› 2ppc

X-ray diffraction
1.58Å resolution

Oxidized wild type AfNiR exposed to NO (nitrite bound)

Released:
DOI: 10.2210/pdb2ppc/pdb
PDB entry 2ppc coloured by chain, front view.
PDB entry 2ppc coloured by chain, side view.
PDB entry 2ppc coloured by chain, top view.
Source organism: Alcaligenes faecalis
Primary publication:
Stable copper-nitrosyl formation by nitrite reductase in either oxidation state.
Tocheva EI, Rosell FI, Mauk AG, Murphy ME
Biochemistry 46 12366-74 (2007)
PMID: 17924665

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 BL21(DE3)
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 NO2 3 x NO2
Ligand ACT 10 x ACT
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 61.111Å b: 101.833Å c: 145.508Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.161 0.182
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Binding and activation of nitrite and nitric oxide by copper nitrite reductase and corresponding model complexes.
Merkle et al. (2012)
2 more

1 mention without citation

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