› 2dsa

X-ray diffraction
2.1Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176821 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 203 amino acids
Theoretical weight: 22.4 KDa
Source organism: Paraburkholderia xenovorans LB400
Expression system: Escherichia coli
UniProt:
  • Canonical: Q59721 (Residues: 1-203; Coverage: 100%)
Gene names: Bxe_C1190, bphK
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 4 x GSH
1 bound ligand:
Ligand HPX 4 x HPX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: R3
Unit cell:
a: 112.2Å b: 112.2Å c: 221.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.203 0.236
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

9 mentions without citation

The still mysterious roles of cysteine-containing glutathione transferases in plants.
Lallement et al. (2014)
8 more