› 1nid

X-ray diffraction
2.2Å 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/pdb1nid/pdb
PDB entry 1nid coloured by chain, front view.
PDB entry 1nid coloured by chain, side view.
PDB entry 1nid 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 Chain: A
Molecule details ›
Chain: A
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

2 bound ligands:
Ligand CU 2 x CU
Ligand NO2 1 x NO2
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P213
Unit cell:
a: 97.6Å b: 97.6Å c: 97.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.149 not available

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Citations

13 review citations

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

3 mentions without citation

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