› 1l9q

X-ray diffraction
1.7Å resolution

CRYSTAL STRUCTURE OF THE I257L VARIANT OF THE COPPER-CONTAINING NITRITE REDUCTASE FROM ALCALIGENES FAECALIS S-6

Released:
DOI: 10.2210/pdb1l9q/pdb
PDB entry 1l9q coloured by chain, front view.
PDB entry 1l9q coloured by chain, side view.
PDB entry 1l9q coloured by chain, top view.
Source organism: Alcaligenes faecalis
Primary publication:
Directing the mode of nitrite binding to a copper-containing nitrite reductase from Alcaligenes faecalis S-6: characterization of an active site isoleucine.
Boulanger MJ, Murphy ME
Protein Sci 12 248-56 (2003)
PMID: 12538888

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 domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153659 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-containing nitrite reductase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 341 amino acids
Theoretical weight: 36.88 KDa
Source organism: Alcaligenes faecalis
Expression system: Escherichia coli
UniProt:
  • Canonical: P38501 (Residues: 40-376; Coverage: 98%)
Gene names: nir, nirK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

2 bound ligands:
Ligand CU 6 x CU
Ligand NO2 3 x NO2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 61.95Å b: 102.48Å c: 146.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.156 0.188
Expression system: Escherichia coli

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Citations

3 review citations

Copper active sites in biology.
Solomon et al. (2014)
2 more