› 3a2x

X-ray diffraction
1.9Å resolution

Peroxiredoxin (C50S) from Aeropyrum pernix K1 (acetate-bound form)

Released:
DOI: 10.2210/pdb3a2x/pdb
PDB entry 3a2x coloured by chain, front view.
PDB entry 3a2x coloured by chain, side view.
PDB entry 3a2x 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

1 bound ligand:
Ligand ACT 10 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P1
Unit cell:
a: 75.825Å b: 102.918Å c: 104.143Å
α: 105.99° β: 105.12° γ: 92.8°
R-values:
R R work R free
0.198 0.195 0.243
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