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2E0X

Crystal Structure of Gamma-glutamyltranspeptidase from Escherichia coli (monoclinic form)

Functional Information from GO Data
ChainGOidnamespacecontents
A0006751biological_processglutathione catabolic process
A0036374molecular_functionglutathione hydrolase activity
C0006751biological_processglutathione catabolic process
C0036374molecular_functionglutathione hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 701
ChainResidue
BASP569
BSER572
BASP575

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA D 702
ChainResidue
DASP569
DSER572
DASP575

Functional Information from PROSITE/UniProt
site_idPS00462
Number of Residues25
DetailsG_GLU_TRANSPEPTIDASE Gamma-glutamyltranspeptidase signature. TTHySVvdkdGNaVAvTyTLNttFG
ChainResidueDetails
BTHR391-GLY415

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16618936","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"16618936","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18555071","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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