PDBe 4gdx

X-ray diffraction
1.67Å resolution

Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex

Released:

Function and Biology Details

Reactions catalysed:
Leukotriene C(4) + H(2)O = leukotriene D(4) + L-glutamate
A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
Glutathione + H(2)O = L-cysteinylglycine + L-glutamate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutathione hydrolase 1 heavy chain Chain: A
Molecule details ›
Chain: A
Length: 374 amino acids
Theoretical weight: 40.87 KDa
Source organism: Homo sapiens
Expression system: Pichia
UniProt: Gene names: GGT, GGT1
Structure domains: Serum Albumin; Chain A, Domain 1
Glutathione hydrolase 1 light chain Chain: B
Molecule details ›
Chain: B
Length: 195 amino acids
Theoretical weight: 20.56 KDa
Source organism: Homo sapiens
Expression system: Pichia
UniProt:
  • Canonical: NEW P19440 (Residues: 375-569; Coverage: 34%)
Gene names: GGT, GGT1
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: C2221
Unit cell:
a: 105.524Å b: 125.247Å c: 104.468Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.147 0.145 0.174
Expression system: Pichia