› 2vl3

X-ray diffraction
1.83Å resolution

Oxidized and reduced forms of human peroxiredoxin 5

Released:
DOI: 10.2210/pdb2vl3/pdb
PDB entry 2vl3 coloured by chain, front view.
PDB entry 2vl3 coloured by chain, side view.
PDB entry 2vl3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins.
Smeets A, Marchand C, Linard D, Knoops B, Declercq JP
Arch Biochem Biophys 477 98-104 (2008)
PMID: 18489898

Function and Biology Details

Reaction catalysed: 
Thioredoxin + ROOH = thioredoxin disulfide + H(2)O + ROH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151617 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxiredoxin-5, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 172 amino acids
Theoretical weight: 18.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli M15
UniProt:
  • Canonical: P30044 (Residues: 54-214; Coverage: 75%)
Gene names: ACR1, PRDX5, SBBI10
Sequence domains: Redoxin
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 X11
Spacegroup: C2221
Unit cell:
a: 78.35Å b: 102.12Å c: 146.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.238 0.235 0.288
Expression system: Escherichia coli M15

Quick links

Citations

9 review citations

Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides.
Rhee et al. (2012)
8 more

7 mentions without citation

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