› 3ik9

X-ray diffraction
2.2Å resolution

Function and Biology Details

Reaction catalysed: 
RX + glutathione = HX + R-S-glutathione
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140083 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase A1 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 222 amino acids
Theoretical weight: 25.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08263 (Residues: 1-222; Coverage: 100%)
Gene name: GSTA1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand BOB 8 x BOB
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P21
Unit cell:
a: 95.889Å b: 114.658Å c: 96.239Å
α: 90° β: 117.76° γ: 90°
R-values:
R R work R free
0.226 0.224 0.279
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Chemistry and biochemistry of lipid peroxidation products.
Guéraud et al. (2010)
8 more

2 mentions without citation

Interactions of glutathione transferases with 4-hydroxynonenal.
Balogh et al. (2011)
1 more