› 2wju

X-ray diffraction
2.3Å resolution

Glutathione transferase A2-2 in complex with glutathione

Released:
DOI: 10.2210/pdb2wju/pdb
PDB entry 2wju coloured by chain, front view.
PDB entry 2wju coloured by chain, side view.
PDB entry 2wju coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for featuring of steroid isomerase activity in alpha class glutathione transferases.
Tars K, Olin B, Mannervik B
J Mol Biol 397 332-40 (2010)
PMID: 20083122

Function and Biology Details

Reaction catalysed: 
RX + glutathione = HX + R-S-glutathione
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140590 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase A2 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 222 amino acids
Theoretical weight: 25.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09210 (Residues: 1-222; Coverage: 100%)
Gene names: GST2, GSTA2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 8 x GSH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P1
Unit cell:
a: 54.16Å b: 85.5Å c: 113.42Å
α: 96° β: 101.78° γ: 97.46°
R-values:
R R work R free
0.248 0.246 0.297
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes.
Deponte M. (2013)
6 more

4 mentions without citation

The impact of nitric oxide toxicity on the evolution of the glutathione transferase superfamily: a proposal for an evolutionary driving force.
Bocedi et al. (2013)
3 more