› 3wi9

X-ray diffraction
1.3Å resolution

Crystal structure of copper nitrite reductase from Geobacillus kaustophilus

Released:
DOI: 10.2210/pdb3wi9/pdb
PDB entry 3wi9 coloured by chain, front view.
PDB entry 3wi9 coloured by chain, side view.
PDB entry 3wi9 coloured by chain, top view.
Source organism: Geobacillus kaustophilus HTA426
Primary publication:
Structural and functional characterization of the Geobacillus copper nitrite reductase: involvement of the unique N-terminal region in the interprotein electron transfer with its redox partner.
Fukuda Y, Koteishi H, Yoneda R, Tamada T, Takami H, Inoue T, Nojiri M
Biochim Biophys Acta 1837 396-405 (2014)
PMID: 24440558

Function and Biology Details

Reaction catalysed: 
Nitric oxide + H(2)O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H(+)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177413 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-containing nitrite reductase Chain: A
Molecule details ›
Chain: A
Length: 324 amino acids
Theoretical weight: 35.51 KDa
Source organism: Geobacillus kaustophilus HTA426
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5L1X8 (Residues: 32-354; Coverage: 96%)
Gene name: GK0767
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

6 bound ligands:
Ligand CU 2 x CU
Ligand ZN 3 x ZN
Ligand NA 2 x NA
Ligand ACY 1 x ACY
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 BL38B1
Spacegroup: R3
Unit cell:
a: 115.069Å b: 115.069Å c: 87.505Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.182 0.197
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Recent structural insights into the function of copper nitrite reductases.
Horrell et al. (2017)
4 other articles

1 mention without citation

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