› 1iqc

X-ray diffraction
1.8Å resolution

Crystal structure of Di-Heme Peroxidase from Nitrosomonas europaea

Released:
DOI: 10.2210/pdb1iqc/pdb
PDB entry 1iqc coloured by chain, front view.
PDB entry 1iqc coloured by chain, side view.
PDB entry 1iqc coloured by chain, top view.
Source organism: Nitrosomonas europaea
Primary publication:
Crystal structure of Nitrosomonas europaea cytochrome c peroxidase and the structural basis for ligand switching in bacterial di-heme peroxidases.
Shimizu H, Schuller DJ, Lanzilotta WN, Sundaramoorthy M, Arciero DM, Hooper AB, Poulos TL
Biochemistry 40 13483-90 (2001)
PMID: 11695895

Function and Biology Details

Reaction catalysed: 
2 ferrocytochrome c + H(2)O(2) = 2 ferricytochrome c + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157361 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c551 peroxidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 308 amino acids
Theoretical weight: 34.02 KDa
Source organism: Nitrosomonas europaea
UniProt:
  • Canonical: P55929 (Residues: 27-334; Coverage: 100%)
Gene names: NE1315, ccp
Sequence domains: Di-haem cytochrome c peroxidase
Structure domains: Cytochrome c-like domain

Ligands and Environments


Cofactor: Ligand HEC 8 x HEC
3 bound ligands:
Ligand CA 5 x CA
Ligand MG 2 x MG
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 88.134Å b: 55.111Å c: 144Å
α: 90° β: 103.6° γ: 90°
R-values:
R R work R free
0.222 0.222 0.257

Quick links

Citations

7 review citations

Heme enzyme structure and function.
Poulos TL. (2014)
6 more

7 mentions without citation

The chemistry and biochemistry of heme c: functional bases for covalent attachment.
Bowman et al. (2008)
6 more