› 3a2w

X-ray diffraction
2.3Å resolution

Peroxiredoxin (C50S) from Aeropytum pernix K1 (peroxide-bound form)

Released:
DOI: 10.2210/pdb3a2w/pdb
PDB entry 3a2w coloured by chain, front view.
PDB entry 3a2w coloured by chain, side view.
PDB entry 3a2w coloured by chain, top view.
Source organism: Aeropyrum pernix K1
Primary publication:
Crystal structure of peroxiredoxin from Aeropyrum pernix K1 complexed with its substrate, hydrogen peroxide.
Nakamura T, Kado Y, Yamaguchi T, Matsumura H, Ishikawa K, Inoue T
J Biochem 147 109-15 (2010)
PMID: 19819903

Function and Biology Details

Reaction catalysed: 
Thioredoxin + ROOH = thioredoxin disulfide + H(2)O + ROH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195428 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxiredoxin Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 249 amino acids
Theoretical weight: 28.6 KDa
Source organism: Aeropyrum pernix K1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y9L0 (Residues: 2-250; Coverage: 100%)
Gene name: APE_2278
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GOL 7 x GOL
Ligand PER 3 x PER
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P1
Unit cell:
a: 76.262Å b: 103.326Å c: 104.554Å
α: 105.72° β: 105.08° γ: 92.63°
R-values:
R R work R free
0.202 0.202 0.249
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling.
Perkins et al. (2015)
11 more

3 mentions without citation

Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins.
Hall et al. (2011)
2 more