› 1w89

X-ray diffraction
2Å resolution

Structure of the reduced form of human thioredoxin 2

Released:
DOI: 10.2210/pdb1w89/pdb
PDB entry 1w89 coloured by chain, front view.
PDB entry 1w89 coloured by chain, side view.
PDB entry 1w89 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of oxidized and reduced forms of human mitochondrial thioredoxin 2.
Smeets A, Evrard C, Landtmeters M, Marchand C, Knoops B, Declercq JP
Protein Sci 14 2610-21 (2005)
PMID: 16195549

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-189264 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin, mitochondrial Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 119 amino acids
Theoretical weight: 13.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99757 (Residues: 60-166; Coverage: 65%)
Gene names: TRX2, TXN2
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: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P1
Unit cell:
a: 49.58Å b: 49.61Å c: 80.02Å
α: 87.77° β: 82.3° γ: 79.31°
R-values:
R R work R free
0.22 0.217 0.284
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling.
Cox et al. (2010)
4 more

3 mentions without citation

Human quiescin-sulfhydryl oxidase, QSOX1: probing internal redox steps by mutagenesis.
Heckler et al. (2008)
2 more