› 4csz

X-ray diffraction
1.75Å resolution

STRUCTURE OF F306C MUTANT OF NITRITE REDUCTASE FROM Achromobacter XYLOSOXIDANS WITH NITRITE BOUND

Released:
DOI: 10.2210/pdb4csz/pdb
PDB entry 4csz coloured by chain, front view.
PDB entry 4csz coloured by chain, side view.
PDB entry 4csz coloured by chain, top view.
Source organism: Achromobacter xylosoxidans
Primary publication:
Impact of residues remote from the catalytic centre on enzyme catalysis of copper nitrite reductase.
Leferink NG, Antonyuk SV, Houwman JA, Scrutton NS, Eady RR, Hasnain SS
Nat Commun 5 4395 (2014)
PMID: 25022223

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-130622 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-containing nitrite reductase Chain: A
Molecule details ›
Chain: A
Length: 335 amino acids
Theoretical weight: 36.4 KDa
Source organism: Achromobacter xylosoxidans
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O68601 (Residues: 26-360; Coverage: 100%)
Gene names: O9570_16215, nir, nirK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

4 bound ligands:
Ligand ZN 7 x ZN
Ligand CU 2 x CU
Ligand NO2 1 x NO2
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: R3
Unit cell:
a: 89.57Å b: 89.57Å c: 144.011Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.178 0.21
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.
Currin et al. (2015)
3 more

1 mention without citation

Impact of residues remote from the catalytic centre on enzyme catalysis of copper nitrite reductase.
Leferink et al. (2014)