› 1aq8

X-ray diffraction
2Å resolution

STRUCTURE OF ALCALIGENES FAECALIS NITRITE REDUCTASE REDUCED WITH ASCORBATE

Released:
DOI: 10.2210/pdb1aq8/pdb
PDB entry 1aq8 coloured by chain, front view.
PDB entry 1aq8 coloured by chain, side view.
PDB entry 1aq8 coloured by chain, top view.
Source organism: Alcaligenes faecalis
Primary publication:
Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. Mechanistic implications.
Murphy ME, Turley S, Adman ET
J Biol Chem 272 28455-60 (1997)
PMID: 9353305

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-153659 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-containing nitrite reductase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 343 amino acids
Theoretical weight: 37.06 KDa
Source organism: Alcaligenes faecalis
Expression system: Escherichia coli
UniProt:
  • Canonical: P38501 (Residues: 34-376; Coverage: 100%)
Gene names: nir, 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
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 61.79Å b: 102.4Å c: 146.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 not available
Expression system: Escherichia coli

Quick links

Citations

17 review citations

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

3 mentions without citation

Electron transfer activity of a de novo designed copper center in a three-helix bundle fold.
Plegaria et al. (2016)
2 more