› 2xx1

X-ray diffraction
3Å resolution

STRUCTURE OF THE N90S MUTANT OF NITRITE REDUCTASE FROM ALCALIGENES XYLOSOXIDANS complexed with nitrite

Released:
DOI: 10.2210/pdb2xx1/pdb
PDB entry 2xx1 coloured by chain, front view.
PDB entry 2xx1 coloured by chain, side view.
PDB entry 2xx1 coloured by chain, top view.
Source organism: Achromobacter xylosoxidans
Primary publication:
Proton-coupled electron transfer in the catalytic cycle of Alcaligenes xylosoxidans copper-dependent nitrite reductase.
Leferink NG, Han C, Antonyuk SV, Heyes DJ, Rigby SE, Hough MA, Eady RR, Scrutton NS, Hasnain SS
Biochemistry 50 4121-31 (2011)
PMID: 21469743

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 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 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 336 amino acids
Theoretical weight: 36.54 KDa
Source organism: Achromobacter xylosoxidans
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O68601 (Residues: 26-360; Coverage: 100%)
Gene names: O9570_16215, nir, nirK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

3 bound ligands:
Ligand CU 12 x CU
Ligand NO2 6 x NO2
Ligand SO4 21 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P212121
Unit cell:
a: 172.67Å b: 174.65Å c: 180.65Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.185 0.221
Expression system: Escherichia coli BL21

Quick links

Citations

8 review citations

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

1 mention without citation

Copper active sites in biology.
Solomon et al. (2014)