› 7kj0

X-ray diffraction
2.29Å 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: 21.82 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
1 modified residue:
Ligand CSD 10 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: C2
Unit cell:
a: 231Å b: 88Å c: 125.6Å
α: 90° β: 100.2° γ: 90°
R-values:
R R work R free
0.185 0.182 0.233
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

1 mention without citation

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