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2DBX

Crystal Structure of Gamma-glutamyltranspeptidase from Escherichia coli Complexed with L-Glutamate

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 Residues5
DetailsBINDING SITE FOR RESIDUE CA B 701
ChainResidue
BASP569
BSER572
BASP575
BHOH1791
BHOH1792

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 702
ChainResidue
DHOH1794
DHOH1795
DASP569
DSER572
DASP575
DHOH1793

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE GLU B 601
ChainResidue
AARG114
BTHR391
BASN411
BGLN430
BASP433
BTYR444
BSER462
BSER463
BMSE464
BPRO482
BGLY483
BGLY484
BILE487
BHOH1067
BHOH1490
BHOH1542

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE GLU D 602
ChainResidue
CARG114
DTHR391
DASN411
DGLN430
DASP433
DTYR444
DSER462
DSER463
DMSE464
DGLY483
DGLY484
DILE487
DHOH1058
DHOH1701

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 703
ChainResidue
AGLN366
AGLU377
AILE378
AARG379
AHOH1074
AHOH1540
AHOH1556
AHOH1600
AHOH1650

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 2024-07-17

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