5ucx

X-ray diffraction
2.4Å resolution

Structure of S78C Human Peroxiredoxin 3 as three stacked rings

Released:
Source organism: Homo sapiens
Primary publication:
Quaternary structure influences the peroxidase activity of peroxiredoxin 3.
Biochem Biophys Res Commun 497 558-563 (2018)
PMID: 29438714

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
PDBe Complex ID:
PDB-CPX-151623 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin-dependent peroxide reductase, mitochondrial Chains: A, B, C, D, E, F, G, H, I
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I
Length: 201 amino acids
Theoretical weight: 22.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P30048 (Residues: 62-256; Coverage: 76%)
Gene names: AOP1, PRDX3
Sequence domains:
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: I222
Unit cell:
a: 133.449Å b: 167.59Å c: 221.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.228
Expression system: Escherichia coli