› 3l0h

X-ray diffraction
2.13Å resolution

Crystal Structure Analysis of W21A mutant of human GSTA1-1 in complex with S-hexylglutathione

Released:
DOI: 10.2210/pdb3l0h/pdb
PDB entry 3l0h coloured by chain, front view.
PDB entry 3l0h coloured by chain, side view.
PDB entry 3l0h coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Stability of the domain interface contributes towards the catalytic function at the H-site of class alpha glutathione transferase A1-1.
Balchin D, Fanucchi S, Achilonu I, Adamson RJ, Burke J, Fernandes M, Gildenhuys S, Dirr HW
Biochim Biophys Acta 1804 2228-33 (2010)
PMID: 20833278

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
Molecule details ›
Chains: A, B
Length: 222 amino acids
Theoretical weight: 25.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P08263 (Residues: 1-222; Coverage: 100%)
Gene name: GSTA1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GTX 2 x GTX
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: C2
Unit cell:
a: 100.229Å b: 94.98Å c: 51.987Å
α: 90° β: 92.63° γ: 90°
R-values:
R R work R free
0.174 0.17 0.233
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Interactions of glutathione transferases with 4-hydroxynonenal.
Balogh et al. (2011)
5 other articles