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2DG5

Crystal Structure of Gamma-glutamyl transpeptidase from Escherichia coli in complex with hydrolyzed Glutathione

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 Residues7
DetailsBINDING SITE FOR RESIDUE CA B 701
ChainResidue
BASP569
BSER572
BASP575
BHOH1860
BHOH1861
BHOH1862
BHOH1863

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA D 702
ChainResidue
DASP575
DHOH1864
DHOH1865
DHOH1866
DHOH1867
DASP569
DSER572

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GLU B 601
ChainResidue
AARG114
BTHR391
BASN411
BGLN430
BASP433
BTYR444
BSER462
BSER463
BMSE464
BGLY483
BGLY484
BHOH1067

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GLU D 602
ChainResidue
CARG114
DTHR391
DASN411
DGLN430
DASP433
DTYR444
DSER462
DSER463
DMSE464
DGLY483
DGLY484
DHOH1058
DHOH1669

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 703
ChainResidue
AGLN366
AGLU377
AILE378
AARG379
AHOH1074
AHOH1524
AHOH1540
AHOH1623

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 2025-07-02

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