› 4yso

X-ray diffraction
1.5Å resolution

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 analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107338 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-containing nitrite reductase Chain: A
Molecule details ›
Chain: A
Length: 323 amino acids
Theoretical weight: 35.52 KDa
Source organism: Geobacillus thermodenitrificans NG80-2
Expression system: Escherichia coli
UniProt:
  • Canonical: A4IL26 (Residues: 31-352; Coverage: 97%)
Gene names: GTNG_0650, nirK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

3 bound ligands:
Ligand CU 7 x CU
Ligand MPD 1 x MPD
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL32XU
Spacegroup: R3
Unit cell:
a: 114.771Å b: 114.771Å c: 84.098Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.132 0.129 0.177
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Recent structural insights into the function of copper nitrite reductases.
Horrell et al. (2017)
2 more

2 mentions without citation

The Sec System: Protein Export in Escherichia coli.
Crane et al. (2017)
1 more