› 1qo4

X-ray diffraction
3Å resolution

Function and Biology Details

Reaction catalysed: 
2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174969 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxidase 53 Chain: A
Molecule details ›
Chain: A
Length: 306 amino acids
Theoretical weight: 32.09 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q42578 (Residues: 31-335; Coverage: 100%)
Gene names: At5g06720, MPH15.8, P53, PER53
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 46.29Å b: 74.848Å c: 80.794Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.235
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Horseradish peroxidase: a modern view of a classic enzyme.
Veitch NC. (2004)
9 more

3 mentions without citation

Apoplastic class III peroxidases PRX62 and PRX69 promote Arabidopsis root hair growth at low temperature.
Pacheco et al. (2022)
2 more