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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
B0006751biological_processglutathione catabolic process
B0036374molecular_functionglutathione hydrolase activity
C0006751biological_processglutathione catabolic process
C0036374molecular_functionglutathione hydrolase activity
D0006751biological_processglutathione catabolic process
D0036374molecular_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 Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:16618936, ECO:0000269|PubMed:18555071
ChainResidueDetails
BTHR391
DTHR391

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16618936
ChainResidueDetails
BTHR409
BASN411
BGLN430
BASP433
DTHR409
DASN411
DGLN430
DASP433

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING:
ChainResidueDetails
BSER462
BGLY483
DSER462
DGLY483

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PDB entries from 2024-07-24

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