› 1tu7

X-ray diffraction
1.5Å resolution

Structure of Onchocerca Volvulus Pi-class Glutathione S-transferase

Released:
DOI: 10.2210/pdb1tu7/pdb
PDB entry 1tu7 coloured by chain, front view.
PDB entry 1tu7 coloured by chain, side view.
PDB entry 1tu7 coloured by chain, top view.
Source organism: Onchocerca volvulus
Primary publication:
Structure of the major cytosolic glutathione S-transferase from the parasitic nematode Onchocerca volvulus.
Perbandt M, Höppner J, Betzel C, Walter RD, Liebau E
J Biol Chem 280 12630-6 (2005)
PMID: 15640152

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155470 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 208 amino acids
Theoretical weight: 24.3 KDa
Source organism: Onchocerca volvulus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P46427 (Residues: 1-208; Coverage: 100%)
Gene name: GST2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 2 x GSH
1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 51.645Å b: 82.33Å c: 56.662Å
α: 90° β: 95.89° γ: 90°
R-values:
R R work R free
0.152 0.15 0.181
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Glutathione transferases from parasites: a biochemical view.
Torres-Rivera et al. (2008)
2 more

4 mentions without citation

Prediction of homoprotein and heteroprotein complexes by protein docking and template-based modeling: A CASP-CAPRI experiment.
Lensink et al. (2016)
3 more