3ctf

X-ray diffraction
2.1Å resolution

Crystal structure of oxidized GRX2

Released:
Source organism: Saccharomyces cerevisiae
Primary publication:
Structural basis for the different activities of yeast Grx1 and Grx2.
Biochim. Biophys. Acta 1804 1542-7 (2010)
PMID: 20417731

Function and Biology Details

Reactions catalysed:
RX + glutathione = HX + R-S-glutathione
2 glutathione + H(2)O(2) = glutathione disulfide + 2 H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaredoxin-2 Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 14.15 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P17695 (Residues: 35-143; Coverage: 76%)
  • Best match: P17695-2 (Residues: 1-109)
Gene names: D9719.17, GRX2, TTR, TTR1, YDR513W
Sequence domains: Glutaredoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P41212
Unit cell:
a: 48.77Å b: 48.77Å c: 96.446Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.222 0.25
Expression system: Escherichia coli