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4OTU

Crystal structure of the gamma-glutamyltranspeptidase from Bacillus licheniformis in complex 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
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 601
ChainResidue
BGLU523
BASP568

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GLU B 602
ChainResidue
BSER461
BMET462
BGLY482
AARG109
BTHR399
BTHR417
BGLU419
BGLU438
BASP441
BSER460

Functional Information from PROSITE/UniProt
site_idPS00063
Number of Residues16
DetailsALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. MAKTFKliRKeGSkAF
ChainResidueDetails
AMET221-PHE236

site_idPS00462
Number of Residues25
DetailsG_GLU_TRANSPEPTIDASE Gamma-glutamyltranspeptidase signature. TTHfTVtdqwGNvVSyTtTIEqlFG
ChainResidueDetails
BTHR399-GLY423

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PDB entries from 2024-07-24

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