› 1fgj

X-ray diffraction
2.8Å resolution

X-RAY STRUCTURE OF HYDROXYLAMINE OXIDOREDUCTASE

Released:
DOI: 10.2210/pdb1fgj/pdb
PDB entry 1fgj coloured by chain, front view.
PDB entry 1fgj coloured by chain, side view.
PDB entry 1fgj coloured by chain, top view.
Source organism: Nitrosomonas europaea
Primary publication:
The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea.
Igarashi N, Moriyama H, Fujiwara T, Fukumori Y, Tanaka N
Nat Struct Biol 4 276-84 (1997)
PMID: 9095195

Function and Biology Details

Reaction catalysed: 
Hydroxylamine + 3 ferricytochrome c = nitric oxide + 3 ferrocytochrome c + 3 H(+)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175889 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydroxylamine oxidoreductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 546 amino acids
Theoretical weight: 61.74 KDa
Source organism: Nitrosomonas europaea
UniProt:
  • Canonical: Q50925 (Residues: 25-570; Coverage: 100%)
Gene names: NE0962, NE2044, NE2339, hao1, hao2, hao3
Sequence domains: Seven times multi-haem cytochrome CxxCH
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 14 x HEM

Cofactor: Ligand HEC 2 x HEC
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P63
Unit cell:
a: 96.2Å b: 96.2Å c: 265.7Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.23 0.23 0.309

Quick links

Citations

22 review citations

Cell biology and molecular basis of denitrification.
Zumft WG. (1997)
21 more

13 mentions without citation

Multi-heme proteins: nature's electronic multi-purpose tool.
Bewley et al. (2013)
12 more