› 2oe3

X-ray diffraction
1.8Å resolution

Crystal Structure of Mitochondrial Thioredoxin 3 from Saccharomyces cerevisiae (oxidized form)

Released:
DOI: 10.2210/pdb2oe3/pdb
PDB entry 2oe3 coloured by chain, front view.
PDB entry 2oe3 coloured by chain, side view.
PDB entry 2oe3 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structural and mechanistic analyses of yeast mitochondrial thioredoxin Trx3 reveal putative function of its additional cysteine residues.
Bao R, Zhang Y, Zhou CZ, Chen Y
Biochim Biophys Acta 1794 716-21 (2009)
PMID: 19166985

Function and Biology Details

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-150450 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin-3, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 114 amino acids
Theoretical weight: 12.87 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P25372 (Residues: 22-127; Coverage: 84%)
Gene names: TRX3, YCR083W, YCR83W
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 49.313Å b: 60.682Å c: 72.679Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.198 0.255
Expression system: Escherichia coli BL21

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Citations

9 citation in other articles

Inactivation of a peroxiredoxin by hydrogen peroxide is critical for thioredoxin-mediated repair of oxidized proteins and cell survival.
Day et al. (2012)
8 more