› 1nib

X-ray diffraction
2.7Å resolution

THE STRUCTURE OF CU-NITRITE REDUCTASE FROM ACHROMOBACTER CYCLOCLASTES AT FIVE PH VALUES, WITH NITRITE BOUND AND WITH TYPE II CU DEPLETED

Released:
DOI: 10.2210/pdb1nib/pdb
PDB entry 1nib coloured by chain, front view.
PDB entry 1nib coloured by chain, side view.
PDB entry 1nib coloured by chain, top view.
Source organism: Achromobacter cycloclastes
Primary publication:
The structure of copper-nitrite reductase from Achromobacter cycloclastes at five pH values, with NO2- bound and with type II copper depleted.
Adman ET, Godden JW, Turley S
J Biol Chem 270 27458-74 (1995)
PMID: 7499203

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-150327 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-containing nitrite reductase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 340 amino acids
Theoretical weight: 37.06 KDa
Source organism: Achromobacter cycloclastes
UniProt:
  • Canonical: P25006 (Residues: 39-378; Coverage: 100%)
Gene name: nirK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

1 bound ligand:
Ligand CU 6 x CU
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 99.56Å b: 115.36Å c: 115.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.155 not available

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Citations

14 review citations

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

6 mentions without citation

Analysis of gene expression in Parkinson's disease: possible involvement of neurotrophic support and axon guidance in dopaminergic cell death.
Bossers et al. (2009)
5 more