Structure of PDB 4gg2 Chain B Binding Site BS02

Receptor Information
>4gg2 Chain B (length=189) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNEMDDFSSPSIT
NEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTA
TALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETR
HHHTQIASTFIAVVQAIVRTAGGWAAASDSRKGGEPAGY
Ligand information
Ligand IDCL
InChIInChI=1S/ClH/h1H/p-1
InChIKeyVEXZGXHMUGYJMC-UHFFFAOYSA-M
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Cl-]
FormulaCl
NameCHLORIDE ION
ChEMBL
DrugBankDB14547
ZINC
PDB chain4gg2 Chain B Residue 607 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4gg2 Novel Insights into Eukaryotic gamma-Glutamyltranspeptidase 1 from the Crystal Structure of the Glutamate-bound Human Enzyme.
Resolution2.21 Å
Binding residue
(original residue number in PDB)		A382 K562
Binding residue
(residue number reindexed from 1)		A2 K182
Annotation score1
Enzymatic activity
Enzyme Commision number 2.3.2.2: gamma-glutamyltransferase.
3.4.19.13: glutathione gamma-glutamate hydrolase.
3.4.19.14: leukotriene-C4 hydrolase.
Gene Ontology
Molecular Function
GO:0036374 glutathione hydrolase activity
Biological Process
GO:0006751 glutathione catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4gg2, PDBe:4gg2, PDBj:4gg2
PDBsum4gg2
PubMed24047895
UniProtP19440|GGT1_HUMAN Glutathione hydrolase 1 proenzyme (Gene Name=GGT1)

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