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Ligands
Code Name Style Show Link
GOL Glycerol
GGL Gamma-L-glutamic acid
Non-standard Residues
Code Name Show
MSE Selenomethionine
Glycosylation
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Code : 2DBW   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Crystal Structure of Gamma-glutamyltranspeptidase from Escherichia coli Acyl-Enzyme Intermediate
Release Data : 2006-04-18
Compound :
mol_id molecule chains
1 Gamma-glutamyltranspeptidase A,C
ec: 2.3.2.2
fragment: LARGE SUBUNIT
mol_id molecule chains
2 Gamma-glutamyltranspeptidase B,D
ec: 2.3.2.2
fragment: SMALL SUBUNIT
Source :
mol_id organism_scientific expression_system
1 Escherichia coli K12  (taxid:83333) Escherichia coli  (taxid:562)
strain: K-12
gene: GGT
expression_system_strain: SH1603
expression_system_vector_type: PLASMID
expression_system_plasmid: PSH1291
mol_id organism_scientific expression_system
2 Escherichia coli K12  (taxid:83333) Escherichia coli  (taxid:562)
strain: K-12
gene: GGT
expression_system_strain: SH1603
expression_system_vector_type: PLASMID
expression_system_plasmid: PSH1291
Authors : Okada, T., Wada, K., Fukuyama, K.
Keywords : gamma-glutamyltransferase, ggt, gamma-gtp, glutathione, acyl-enzyme intermediate, Transferase
Exp. method : X-RAY DIFFRACTION ( 1.80 Å )
Citation :

Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate

Okada, T.,Suzuki, H.,Wada, K.  et al.
(2006)  Proc.Natl.Acad.Sci.USA  103 : 6471 - 6476

PubMed: 16618936
DOI: 10.1073/pnas.0511020103

Chain : B, D
UniProt : P18956 (GGT_ECOLI)
Reaction: EC: Evidence:
Physiological Direction:
an N-terminal (5-L-glutamyl)-[peptide] + an alpha-amino acid = 5-L-glutamyl amino acid + an N-terminal L-alpha-aminoacyl-[peptide] 2.3.2.2 PubMed:1360205
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glutathione + H2O = L-cysteinylglycine + L-glutamate 3.4.19.13 PubMed:2877974
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an S-substituted glutathione + H2O = an S-substituted L- cysteinylglycine + L-glutamate 3.4.19.13 PubMed:2877974
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