› 3zow

X-ray diffraction
2.35Å resolution

Crystal Structure of Wild Type Nitrosomonas europaea Cytochrome c552

Released:
DOI: 10.2210/pdb3zow/pdb
PDB entry 3zow coloured by chain, front view.
PDB entry 3zow coloured by chain, side view.
PDB entry 3zow coloured by chain, top view.
Source organism: Nitrosomonas europaea
Primary publication:
Structural characterization of nitrosomonas europaea cytochrome c-552 variants with marked differences in electronic structure.
Can M, Krucinska J, Zoppellaro G, Andersen NH, Wedekind JE, Hersleth HP, Andersson KK, Bren KL
Chembiochem 14 1828-38 (2013)
PMID: 23908017

Function and Biology Details

Reaction catalysed: 
NH(3) + 2 H(2)O + 6 ferricytochrome c = nitrite + 6 ferrocytochrome c + 7 H(+)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161152 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c-552 Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R
Length: 81 amino acids
Theoretical weight: 8.49 KDa
Source organism: Nitrosomonas europaea
UniProt:
  • Canonical: P95339 (Residues: 23-103; Coverage: 100%)
Gene names: NE0102, cyt, cyt_c552
Sequence domains: Cytochrome c
Structure domains: Cytochrome c-like domain

Ligands and Environments


Cofactor: Ligand HEC 18 x HEC
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 59.45Å b: 137.93Å c: 204.66Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.201 0.258

Quick links

Citations

5 citation in other articles

Structure of a mitochondrial cytochrome c conformer competent for peroxidase activity.
McClelland et al. (2014)
4 more

3 mentions without citation

Structural characterization of nitrosomonas europaea cytochrome c-552 variants with marked differences in electronic structure.
Can et al. (2013)
2 more