› 5lcz

X-ray diffraction
2.32Å 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-138254 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase A1, N-terminally processed; Glutathione S-transferase alpha-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 222 amino acids
Theoretical weight: 25.78 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P04903 (Residues: 1-1, 86-218; Coverage: 60%)
  • Canonical: P08263 (Residues: 2-85, 219-222; Coverage: 40%)
Gene names: GSTA1, Gsta2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 1 x GSH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: C2
Unit cell:
a: 98.92Å b: 91.38Å c: 51.49Å
α: 90° β: 93.18° γ: 90°
R-values:
R R work R free
0.204 0.2 0.268
Expression system: Escherichia coli

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Citations

3 review citations

Review: Engineering of thermostable enzymes for industrial applications.
Rigoldi et al. (2018)
2 more