› 1aof

X-ray diffraction
2Å resolution

CYTOCHROME CD1 NITRITE REDUCTASE, REDUCED FORM

Released:
DOI: 10.2210/pdb1aof/pdb
PDB entry 1aof coloured by chain, front view.
PDB entry 1aof coloured by chain, side view.
PDB entry 1aof coloured by chain, top view.
Source organism: Paracoccus pantotrophus
Primary publication:
Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme.
Williams PA, Fülöp V, Garman EF, Saunders NF, Ferguson SJ, Hajdu J
Nature 389 406-12 (1997)
PMID: 9311786

Function and Biology Details

Reactions catalysed: 
Nitric oxide + H(2)O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H(+)
NH(3) + H(2)O + acceptor = hydroxylamine + reduced acceptor
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159836 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nitrite reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 567 amino acids
Theoretical weight: 62.61 KDa
Source organism: Paracoccus pantotrophus
UniProt:
  • Canonical: P72181 (Residues: 30-596; Coverage: 100%)
Gene name: nirS
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM

Cofactor: Ligand DHE 2 x DHE
1 bound ligand:
Ligand SO2 2 x SO2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: P21
Unit cell:
a: 107.4Å b: 61.7Å c: 101.2Å
α: 90° β: 112.1° γ: 90°
R-values:
R R work R free
0.17 0.17 0.201

Quick links

Citations

18 review citations

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

6 mentions without citation

Nitric Oxide, Nitric Oxide Formers and Their Physiological Impacts in Bacteria.
Chen et al. (2022)
5 more