› 1bq5

X-ray diffraction
2.05Å resolution

Function and Biology Details

Reaction catalysed: 
Nitric oxide + H(2)O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H(+)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130622 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-containing nitrite reductase Chain: A
Molecule details ›
Chain: A
Length: 342 amino acids
Theoretical weight: 37.13 KDa
Source organism: Achromobacter xylosoxidans
UniProt:
  • Canonical: O68601 (Residues: 19-360; Coverage: 100%)
Gene names: O9570_16215, nir, nirK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

1 bound ligand:
Ligand CU 2 x CU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P63
Unit cell:
a: 106.565Å b: 106.565Å c: 63.578Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.18 0.226

Quick links

Citations

27 citation in other articles

Crystal structure of the soluble domain of the major anaerobically induced outer membrane protein (AniA) from pathogenic Neisseria: a new class of copper-containing nitrite reductases.
Boulanger et al. (2002)
26 more

1 mention without citation

Expression, purification, crystallization and preliminary X-ray diffraction analysis of the soluble domain of PPA0092, a putative nitrite reductase from Propionibacterium acnes.
Nojiri et al. (2009)