X-ray diffraction
1.8Å resolution

Crystal structure of glutathione transferase Xi 3 from Trametes versicolor in complex with glutathione


Function and Biology Details

Reaction catalysed:
RX + glutathione = HX + R-S-glutathione
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
GST C-terminal domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 325 amino acids
Theoretical weight: 37.16 KDa
Source organism: Trametes versicolor
Expression system: Escherichia coli
  • Canonical: A0A3F2YM27 (Residues: 1-325; Coverage: 100%)
Sequence domains:

Ligands and Environments

Cofactor: Ligand GSH 2 x GSH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P43212
Unit cell:
a: 72.37Å b: 72.37Å c: 316.71Å
α: 90° β: 90° γ: 90°
R R work R free
0.162 0.161 0.189
Expression system: Escherichia coli