› 1oe8

X-ray diffraction
1.65Å resolution

28kDa glutathione S-transferase from Schistosoma haematobium (glutathione saturated)

Released:
DOI: 10.2210/pdb1oe8/pdb
PDB entry 1oe8 coloured by chain, front view.
PDB entry 1oe8 coloured by chain, side view.
PDB entry 1oe8 coloured by chain, top view.
Source organism: Schistosoma haematobium
Primary publication:
Crystal structure of the 28 kDa glutathione S-transferase from Schistosoma haematobium.
Johnson KA, Angelucci F, Bellelli A, Hervé M, Fontaine J, Tsernoglou D, Capron A, Trottein F, Brunori M
Biochemistry 42 10084-94 (2003)
PMID: 12939136

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-151639 (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: P30114 (Residues: 1-211; Coverage: 100%)
Sequence domains:
Structure 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: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P21
Unit cell:
a: 53.142Å b: 77.705Å c: 53.195Å
α: 90° β: 93.4° γ: 90°
R-values:
R R work R free
0.229 0.229 0.28
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

Schistosomes: the road from host-parasite interactions to vaccines in clinical trials.
Capron et al. (2005)
7 more

2 mentions without citation

ResBoost: characterizing and predicting catalytic residues in enzymes.
Alterovitz et al. (2009)
1 more