› 5og6

X-ray diffraction
1.85Å resolution

Cu nitrite reductase serial data at varying temperatures RT 0.24MGy

Released:
DOI: 10.2210/pdb5og6/pdb
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PDB entry 5og6 coloured by chain, front view.
PDB entry 5og6 coloured by chain, side view.
PDB entry 5og6 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
OpenAccess logo 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

4 bound ligands:
Ligand CU 2 x CU
Ligand ACT 1 x ACT
Ligand NO2 5 x NO2
Ligand NO 1 x NO
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P213
Unit cell:
a: 96.259Å b: 96.259Å c: 96.259Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.177 0.223
Expression system: Escherichia coli

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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)

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