› 5i6m

X-ray diffraction
1.09Å resolution

Crystal Structure of Copper Nitrite Reductase at 100K after 7.59 MGy

Released:
DOI: 10.2210/pdb5i6m/pdb
PDB entry 5i6m coloured by chain, front view.
PDB entry 5i6m coloured by chain, side view.
PDB entry 5i6m coloured by chain, top view.
Source organism: Achromobacter cycloclastes
Primary publication:
Serial crystallography captures enzyme catalysis in copper nitrite reductase at atomic resolution from one crystal.
Horrell S, Antonyuk SV, Eady RR, Hasnain SS, Hough MA, Strange RW
IUCrJ 3 271-81 (2016)
PMID: 27437114

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: 332 amino acids
Theoretical weight: 36.39 KDa
Source organism: Achromobacter cycloclastes
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P25006 (Residues: 46-377; Coverage: 98%)
Gene name: nirK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

5 bound ligands:
Ligand CU 2 x CU
Ligand ACT 1 x ACT
Ligand MLI 1 x MLI
Ligand NO2 7 x NO2
Ligand NO 1 x NO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P213
Unit cell:
a: 95.155Å b: 95.155Å c: 95.155Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.128 0.127 0.146
Expression system: Escherichia coli BL21(DE3)

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Citations

5 review citations

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

1 mention without citation

Serial crystallography captures enzyme catalysis in copper nitrite reductase at atomic resolution from one crystal.
Horrell et al. (2016)