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3WHS

Crystal structure of Bacillus subtilis gamma-glutamyltranspeptidase in complex with acivicin

Functional Information from GO Data
ChainGOidnamespacecontents
A0006751biological_processglutathione catabolic process
A0036374molecular_functionglutathione hydrolase activity
B0006751biological_processglutathione catabolic process
B0036374molecular_functionglutathione hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AVN B 600
ChainResidue
AARG113
BGLY485
BGLY486
BILE489
BHOH713
BHOH774
BTHR403
BTHR421
BGLU423
BGLU442
BASP445
BSER464
BSER465
BMET466

Functional Information from PROSITE/UniProt
site_idPS00462
Number of Residues25
DetailsG_GLU_TRANSPEPTIDASE Gamma-glutamyltranspeptidase signature. TTHfTVadrwGNvVSyTtTIEqlFG
ChainResidueDetails
BTHR403-GLY427

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:20088880
ChainResidueDetails
BTHR403

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BTHR421

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:20088880
ChainResidueDetails
BGLU423
BGLU442
BASP445

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20088880, ECO:0007744|PDB:3A75
ChainResidueDetails
BSER464
BGLY485

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PDB entries from 2024-10-16

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