Structure of PDB 2dbx Chain D Binding Site BS01

Receptor Information
>2dbx Chain D (length=190) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TTHYSVVDKDGNAVAVTYTLNTTFGTGIVAGESGILLNNQMDDFSAKPGV
PNVYGLVGGDANAVGPNKRPLSSMSPTIVVKDGKTWLVTGSPGGSRIITT
VLQMVVNSIDYGLNVAEATNAPRFHHQWLPDELRVEKGFSPDTLKLLEAK
GQKVALKEAMGSTQSIMVGPDGELYGASDPRSVDDLTAGY
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain2dbx Chain D Residue 702 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2dbx Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		D569 P570 S572 D575
Binding residue
(residue number reindexed from 1)		D179 P180 S182 D185
Annotation score1
Enzymatic activity
Enzyme Commision number 2.3.2.2: gamma-glutamyltransferase.
3.4.19.13: glutathione gamma-glutamate 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:2dbx, PDBe:2dbx, PDBj:2dbx
PDBsum2dbx
PubMed16618936
UniProtP18956|GGT_ECOLI Glutathione hydrolase proenzyme (Gene Name=ggt)

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