› 1kzm

X-ray diffraction
2Å resolution

Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (HRP C).

Released:
DOI: 10.2210/pdb1kzm/pdb
PDB entry 1kzm coloured by chain, front view.
PDB entry 1kzm coloured by chain, side view.
PDB entry 1kzm coloured by chain, top view.
Source organism: Armoracia rusticana
Primary publication:
Structural analysis of the two horseradish peroxidase catalytic residue variants H42E and R38S/H42E: implications for the catalytic cycle.
Meno K, Jennings S, Smith AT, Henriksen A, Gajhede M
Acta Crystallogr D Biol Crystallogr 58 1803-12 (2002)
PMID: 12351824

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-132478 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxidase C1A Chain: A
Molecule details ›
Chain: A
Length: 308 amino acids
Theoretical weight: 33.87 KDa
Source organism: Armoracia rusticana
Expression system: Escherichia coli
UniProt:
  • Canonical: P00433 (Residues: 31-338; Coverage: 95%)
Gene names: HPRC1, PRXC1A
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF
Spacegroup: P212121
Unit cell:
a: 40.4Å b: 66.7Å c: 117.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.168 0.203
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes.
Matsunaga et al. (2004)
2 other articles

1 mention without citation

Hemoglobins Likely Function as Peroxidase in Blood Clam Tegillarca granosa Hemocytes.
Wang et al. (2017)