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2Z8J

Crystal Structure of Escherichia coli gamma-Glutamyltranspeptidase in Complex with Azaserine prepared in the dark

Functional Information from GO Data
ChainGOidnamespacecontents
A0006751biological_processglutathione catabolic process
A0036374molecular_functionglutathione gamma-glutamate hydrolase
C0006751biological_processglutathione catabolic process
C0036374molecular_functionglutathione gamma-glutamate hydrolase
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AZS B 390
ChainResidue
AARG114
BPRO482
BGLY483
BGLY484
BHOH596
BHOH641
BTHR391
BASN411
BGLN430
BASP433
BTYR444
BSER462
BSER463
BMET464

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AZS D 390
ChainResidue
CARG114
DTHR391
DTHR409
DASN411
DGLN430
DASP433
DTYR444
DSER462
DSER463
DMET464
DGLY483
DGLY484
DHOH586
DHOH608

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 Residues38
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
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_FI4
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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