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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
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 Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20088880","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"20088880","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20088880","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3A75","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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