› 2c80

X-ray diffraction
2.3Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151637 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase class-mu 28 kDa isozyme Chains: A, B
Molecule details ›
Chains: A, B
Length: 211 amino acids
Theoretical weight: 23.94 KDa
Source organism: Schistosoma haematobium
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P30113 (Residues: 1-211; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GTX 2 x GTX
1 bound ligand:
Ligand PG4 1 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P32
Unit cell:
a: 52.832Å b: 52.832Å c: 141.451Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.188 0.246
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

1 mention without citation

X-ray structure of Fasciola hepatica Sigma class glutathione transferase 1 reveals a disulfide bond to support stability in gastro-intestinal environment.
Line et al. (2019)