› 4acs

X-ray diffraction
2.1Å resolution

Crystal structure of mutant GST A2-2 with enhanced catalytic efficiency with azathioprine

Released:
DOI: 10.2210/pdb4acs/pdb
PDB entry 4acs coloured by chain, front view.
PDB entry 4acs coloured by chain, side view.
PDB entry 4acs coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-based redesign of GST A2-2 for enhanced catalytic efficiency with azathioprine.
Zhang W, Modén O, Tars K, Mannervik B
Chem Biol 19 414-21 (2012)
PMID: 22444596

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-140590 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase A2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 222 amino acids
Theoretical weight: 25.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P09210 (Residues: 1-222; Coverage: 100%)
Gene names: GST2, GSTA2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 4 x GSH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF
Spacegroup: P21
Unit cell:
a: 48.66Å b: 94.8Å c: 113.72Å
α: 90° β: 92.77° γ: 90°
R-values:
R R work R free
0.264 0.261 0.321
Expression system: Escherichia coli K-12

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Citations

3 review citations

Recent advances in protein engineering and biotechnological applications of glutathione transferases.
Perperopoulou et al. (2018)
2 more

1 mention without citation

[A systematic pharmacological investigation of pharmacologically active ingredients in Toujie Quwen granules for treatment of COVID-19].
Ma et al. (2020)