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X-ray diffraction
1.7Å resolution

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-152205 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxiredoxin-2 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: 197 amino acids
Theoretical weight: 21.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P32119 (Residues: 2-198; Coverage: 100%)
Gene names: NKEFB, PRDX2, TDPX1
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: C2
Unit cell:
a: 229.8Å b: 88.1Å c: 127.1Å
α: 90° β: 100° γ: 90°
R-values:
R R work R free
0.184 0.182 0.22
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Antioxidant Therapy in Cancer: Rationale and Progress.
Luo et al. (2022)
2 more

2 mentions without citation

Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2.
Peskin et al. (2021)
1 more