› 5ofd

X-ray diffraction
1.77Å resolution

Cu nitrite reductase serial data at varying temperatures 190K 0.48MGy

Released:
DOI: 10.2210/pdb5ofd/pdb
PDB entry 5ofd coloured by chain, front view.
PDB entry 5ofd coloured by chain, side view.
PDB entry 5ofd coloured by chain, top view.
Source organism: Achromobacter cycloclastes
Primary publication:
Enzyme catalysis captured using multiple structures from one crystal at varying temperatures.
Horrell S, Kekilli D, Sen K, Owen RL, Dworkowski FSN, Antonyuk SV, Keal TW, Yong CW, Eady RR, Hasnain SS, Strange RW, Hough MA
IUCrJ 5 283-292 (2018)
PMID: 29755744

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-150327 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-containing nitrite reductase Chain: A
Molecule details ›
Chain: A
Length: 334 amino acids
Theoretical weight: 36.62 KDa
Source organism: Achromobacter cycloclastes
Expression system: Escherichia coli
UniProt:
  • Canonical: P25006 (Residues: 45-378; Coverage: 98%)
Gene name: nirK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

2 bound ligands:
Ligand CU 2 x CU
Ligand NO 1 x NO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P213
Unit cell:
a: 95.022Å b: 95.022Å c: 95.022Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.201 0.226
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

1 mention without citation

Enzyme catalysis captured using multiple structures from one crystal at varying temperatures.
Horrell et al. (2018)