› 2caq

X-ray diffraction
2Å 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 Chain: A
Molecule details ›
Chain: A
Length: 211 amino acids
Theoretical weight: 23.89 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 GSH 1 x GSH
2 bound ligands:
Ligand PG4 1 x PG4
Ligand BME 1 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: P3221
Unit cell:
a: 53.185Å b: 53.185Å c: 141.856Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.188 0.24
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

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