› 3tks

X-ray diffraction
2.4Å resolution

Crystal structure of full-length human peroxiredoxin 4 in three different redox states

Released:
DOI: 10.2210/pdb3tks/pdb
PDB entry 3tks coloured by chain, front view.
PDB entry 3tks coloured by chain, side view.
PDB entry 3tks coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4.
Wang X, Wang L, Wang X, Sun F, Wang CC
Biochem J 441 113-8 (2012)
PMID: 21916849

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:
hetero decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171578 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Peroxiredoxin-4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 246 amino acids
Theoretical weight: 28.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13162 (Residues: 38-271; Coverage: 100%)
Gene name: PRDX4
Sequence domains:
Structure domains: Glutaredoxin
Peroxiredoxin-4 Chains: C, D
Molecule details ›
Chains: C, D
Length: 246 amino acids
Theoretical weight: 28.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13162 (Residues: 38-271; Coverage: 100%)
Gene name: PRDX4
Sequence domains:
Structure domains: Glutaredoxin
Peroxiredoxin-4 Chain: E
Molecule details ›
Chain: E
Length: 246 amino acids
Theoretical weight: 28.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13162 (Residues: 38-271; Coverage: 100%)
Gene name: PRDX4
Sequence domains:
Structure domains: Glutaredoxin

Ligands and Environments

1 bound ligand:
Ligand PER 3 x PER
2 modified residues:
Ligand CSO 2 x CSO
Ligand CSD 2 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E DW
Spacegroup: C2
Unit cell:
a: 183.178Å b: 140.104Å c: 61.504Å
α: 90° β: 102.48° γ: 90°
R-values:
R R work R free
0.213 0.183 0.232
Expression system: Escherichia coli

Quick links

Citations

23 review citations

ERO1: A protein disulfide oxidase and H2O2 producer.
Zito E. (2015)
22 more

1 mention without citation

Peroxiredoxins wear many hats: Factors that fashion their peroxide sensing personalities.
Bolduc et al. (2021)