEMBL) Alternative ID(s) of Target Chain 41 BindingDB Target Chain Sequence 42 PDB ID(s) of Target Chain 42 UniProt (SwissProt) Recommended Name of Target Chain 42 UniProt (SwissProt) Entry Name of Target Chain 42 UniProt (SwissProt) Primary ID of Target Chain 42 UniProt (SwissProt) Secondary ID(s) of Target Chain 42 UniProt (SwissProt) Alternative ID(s) of Target Chain 42 UniProt (TrEMBL) Submitted Name of Target Chain 42 UniProt (TrEMBL) Entry Name of Target Chain 42 UniProt (TrEMBL) Primary ID of Target Chain 42 UniProt (TrEMBL) Secondary ID(s) of Target Chain 42 UniProt (TrEMBL) Alternative ID(s) of Target Chain 42 BindingDB Target Chain Sequence 43 PDB ID(s) of Target Chain 43 UniProt (SwissProt) Recommended Name of Target Chain 43 UniProt (SwissProt) Entry Name of Target Chain 43 UniProt (SwissProt) Primary ID of Target Chain 43 UniProt (SwissProt) Secondary ID(s) of Target Chain 43 UniProt (SwissProt) Alternative ID(s) of Target Chain 43 UniProt (TrEMBL) Submitted Name of Target Chain 43 UniProt (TrEMBL) Entry Name of Target Chain 43 UniProt (TrEMBL) Primary ID of Target Chain 43 UniProt (TrEMBL) Secondary ID(s) of Target Chain 43 UniProt (TrEMBL) Alternative ID(s) of Target Chain 43 BindingDB Target Chain Sequence 44 PDB ID(s) of Target Chain 44 UniProt (SwissProt) Recommended Name of Target Chain 44 UniProt (SwissProt) Entry Name of Target Chain 44 UniProt (SwissProt) Primary ID of Target Chain 44 UniProt (SwissProt) Secondary ID(s) of Target Chain 44 UniProt (SwissProt) Alternative ID(s) of Target Chain 44 UniProt (TrEMBL) Submitted Name of Target Chain 44 UniProt (TrEMBL) Entry Name of Target Chain 44 UniProt (TrEMBL) Primary ID of Target Chain 44 UniProt (TrEMBL) Secondary ID(s) of Target Chain 44 UniProt (TrEMBL) Alternative ID(s) of Target Chain 44 BindingDB Target Chain Sequence 45 PDB ID(s) of Target Chain 45 UniProt (SwissProt) Recommended Name of Target Chain 45 UniProt (SwissProt) Entry Name of Target Chain 45 UniProt (SwissProt) Primary ID of Target Chain 45 UniProt (SwissProt) Secondary ID(s) of Target Chain 45 UniProt (SwissProt) Alternative ID(s) of Target Chain 45 UniProt (TrEMBL) Submitted Name of Target Chain 45 UniProt (TrEMBL) Entry Name of Target Chain 45 UniProt (TrEMBL) Primary ID of Target Chain 45 UniProt (TrEMBL) Secondary ID(s) of Target Chain 45 UniProt (TrEMBL) Alternative ID(s) of Target Chain 45 BindingDB Target Chain Sequence 46 PDB ID(s) of Target Chain 46 UniProt (SwissProt) Recommended Name of Target Chain 46 UniProt (SwissProt) Entry Name of Target Chain 46 UniProt (SwissProt) Primary ID of Target Chain 46 UniProt (SwissProt) Secondary ID(s) of Target Chain 46 UniProt (SwissProt) Alternative ID(s) of Target Chain 46 UniProt (TrEMBL) Submitted Name of Target Chain 46 UniProt (TrEMBL) Entry Name of Target Chain 46 UniProt (TrEMBL) Primary ID of Target Chain 46 UniProt (TrEMBL) Secondary ID(s) of Target Chain 46 UniProt (TrEMBL) Alternative ID(s) of Target Chain 46 BindingDB Target Chain Sequence 47 PDB ID(s) of Target Chain 47 UniProt (SwissProt) Recommended Name of Target Chain 47 UniProt (SwissProt) Entry Name of Target Chain 47 UniProt (SwissProt) Primary ID of Target Chain 47 UniProt (SwissProt) Secondary ID(s) of Target Chain 47 UniProt (SwissProt) Alternative ID(s) of Target Chain 47 UniProt (TrEMBL) Submitted Name of Target Chain 47 UniProt (TrEMBL) Entry Name of Target Chain 47 UniProt (TrEMBL) Primary ID of Target Chain 47 UniProt (TrEMBL) Secondary ID(s) of Target Chain 47 UniProt (TrEMBL) Alternative ID(s) of Target Chain 47 BindingDB Target Chain Sequence 48 PDB ID(s) of Target Chain 48 UniProt (SwissProt) Recommended Name of Target Chain 48 UniProt (SwissProt) Entry Name of Target Chain 48 UniProt (SwissProt) Primary ID of Target Chain 48 UniProt (SwissProt) Secondary ID(s) of Target Chain 48 UniProt (SwissProt) Alternative ID(s) of Target Chain 48 UniProt (TrEMBL) Submitted Name of Target Chain 48 UniProt (TrEMBL) Entry Name of Target Chain 48 UniProt (TrEMBL) Primary ID of Target Chain 48 UniProt (TrEMBL) Secondary ID(s) of Target Chain 48 UniProt (TrEMBL) Alternative ID(s) of Target Chain 48 BindingDB Target Chain Sequence 49 PDB ID(s) of Target Chain 49 UniProt (SwissProt) Recommended Name of Target Chain 49 UniProt (SwissProt) Entry Name of Target Chain 49 UniProt (SwissProt) Primary ID of Target Chain 49 UniProt (SwissProt) Secondary ID(s) of Target Chain 49 UniProt (SwissProt) Alternative ID(s) of Target Chain 49 UniProt (TrEMBL) Submitted Name of Target Chain 49 UniProt (TrEMBL) Entry Name of Target Chain 49 UniProt (TrEMBL) Primary ID of Target Chain 49 UniProt (TrEMBL) Secondary ID(s) of Target Chain 49 UniProt (TrEMBL) Alternative ID(s) of Target Chain 49 BindingDB Target Chain Sequence 50 PDB ID(s) of Target Chain 50 UniProt (SwissProt) Recommended Name of Target Chain 50 UniProt (SwissProt) Entry Name of Target Chain 50 UniProt (SwissProt) Primary ID of Target Chain 50 UniProt (SwissProt) Secondary ID(s) of Target Chain 50 UniProt (SwissProt) Alternative ID(s) of Target Chain 50 UniProt (TrEMBL) Submitted Name of Target Chain 50 UniProt (TrEMBL) Entry Name of Target Chain 50 UniProt (TrEMBL) Primary ID of Target Chain 50 UniProt (TrEMBL) Secondary ID(s) of Target Chain 50 UniProt (TrEMBL) Alternative ID(s) of Target Chain 50 396344 C=CCOCCOC(=O)[C@@H]1CCCCN1C(=O)[C@H](c2cc(OC)c(OCC=C)c(OC)c2)C3CCCCC3 InChI=1S/C30H43NO7/c1-5-16-36-18-19-38-30(33)24-14-10-11-15-31(24)29(32)27(22-12-8-7-9-13-22)23-20-25(34-3)28(37-17-6-2)26(21-23)35-4/h5-6,20-22,24,27H,1-2,7-19H2,3-4H3 MIALGCWAXUGHIN-UHFFFAOYSA-N 790513 US20260034106, Compound p4(3,1) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 3159 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790513 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790513&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396345 COc1cc2cc(OC)c1OC/C=C/COCCOC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C28H39NO7/c1-32-23-18-21-19-24(33-2)26(23)35-15-9-8-14-34-16-17-36-28(31)22-12-6-7-13-29(22)27(30)25(21)20-10-4-3-5-11-20/h8-9,18-20,22,25H,3-7,10-17H2,1-2H3 IJBSWRPOQSCZFA-UHFFFAOYSA-N 790880 US20260034106, Compound p5(3,1)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 386 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790880 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790880&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search A1IN2 9GQ4 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396346 C=CCOC[C@H](C)COc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](C)CC=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C34H51NO7/c1-7-14-25(4)42-34(37)28-17-12-13-18-35(28)33(36)31(26-15-10-9-11-16-26)27-20-29(38-5)32(39-6)30(21-27)41-23-24(3)22-40-19-8-2/h7-8,20-21,24-26,28,31H,1-2,9-19,22-23H2,3-6H3 XPFBKNKZPYOQEW-UHFFFAOYSA-N 790881 US20260034106, Compound m4(6,11) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 1311 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790881 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790881&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396347 COc1cc2cc(c1OC)OC[C@@H](C)COC/C=C/C[C@@H](C)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C32H47NO7/c1-22-20-38-17-11-9-12-23(2)40-32(35)26-15-8-10-16-33(26)31(34)29(24-13-6-5-7-14-24)25-18-27(36-3)30(37-4)28(19-25)39-21-22/h9,11,18-19,22-24,26,29H,5-8,10,12-17,20-21H2,1-4H3 QRDJRNRANMCJIJ-UHFFFAOYSA-N 790882 US20260034106, Compound m5(6,11)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 108 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790882 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790882&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396348 C=CCOCCCOc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](C)[C@H](C)C=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C34H51NO7/c1-7-19-40-20-14-21-41-30-23-27(22-29(38-5)32(30)39-6)31(26-15-10-9-11-16-26)33(36)35-18-13-12-17-28(35)34(37)42-25(4)24(3)8-2/h7-8,22-26,28,31H,1-2,9-21H2,3-6H3 MKQFOLPQXKCHDI-UHFFFAOYSA-N 790883 US20260034106, Compound m4(10,4) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 1650 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790883 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790883&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396349 COc1cc2cc(c1OC)OCCCOC/C=C/[C@@H](C)[C@@H](C)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C32H47NO7/c1-22-12-10-17-38-18-11-19-39-28-21-25(20-27(36-3)30(28)37-4)29(24-13-6-5-7-14-24)31(34)33-16-9-8-15-26(33)32(35)40-23(22)2/h10,12,20-24,26,29H,5-9,11,13-19H2,1-4H3 KXJVTUYDFOMJIN-UHFFFAOYSA-N 790884 US20260034106, Compound m5(10,4)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 79.0 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790884 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790884&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396350 C=CCOCCOc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](C)[C@H](C)C=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C33H49NO7/c1-7-18-39-19-20-40-29-22-26(21-28(37-5)31(29)38-6)30(25-14-10-9-11-15-25)32(35)34-17-13-12-16-27(34)33(36)41-24(4)23(3)8-2/h7-8,21-25,27,30H,1-2,9-20H2,3-6H3 SABDNBCOMQGRRI-UHFFFAOYSA-N 790885 US20260034106, Compound m4(10,3) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 2143 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790885 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790885&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396351 COc1cc2cc(c1OC)OCCOC/C=C/[C@@H](C)[C@@H](C)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C31H45NO7/c1-21-11-10-16-37-17-18-38-27-20-24(19-26(35-3)29(27)36-4)28(23-12-6-5-7-13-23)30(33)32-15-9-8-14-25(32)31(34)39-22(21)2/h10-11,19-23,25,28H,5-9,12-18H2,1-4H3 IAKNHKGCDSUWEK-UHFFFAOYSA-N 790886 US20260034106, Compound m5(10,3)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 151 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790886 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790886&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396352 C=CCOCCOc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](C)[C@@H](C)C=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C33H49NO7/c1-7-18-39-19-20-40-29-22-26(21-28(37-5)31(29)38-6)30(25-14-10-9-11-15-25)32(35)34-17-13-12-16-27(34)33(36)41-24(4)23(3)8-2/h7-8,21-25,27,30H,1-2,9-20H2,3-6H3 SABDNBCOMQGRRI-UHFFFAOYSA-N 790887 US20260034106, Compound m4(9,3) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 553 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790887 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790887&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396353 COc1cc2cc(c1OC)OCCOC/C=C/[C@H](C)[C@@H](C)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C31H45NO7/c1-21-11-10-16-37-17-18-38-27-20-24(19-26(35-3)29(27)36-4)28(23-12-6-5-7-13-23)30(33)32-15-9-8-14-25(32)31(34)39-22(21)2/h10-11,19-23,25,28H,5-9,12-18H2,1-4H3 IAKNHKGCDSUWEK-UHFFFAOYSA-N 790888 US20260034106, Compound m5(9,3)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 123 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790888 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790888&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396354 C=CCO[C@@H](C)COc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](C)[C@@H](C)C=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C34H51NO7/c1-8-19-40-24(4)22-41-30-21-27(20-29(38-6)32(30)39-7)31(26-15-11-10-12-16-26)33(36)35-18-14-13-17-28(35)34(37)42-25(5)23(3)9-2/h8-9,20-21,23-26,28,31H,1-2,10-19,22H2,3-7H3 JFYJUFYPHTUFST-UHFFFAOYSA-N 790889 US20260034106, Compound m4(9,5) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 1581 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790889 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790889&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396355 COc1cc2cc(c1OC)OC[C@H](C)OC/C=C/[C@H](C)[C@@H](C)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C32H47NO7/c1-21-12-11-17-38-22(2)20-39-28-19-25(18-27(36-4)30(28)37-5)29(24-13-7-6-8-14-24)31(34)33-16-10-9-15-26(33)32(35)40-23(21)3/h11-12,18-19,21-24,26,29H,6-10,13-17,20H2,1-5H3 ZVHWLQVCRWWNGD-UHFFFAOYSA-N 790890 US20260034106, Compound m5(9,5)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 182 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790890 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790890&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396356 C=CCCOCCCOc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](C)[C@@H](C)C=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C35H53NO7/c1-7-9-20-41-21-15-22-42-31-24-28(23-30(39-5)33(31)40-6)32(27-16-11-10-12-17-27)34(37)36-19-14-13-18-29(36)35(38)43-26(4)25(3)8-2/h7-8,23-27,29,32H,1-2,9-22H2,3-6H3 LUNSZVYUEHINAT-UHFFFAOYSA-N 790891 US20260034106, Compound m4(9,4) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 846 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790891 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790891&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396357 COc1cc2cc(c1OC)OCCCOC/C=C/[C@H](C)[C@@H](C)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C32H47NO7/c1-22-12-10-17-38-18-11-19-39-28-21-25(20-27(36-3)30(28)37-4)29(24-13-6-5-7-14-24)31(34)33-16-9-8-15-26(33)32(35)40-23(22)2/h10,12,20-24,26,29H,5-9,11,13-19H2,1-4H3 KXJVTUYDFOMJIN-UHFFFAOYSA-N 790892 US20260034106, Compound m5(9,4)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 295 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790892 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790892&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396358 C=CCOC[C@H](C)COc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](C)[C@@H](C)C=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C35H53NO7/c1-8-19-41-22-24(3)23-42-31-21-28(20-30(39-6)33(31)40-7)32(27-15-11-10-12-16-27)34(37)36-18-14-13-17-29(36)35(38)43-26(5)25(4)9-2/h8-9,20-21,24-27,29,32H,1-2,10-19,22-23H2,3-7H3 AUVNTOFFANVRLK-UHFFFAOYSA-N 790893 US20260034106, Compound m4(9,11) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 1331 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790893 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790893&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396359 COc1cc2cc(c1OC)OC[C@@H](C)COC/C=C/[C@H](C)[C@@H](C)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C33H49NO7/c1-22-20-39-17-11-12-23(2)24(3)41-33(36)27-15-9-10-16-34(27)32(35)30(25-13-7-6-8-14-25)26-18-28(37-4)31(38-5)29(19-26)40-21-22/h11-12,18-19,22-25,27,30H,6-10,13-17,20-21H2,1-5H3 QARZPYMNOUYIRP-UHFFFAOYSA-N 790894 US20260034106, Compound m5(9,11)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 648 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790894 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790894&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396360 C=CCO[C@H](C)CCOc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](C)[C@@H](C)C=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C35H53NO7/c1-8-20-41-25(4)18-21-42-31-23-28(22-30(39-6)33(31)40-7)32(27-15-11-10-12-16-27)34(37)36-19-14-13-17-29(36)35(38)43-26(5)24(3)9-2/h8-9,22-27,29,32H,1-2,10-21H2,3-7H3 BPXCAFMDUCYRNS-UHFFFAOYSA-N 790895 US20260034106, Compound m4(9,13) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 732 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790895 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790895&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396361 COc1cc2cc(c1OC)OCC[C@@H](C)OC/C=C/[C@H](C)[C@@H](C)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C33H49NO7/c1-22-12-11-18-39-23(2)16-19-40-29-21-26(20-28(37-4)31(29)38-5)30(25-13-7-6-8-14-25)32(35)34-17-10-9-15-27(34)33(36)41-24(22)3/h11-12,20-25,27,30H,6-10,13-19H2,1-5H3 HYCLKSQMVFQGFO-UHFFFAOYSA-N 790896 US20260034106, Compound m5(9,13)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 253 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790896 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790896&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396362 C=CCO[C@@H](C)CCOc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](C)[C@@H](C)C=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C35H53NO7/c1-8-20-41-25(4)18-21-42-31-23-28(22-30(39-6)33(31)40-7)32(27-15-11-10-12-16-27)34(37)36-19-14-13-17-29(36)35(38)43-26(5)24(3)9-2/h8-9,22-27,29,32H,1-2,10-21H2,3-7H3 BPXCAFMDUCYRNS-UHFFFAOYSA-N 790897 US20260034106, Compound m4(9,14) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 762 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790897 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790897&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396363 COc1cc2cc(c1OC)OCC[C@H](C)OC/C=C/[C@H](C)[C@@H](C)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C33H49NO7/c1-22-12-11-18-39-23(2)16-19-40-29-21-26(20-28(37-4)31(29)38-5)30(25-13-7-6-8-14-25)32(35)34-17-10-9-15-27(34)33(36)41-24(22)3/h11-12,20-25,27,30H,6-10,13-19H2,1-5H3 HYCLKSQMVFQGFO-UHFFFAOYSA-N 790898 US20260034106, Compound m5(9,14)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 297 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790898 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790898&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396364 C=CCOC[C@@H](C)Oc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](C)[C@H](C)C=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C34H51NO7/c1-8-19-40-22-24(4)41-30-21-27(20-29(38-6)32(30)39-7)31(26-15-11-10-12-16-26)33(36)35-18-14-13-17-28(35)34(37)42-25(5)23(3)9-2/h8-9,20-21,23-26,28,31H,1-2,10-19,22H2,3-7H3 HWVIGZCRLAJZRW-UHFFFAOYSA-N 790899 US20260034106, Compound m4(10,9) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 1770 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790899 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790899&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396365 COc1cc2cc(c1OC)O[C@H](C)COC/C=C/[C@@H](C)[C@@H](C)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C32H47NO7/c1-21-12-11-17-38-20-22(2)39-28-19-25(18-27(36-4)30(28)37-5)29(24-13-7-6-8-14-24)31(34)33-16-10-9-15-26(33)32(35)40-23(21)3/h11-12,18-19,21-24,26,29H,6-10,13-17,20H2,1-5H3 FWJXOAVBANRSGP-UHFFFAOYSA-N 790900 US20260034106, Compound m5(10,9)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 498 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790900 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790900&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396366 C=CCOC[C@H](C)Oc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](C)[C@H](C)C=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C34H51NO7/c1-8-19-40-22-24(4)41-30-21-27(20-29(38-6)32(30)39-7)31(26-15-11-10-12-16-26)33(36)35-18-14-13-17-28(35)34(37)42-25(5)23(3)9-2/h8-9,20-21,23-26,28,31H,1-2,10-19,22H2,3-7H3 HWVIGZCRLAJZRW-UHFFFAOYSA-N 790901 US20260034106, Compound m4(10,10) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 1200 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790901 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790901&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396367 COc1cc2cc(c1OC)O[C@@H](C)COC/C=C/[C@@H](C)[C@@H](C)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C32H47NO7/c1-21-12-11-17-38-20-22(2)39-28-19-25(18-27(36-4)30(28)37-5)29(24-13-7-6-8-14-24)31(34)33-16-10-9-15-26(33)32(35)40-23(21)3/h11-12,18-19,21-24,26,29H,6-10,13-17,20H2,1-5H3 FWJXOAVBANRSGP-UHFFFAOYSA-N 790902 US20260034106, Compound m5(10,10)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 45.0 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790902 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790902&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396368 C=CCOC[C@H](C)Oc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](C)[C@@H](C)C=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C34H51NO7/c1-8-19-40-22-24(4)41-30-21-27(20-29(38-6)32(30)39-7)31(26-15-11-10-12-16-26)33(36)35-18-14-13-17-28(35)34(37)42-25(5)23(3)9-2/h8-9,20-21,23-26,28,31H,1-2,10-19,22H2,3-7H3 HWVIGZCRLAJZRW-UHFFFAOYSA-N 790903 US20260034106, Compound M4(9,10) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 930 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790903 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790903&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396369 COc1cc2cc(c1OC)O[C@@H](C)COC/C=C/[C@H](C)[C@@H](C)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C32H47NO7/c1-21-12-11-17-38-20-22(2)39-28-19-25(18-27(36-4)30(28)37-5)29(24-13-7-6-8-14-24)31(34)33-16-10-9-15-26(33)32(35)40-23(21)3/h11-12,18-19,21-24,26,29H,6-10,13-17,20H2,1-5H3 FWJXOAVBANRSGP-UHFFFAOYSA-N 790904 US20260034106, Compound m5(9,10)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 151 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790904 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790904&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396370 C=CCOCC[C@@H](C)Oc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](C)CC=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C34H51NO7/c1-7-14-24(3)42-34(37)28-17-12-13-19-35(28)33(36)31(26-15-10-9-11-16-26)27-22-29(38-5)32(39-6)30(23-27)41-25(4)18-21-40-20-8-2/h7-8,22-26,28,31H,1-2,9-21H2,3-6H3 CVDMUZYJIDKZQU-UHFFFAOYSA-N 790905 US20260034106, Compound m4(6,17) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 2107 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790905 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790905&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396371 COc1cc2cc(c1OC)O[C@@H](C)CCOC/C=C/C[C@@H](C)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C32H47NO7/c1-22-12-9-11-18-38-19-16-23(2)39-28-21-25(20-27(36-3)30(28)37-4)29(24-13-6-5-7-14-24)31(34)33-17-10-8-15-26(33)32(35)40-22/h9,11,20-24,26,29H,5-8,10,12-19H2,1-4H3 OIMYTGXPNQEVDH-UHFFFAOYSA-N 790906 US20260034106, Compound m5(6,17)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 109 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790906 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790906&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396372 C=CCOCC[C@@H](C)Oc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](C)[C@H](C)C=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C35H53NO7/c1-8-20-41-21-18-25(4)42-31-23-28(22-30(39-6)33(31)40-7)32(27-15-11-10-12-16-27)34(37)36-19-14-13-17-29(36)35(38)43-26(5)24(3)9-2/h8-9,22-27,29,32H,1-2,10-21H2,3-7H3 LXHBBKGMBRFWJS-UHFFFAOYSA-N 790907 US20260034106, Compound m4(10,17) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 2454 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790907 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790907&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396373 COc1cc2cc(c1OC)O[C@@H](C)CCOC/C=C/[C@@H](C)[C@@H](C)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C33H49NO7/c1-22-12-11-18-39-19-16-23(2)40-29-21-26(20-28(37-4)31(29)38-5)30(25-13-7-6-8-14-25)32(35)34-17-10-9-15-27(34)33(36)41-24(22)3/h11-12,20-25,27,30H,6-10,13-19H2,1-5H3 JMMGXUUZDWQOCT-UHFFFAOYSA-N 790908 US20260034106, Compound m5(10,17)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 91.0 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790908 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790908&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396374 C=CCOCC[C@H](C)Oc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](C)[C@@H](C)C=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C35H53NO7/c1-8-20-41-21-18-25(4)42-31-23-28(22-30(39-6)33(31)40-7)32(27-15-11-10-12-16-27)34(37)36-19-14-13-17-29(36)35(38)43-26(5)24(3)9-2/h8-9,22-27,29,32H,1-2,10-21H2,3-7H3 LXHBBKGMBRFWJS-UHFFFAOYSA-N 790909 US20260034106, Compound m4(9,18) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 1573 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790909 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790909&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396375 COc1cc2cc(c1OC)O[C@@H](C)CCOC/C=C/[C@H](C)[C@@H](C)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C33H49NO7/c1-22-12-11-18-39-19-16-23(2)40-29-21-26(20-28(37-4)31(29)38-5)30(25-13-7-6-8-14-25)32(35)34-17-10-9-15-27(34)33(36)41-24(22)3/h11-12,20-25,27,30H,6-10,13-19H2,1-5H3 JMMGXUUZDWQOCT-UHFFFAOYSA-N 790910 US20260034106, Compound m5(9,18)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 451 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790910 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790910&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396376 C=CCCOC(=O)[C@@H]1CCCCN1C(=O)[C@H](c1cc(OC)c(OC)c(OCCCOCC=C)c1)C1CCCCC1 InChI=1S/C32H47NO7/c1-5-7-20-40-32(35)26-16-11-12-17-33(26)31(34)29(24-14-9-8-10-15-24)25-22-27(36-3)30(37-4)28(23-25)39-21-13-19-38-18-6-2/h5-6,22-24,26,29H,1-2,7-21H2,3-4H3 SONMNSXSWYPLAX-UHFFFAOYSA-N 790911 US20260034106, Compound m4(2,4) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 559 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790911 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790911&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396377 COc1cc2cc(c1OC)OCCCOC/C=C/CCOC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C30H43NO7/c1-34-25-20-23-21-26(28(25)35-2)37-19-11-17-36-16-9-4-10-18-38-30(33)24-14-7-8-15-31(24)29(32)27(23)22-12-5-3-6-13-22/h4,9,20-22,24,27H,3,5-8,10-19H2,1-2H3 OTNSABIMHVQNCJ-UHFFFAOYSA-N 790912 US20260034106, Compound m5(2,4)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 102 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790912 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790912&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search A1IOA 9GQD 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396378 C=CCCOC(=O)[C@@H]1CCCCN1C(=O)[C@H](c1cc(OC)c(OC)c(OCCOCC=C)c1)C1CCCCC1 InChI=1S/C31H45NO7/c1-5-7-18-39-31(34)25-15-11-12-16-32(25)30(33)28(23-13-9-8-10-14-23)24-21-26(35-3)29(36-4)27(22-24)38-20-19-37-17-6-2/h5-6,21-23,25,28H,1-2,7-20H2,3-4H3 FFNOQKAPTOVRLR-UHFFFAOYSA-N 790913 US20260034106, Compound m4(2,3) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 453 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790913 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790913&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396379 COc1cc2cc(c1OC)OCCOC/C=C/CCOC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C29H41NO7/c1-33-24-19-22-20-25(27(24)34-2)36-18-17-35-15-9-4-10-16-37-29(32)23-13-7-8-14-30(23)28(31)26(22)21-11-5-3-6-12-21/h4,9,19-21,23,26H,3,5-8,10-18H2,1-2H3 PNDVORSWFXFXQZ-UHFFFAOYSA-N 790914 US20260034106, Compound m5(2,3)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 86.0 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790914 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790914&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search A1IOC 9GQF 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396380 C=CCOCCOc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](C)CC=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C32H47NO7/c1-6-13-23(3)40-32(35)26-16-11-12-17-33(26)31(34)29(24-14-9-8-10-15-24)25-21-27(36-4)30(37-5)28(22-25)39-20-19-38-18-7-2/h6-7,21-24,26,29H,1-2,8-20H2,3-5H3 QFUDBPPYSCYMOB-UHFFFAOYSA-N 790915 US20260034106, Compound m4(6,3) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 1013 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790915 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790915&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396381 COc1cc2cc(c1OC)OCCOC/C=C/C[C@@H](C)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C30H43NO7/c1-21-11-8-10-16-36-17-18-37-26-20-23(19-25(34-2)28(26)35-3)27(22-12-5-4-6-13-22)29(32)31-15-9-7-14-24(31)30(33)38-21/h8,10,19-22,24,27H,4-7,9,11-18H2,1-3H3 CTNGZIYVWIPNFF-UHFFFAOYSA-N 790916 US20260034106, Compound m5(6,3)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 56.0 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790916 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790916&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396382 C=CCOC[C@H](C)Oc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](CO)CC=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C33H49NO8/c1-6-13-26(21-35)42-33(37)27-16-11-12-17-34(27)32(36)30(24-14-9-8-10-15-24)25-19-28(38-4)31(39-5)29(20-25)41-23(3)22-40-18-7-2/h6-7,19-20,23-24,26-27,30,35H,1-2,8-18,21-22H2,3-5H3 WZCICYSXDCXYAJ-UHFFFAOYSA-N 790917 US20260034106, Compound m4(8,10)-OH Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 1588 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790917 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790917&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396383 COc1cc2cc(c1OC)O[C@@H](C)COC/C=C/C[C@@H](CO)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C31H45NO8/c1-21-20-38-16-10-8-13-24(19-33)40-31(35)25-14-7-9-15-32(25)30(34)28(22-11-5-4-6-12-22)23-17-26(36-2)29(37-3)27(18-23)39-21/h8,10,17-18,21-22,24-25,28,33H,4-7,9,11-16,19-20H2,1-3H3 CEUBJLAWUFVLFO-UHFFFAOYSA-N 790918 US20260034106, Compound m5(8,10)-(E)-OH Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 58.0 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790918 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790918&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396384 C=CCO[C@@H](CO)COc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](C)[C@H](C)C=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C34H51NO8/c1-7-18-41-27(21-36)22-42-30-20-26(19-29(39-5)32(30)40-6)31(25-14-10-9-11-15-25)33(37)35-17-13-12-16-28(35)34(38)43-24(4)23(3)8-2/h7-8,19-20,23-25,27-28,31,36H,1-2,9-18,21-22H2,3-6H3 BANCWAIDKHRGKY-UHFFFAOYSA-N 790919 US20260034106, Compound m4(10,7)-OH Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 2732 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790919 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790919&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396385 COc1cc2cc(c1OC)O[C@@H](C)COC/C=C/C[C@@H](CO)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C31H45NO8/c1-21-20-38-16-10-8-13-24(19-33)40-31(35)25-14-7-9-15-32(25)30(34)28(22-11-5-4-6-12-22)23-17-26(36-2)29(37-3)27(18-23)39-21/h8,10,17-18,21-22,24-25,28,33H,4-7,9,11-16,19-20H2,1-3H3 CEUBJLAWUFVLFO-UHFFFAOYSA-N 790920 US20260034106, Compound m5(10,7)-(E)-OH Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 43.0 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790920 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790920&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396386 C=CCOCCOc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](CO)CC=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C32H47NO8/c1-5-12-25(22-34)41-32(36)26-15-10-11-16-33(26)31(35)29(23-13-8-7-9-14-23)24-20-27(37-3)30(38-4)28(21-24)40-19-18-39-17-6-2/h5-6,20-21,23,25-26,29,34H,1-2,7-19,22H2,3-4H3 FLKPGDBPHLVORT-UHFFFAOYSA-N 790921 US20260034106, Compound m4(8,3)-OH Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 1016 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790921 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790921&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396387 COc1cc2cc(c1OC)OCCOC/C=C/C[C@@H](CO)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C30H43NO8/c1-35-25-18-22-19-26(28(25)36-2)38-17-16-37-15-9-7-12-23(20-32)39-30(34)24-13-6-8-14-31(24)29(33)27(22)21-10-4-3-5-11-21/h7,9,18-19,21,23-24,27,32H,3-6,8,10-17,20H2,1-2H3 GRXCOFYTBLQQSF-UHFFFAOYSA-N 790922 US20260034106, Compound m5(8,3)-(E)-OH Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 38.0 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790922 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790922&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396388 C=CCO[C@@H](C)COc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](CO)CC=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C33H49NO8/c1-6-13-26(21-35)42-33(37)27-16-11-12-17-34(27)32(36)30(24-14-9-8-10-15-24)25-19-28(38-4)31(39-5)29(20-25)41-22-23(3)40-18-7-2/h6-7,19-20,23-24,26-27,30,35H,1-2,8-18,21-22H2,3-5H3 JLJCQURDGAQCMV-UHFFFAOYSA-N 790923 US20260034106, Compound m4(8,5)-OH Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 1988 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790923 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790923&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396389 COc1cc2cc(c1OC)OC[C@H](C)OC/C=C/C[C@@H](CO)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C31H45NO8/c1-21-20-39-27-18-23(17-26(36-2)29(27)37-3)28(22-11-5-4-6-12-22)30(34)32-15-9-7-14-25(32)31(35)40-24(19-33)13-8-10-16-38-21/h8,10,17-18,21-22,24-25,28,33H,4-7,9,11-16,19-20H2,1-3H3 WZGBGLLYSRSOQY-UHFFFAOYSA-N 790924 US20260034106, Compound m5(8,5)-(E)-OH Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 74.0 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790924 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790924&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396390 C=CCOC[C@H](O)COc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](C)CC=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C33H49NO8/c1-6-13-23(3)42-33(37)27-16-11-12-17-34(27)32(36)30(24-14-9-8-10-15-24)25-19-28(38-4)31(39-5)29(20-25)41-22-26(35)21-40-18-7-2/h6-7,19-20,23-24,26-27,30,35H,1-2,8-18,21-22H2,3-5H3 FJFRDGVFPUTNDE-UHFFFAOYSA-N 790925 US20260034106, Compound m4(6,16)-OH Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 926 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790925 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790925&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396391 COc1cc2cc(c1OC)OC[C@@H](O)COC/C=C/C[C@@H](C)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C31H45NO8/c1-21-11-8-10-16-38-19-24(33)20-39-27-18-23(17-26(36-2)29(27)37-3)28(22-12-5-4-6-13-22)30(34)32-15-9-7-14-25(32)31(35)40-21/h8,10,17-18,21-22,24-25,28,33H,4-7,9,11-16,19-20H2,1-3H3 JKSWACQSJXNSKO-UHFFFAOYSA-N 790926 US20260034106, Compound m5(6,16)-(E)-OH Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 61.0 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790926 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790926&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396392 C=CCOC[C@@H](O)COc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](C)[C@H](C)C=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C34H51NO8/c1-7-18-41-21-27(36)22-42-30-20-26(19-29(39-5)32(30)40-6)31(25-14-10-9-11-15-25)33(37)35-17-13-12-16-28(35)34(38)43-24(4)23(3)8-2/h7-8,19-20,23-25,27-28,31,36H,1-2,9-18,21-22H2,3-6H3 ZRRVWLIXEZTIAN-UHFFFAOYSA-N 790927 US20260034106, Compound m4(9,15)-OH Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 1335 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790927 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790927&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396393 COc1cc2cc(c1OC)OC[C@H](O)COC/C=C/[C@@H](C)[C@@H](C)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C32H47NO8/c1-21-11-10-16-39-19-25(34)20-40-28-18-24(17-27(37-3)30(28)38-4)29(23-12-6-5-7-13-23)31(35)33-15-9-8-14-26(33)32(36)41-22(21)2/h10-11,17-18,21-23,25-26,29,34H,5-9,12-16,19-20H2,1-4H3 IWJWSROPOXYJMA-UHFFFAOYSA-N 790928 US20260034106, Compound m5(9,15)-(E) Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 82.0 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790928 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790928&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396394 C=CCOCCCOc1cc([C@@H](C(=O)N2CCCC[C@H]2C(=O)O[C@H](CO)CC=C)C2CCCCC2)cc(OC)c1OC InChI=1S/C33H49NO8/c1-5-13-26(23-35)42-33(37)27-16-10-11-17-34(27)32(36)30(24-14-8-7-9-15-24)25-21-28(38-3)31(39-4)29(22-25)41-20-12-19-40-18-6-2/h5-6,21-22,24,26-27,30,35H,1-2,7-20,23H2,3-4H3 MCDJDFHIZBJEHH-UHFFFAOYSA-N 790929 US20260034106, Compound m4(8,4)-OH Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 1742 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790929 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790929&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6 396395 COc1cc2cc(c1OC)OCCCOC/C=C/C[C@@H](CO)OC(=O)[C@@H]1CCCCN1C(=O)[C@H]2C1CCCCC1 InChI=1S/C31H45NO8/c1-36-26-19-23-20-27(29(26)37-2)39-18-10-17-38-16-9-7-13-24(21-33)40-31(35)25-14-6-8-15-32(25)30(34)28(23)22-11-4-3-5-12-22/h7,9,19-20,22,24-25,28,33H,3-6,8,10-18,21H2,1-2H3 JPEKPKWKQXYJLI-UHFFFAOYSA-N 790930 US20260034106, Compound m5(8,4)-(E)-OH Peptidyl-prolyl cis-trans isomerase FKBP5 Homo sapiens 42.0 US Patent 10.7270/Q2X63SRK aid1802770 US20260034106 SPISKE, M; HAUSCH, F; MEYNERS, C; BAUDER, M 2/5/2026 6/17/2026 The Technical University of Darmstadt http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=790930 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006096&target=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=790930&enzyme=Peptidyl-prolyl+cis-trans+isomerase+FKBP5&column=ki&startPg=0&Increment=50&submit=Search 1 MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV 9KOX,7L7I,5OMP,5NJX,8FFW,3O5D,3O5F,3O5E,4DRI,4DRH,3O5K,3O5J,3O5I,3O5G,8BAJ,8BA6,7R0L Peptidyl-prolyl cis-trans isomerase FKBP5 FKBP5_HUMAN Q13451 F5H7R1 Q59EB8 Q5TGM6