› 1gs8

X-ray diffraction
1.9Å 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:
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: 336 amino acids
Theoretical weight: 36.57 KDa
Source organism: Achromobacter xylosoxidans
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O68601 (Residues: 25-360; Coverage: 100%)
Gene names: O9570_16215, nir, nirK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

2 bound ligands:
Ligand CU 2 x CU
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P63
Unit cell:
a: 79.636Å b: 79.636Å c: 99.867Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.165 0.165 0.207
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Recent structural insights into the function of copper nitrite reductases.
Horrell et al. (2017)
2 more

1 mention without citation

The geometry of Niggli reduction: SAUC - search of alternative unit cells.
McGill et al. (2014)