› 1snr

X-ray diffraction
1.31Å resolution

Nitric oxide bound to Cu nitrite reductase

Released:
DOI: 10.2210/pdb1snr/pdb
PDB entry 1snr coloured by chain, front view.
PDB entry 1snr coloured by chain, side view.
PDB entry 1snr coloured by chain, top view.
Source organism: Alcaligenes faecalis
Primary publication:
Side-on copper-nitrosyl coordination by nitrite reductase.
Tocheva EI, Rosell FI, Mauk AG, Murphy ME
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:
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: 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

5 bound ligands:
Ligand CU1 3 x CU1
Ligand CU 3 x CU
Ligand ACT 8 x ACT
Ligand NO 3 x NO
Ligand TRS 1 x TRS
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

Quick links

Citations

12 review citations

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

4 mentions without citation

The Rise of Radicals in Bioinorganic Chemistry.
Gray et al. (2016)
3 more