› 1oe1

X-ray diffraction
1.04Å resolution

Atomic Resolution Structure of the Wildtype Native Nitrite Reductase from Alcaligenes xylosoxidans

Released:
DOI: 10.2210/pdb1oe1/pdb
PDB entry 1oe1 coloured by chain, front view.
PDB entry 1oe1 coloured by chain, side view.
PDB entry 1oe1 coloured by chain, top view.
Source organism: Achromobacter xylosoxidans
Primary publication:
Atomic resolution structures of native copper nitrite reductase from Alcaligenes xylosoxidans and the active site mutant Asp92Glu.
Ellis MJ, Dodd FE, Sawers G, Eady RR, Hasnain SS
J Mol Biol 328 429-38 (2003)
PMID: 12691751

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: 36.55 KDa
Source organism: Achromobacter xylosoxidans
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 PG4 1 x PG4
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.2
Spacegroup: P63
Unit cell:
a: 78.725Å b: 78.725Å c: 98.885Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.118 not available 0.142

Quick links

Citations

4 review citations

Binding and activation of nitrite and nitric oxide by copper nitrite reductase and corresponding model complexes.
Merkle et al. (2012)
3 more

12 mentions without citation

Tracking electrons in biological macromolecules: from ensemble to single molecule.
Tabares et al. (2014)
11 more