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2E0Y

Crystal structure of the samarium derivative of mature gamma-glutamyltranspeptidase from Escherichia coli

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 Residues2
DetailsBINDING SITE FOR RESIDUE SM B 601
ChainResidue
BASN411
BASP433

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SM D 602
ChainResidue
DASN411
DASP433

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 701
ChainResidue
AGLN366
AGLU377
AILE378
AARG379
AHOH1025

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 705
ChainResidue
AASN309
ALYS361
AALA364
AASP365

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 702
ChainResidue
BASP574
BASP575
BHOH1090
BHOH1261
BHOH1402

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 704
ChainResidue
CGLN366
CGLU377
CILE378
CARG379
CHOH1304

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL D 703
ChainResidue
DVAL573
DASP574
DASP575
DHOH1042
DHOH1051
DHOH1235
DHOH1328

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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