Structure of PDB 4hj2 Chain B Binding Site BS01

Receptor Information
>4hj2 Chain B (length=213) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQ
QVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYIEGIADLG
EMILLLPVEKDAKLALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRAD
IHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPGSPRKPP
MDEKSLEEARKIF
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
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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)		D101 R131
Binding residue
(residue number reindexed from 1)		D98 R124
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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