PDBe 1snr

X-ray diffraction
1.31Å resolution

Nitric oxide bound to Cu nitrite reductase

Released:
Source organism: Alcaligenes faecalis
Primary publication:
Side-on copper-nitrosyl coordination by nitrite reductase.
Science 304 867-70 (2004)
PMID: 15131305

Function and Biology Details

Reaction catalysed:
Nitric oxide + H(2)O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H(+). 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-containing nitrite reductase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 341 amino acids
Theoretical weight: 36.88 KDa
Source organism: Alcaligenes faecalis
Expression system: Escherichia coli
UniProt:
  • Canonical: P38501 (Residues: 40-376; Coverage: 98%)
Gene names: nir, nirK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 61.726Å b: 102.595Å c: 145.652Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.125 0.124 0.141
Expression system: Escherichia coli