Structure of PDB 4hj2 Chain A Binding Site BS01

Receptor Information
>4hj2 Chain A (length=217) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQ
QVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYIEGIADLG
EMILLLPVCPPEEKDAKLALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKL
SRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPGSP
RKPPMDEKSLEEARKIF
Ligand information
Ligand IDLZ6
InChIInChI=1S/C24H35ClN4O8S/c25-10-11-29(17-6-4-16(5-7-17)2-1-3-21(31)32)12-13-38-15-19(23(35)27-14-22(33)34)28-20(30)9-8-18(26)24(36)37/h4-7,18-19H,1-3,8-15,26H2,(H,27,35)(H,28,30)(H,31,32)(H,33,34)(H,36,37)/t18-,19-/m0/s1
InChIKeyBQVGPQFUMPRIMA-OALUTQOASA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1cc(ccc1CCCC(=O)O)N(CCSC[C@@H](C(=O)NCC(=O)O)NC(=O)CC[C@@H](C(=O)O)N)CCCl
OpenEye OEToolkits 1.5.0c1cc(ccc1CCCC(=O)O)N(CCSCC(C(=O)NCC(=O)O)NC(=O)CCC(C(=O)O)N)CCCl
CACTVS 3.341N[CH](CCC(=O)N[CH](CSCCN(CCCl)c1ccc(CCCC(O)=O)cc1)C(=O)NCC(O)=O)C(O)=O
CACTVS 3.341N[C@@H](CCC(=O)N[C@@H](CSCCN(CCCl)c1ccc(CCCC(O)=O)cc1)C(=O)NCC(O)=O)C(O)=O
ACDLabs 10.04O=C(O)C(N)CCC(=O)NC(C(=O)NCC(=O)O)CSCCN(c1ccc(cc1)CCCC(=O)O)CCCl
FormulaC24 H35 Cl N4 O8 S
NameL-gamma-glutamyl-S-(2-{[4-(3-carboxypropyl)phenyl](2-chloroethyl)amino}ethyl)-L-cysteinylglycine;
Chlorambucil-Glutathione Conjugate
ChEMBL
DrugBank
ZINCZINC000024980297
PDB chain4hj2 Chain A Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4hj2 The interaction of the chemotherapeutic drug chlorambucil with human glutathione transferase A1-1: kinetic and structural analysis.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		Y9 R45 Q54 V55 Q67 T68 L107 P110 M208 F220
Binding residue
(residue number reindexed from 1)		Y6 R42 Q51 V52 Q64 T65 L104 P107 M205 F217
Annotation score2
Binding affinityPDBbind-CN: -logKd/Ki=2.53,Kd=2.95mM
Enzymatic activity
Catalytic site (original residue number in PDB) Y9 R15 R20
Catalytic site (residue number reindexed from 1) Y6 R12 R17
Enzyme Commision number 1.11.1.-
2.5.1.18: glutathione transferase.
5.3.3.-
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0004601 peroxidase activity
GO:0004602 glutathione peroxidase activity
GO:0004769 steroid delta-isomerase activity
GO:0005504 fatty acid binding
GO:0005515 protein binding
GO:0016740 transferase activity
GO:0016853 isomerase activity
Biological Process
GO:0006629 lipid metabolic process
GO:0006693 prostaglandin metabolic process
GO:0006749 glutathione metabolic process
GO:0006805 xenobiotic metabolic process
GO:0030855 epithelial cell differentiation
GO:0043651 linoleic acid metabolic process
GO:0098869 cellular oxidant detoxification
GO:1901687 glutathione derivative biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4hj2, PDBe:4hj2, PDBj:4hj2
PDBsum4hj2
PubMed23460799
UniProtP08263|GSTA1_HUMAN Glutathione S-transferase A1 (Gene Name=GSTA1)

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