› 2pvq

X-ray diffraction
1.8Å resolution

Crystal structure of Ochrobactrum anthropi glutathione transferase Cys10Ala mutant with glutathione bound at the H-site

Released:
DOI: 10.2210/pdb2pvq/pdb
PDB entry 2pvq coloured by chain, front view.
PDB entry 2pvq coloured by chain, side view.
PDB entry 2pvq coloured by chain, top view.
Source organism: Brucella anthropi
Primary publication:
Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site.
Allocati N, Federici L, Masulli M, Favaloro B, Di Ilio C
Proteins 71 16-23 (2008)
PMID: 18076047

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160478 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase Chain: A
Molecule details ›
Chain: A
Length: 201 amino acids
Theoretical weight: 21.73 KDa
Source organism: Brucella anthropi
Expression system: Escherichia coli
UniProt:
  • Canonical: P81065 (Residues: 1-201; Coverage: 100%)
Gene name: gst
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 1 x GSH
1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P6122
Unit cell:
a: 58.373Å b: 58.373Å c: 214.023Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.198 0.248
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Glutathione transferases in bacteria.
Allocati et al. (2009)
3 more

1 mention without citation

Progress in super long loop prediction.
Zhao et al. (2011)