› 3d5j

X-ray diffraction
1.91Å resolution

Structure of yeast Grx2-C30S mutant with glutathionyl mixed disulfide

Released:
DOI: 10.2210/pdb3d5j/pdb
PDB entry 3d5j coloured by chain, front view.
PDB entry 3d5j coloured by chain, side view.
PDB entry 3d5j coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structural aspects of the distinct biochemical properties of glutaredoxin 1 and glutaredoxin 2 from Saccharomyces cerevisiae.
Discola KF, de Oliveira MA, Rosa Cussiol JR, Monteiro G, Bárcena JA, Porras P, Padilla CA, Guimarães BG, Netto LE
J Mol Biol 385 889-901 (2009)
PMID: 18992757

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148137 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaredoxin-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 112 amino acids
Theoretical weight: 12.32 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P17695 (Residues: 35-143; Coverage: 76%)
Gene names: D9719.17, GRX2, TTR, TTR1, YDR513W
Sequence domains: Glutaredoxin
Structure domains: Glutaredoxin

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE D03B-MX1
Spacegroup: P212121
Unit cell:
a: 37.008Å b: 45.205Å c: 105.035Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.198 0.261
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes.
Deponte M. (2013)
10 more

3 mentions without citation

Glutaredoxin catalysis requires two distinct glutathione interaction sites.
Begas et al. (2017)
2 more