› 2z8j

X-ray diffraction
2.05Å resolution

Crystal Structure of Escherichia coli gamma-Glutamyltranspeptidase in Complex with Azaserine prepared in the dark

Released:
DOI: 10.2210/pdb2z8j/pdb
PDB entry 2z8j coloured by chain, front view.
PDB entry 2z8j coloured by chain, side view.
PDB entry 2z8j coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structures of Escherichia coli gamma-glutamyltranspeptidase in complex with azaserine and acivicin: novel mechanistic implication for inhibition by glutamine antagonists.
Wada K, Hiratake J, Irie M, Okada T, Yamada C, Kumagai H, Suzuki H, Fukuyama K
J Mol Biol 380 361-72 (2008)
PMID: 18555071

Function and Biology Details

Reactions catalysed: 
A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
A glutathione-S-conjugate + H(2)O = an (L-cysteinylglycine)-S-conjugate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148481 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutathione hydrolase large chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 366 amino acids
Theoretical weight: 39.31 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P18956 (Residues: 25-390; Coverage: 66%)
Gene names: JW3412, b3447, ggt
Sequence domains: Gamma-glutamyltranspeptidase
Structure domains: Serum Albumin; Chain A, Domain 1
Glutathione hydrolase small chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 190 amino acids
Theoretical weight: 20.03 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P18956 (Residues: 391-580; Coverage: 34%)
Gene names: JW3412, b3447, ggt
Sequence domains: Gamma-glutamyltranspeptidase

Ligands and Environments

1 bound ligand:
Ligand AZS 2 x AZS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 76.26Å b: 126.8Å c: 128.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.227 0.267
Expression system: Escherichia coli

Quick links

Citations

4 review citations

γ-Glutamyltranspeptidases: sequence, structure, biochemical properties, and biotechnological applications.
Castellano et al. (2012)
3 more

2 mentions without citation

Bacterial Gamma-Glutamyl Transpeptidase, an Emerging Biocatalyst: Insights Into Structure-Function Relationship and Its Biotechnological Applications.
Saini et al. (2021)
1 more