4lmw

X-ray diffraction
2.1Å resolution

Crystal structure of glutathione transferase GSTFuA3 from Phanerochaete chrysosporium

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GST N-terminal domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 251 amino acids
Theoretical weight: 28.94 KDa
Source organism: Phanerodontia chrysosporium
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A067XG73 (Residues: 1-251; Coverage: 100%)
Sequence domains: Glutathione S-transferase, N-terminal domain
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P6122
Unit cell:
a: 87Å b: 87Å c: 225.703Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.187 0.216
Expression system: Escherichia coli