› 6gtk

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:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150327 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-containing nitrite reductase Chain: A
Molecule details ›
Chain: A
Length: 378 amino acids
Theoretical weight: 40.82 KDa
Source organism: Achromobacter cycloclastes
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P25006 (Residues: 1-378; Coverage: 100%)
Gene name: nirK
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand CU 2 x CU
Ligand NO2 1 x NO2
Ligand MLI 2 x MLI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P213
Unit cell:
a: 95.47Å b: 95.47Å c: 95.47Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.16 0.185
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography.
Schröder et al. (2021)
8 other articles

2 mentions without citation

Catalytically important damage-free structures of a copper nitrite reductase obtained by femtosecond X-ray laser and room-temperature neutron crystallography.
Halsted et al. (2019)
1 more