› 1et8

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF NITRITE REDUCTASE HIS255ASN MUTANT FROM ALCALIGENES FAECALIS

Released:
DOI: 10.2210/pdb1et8/pdb
PDB entry 1et8 coloured by chain, front view.
PDB entry 1et8 coloured by chain, side view.
PDB entry 1et8 coloured by chain, top view.
Source organism: Alcaligenes faecalis
Primary publication:
Catalytic roles for two water bridged residues (Asp-98 and His-255) in the active site of copper-containing nitrite reductase.
Boulanger MJ, Kukimoto M, Nishiyama M, Horinouchi S, Murphy ME
J Biol Chem 275 23957-64 (2000)
PMID: 10811642

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 Chain: A
Molecule details ›
Chain: A
Length: 341 amino acids
Theoretical weight: 36.85 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 2 x CU
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: R3
Unit cell:
a: 127.659Å b: 127.659Å c: 67.215Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.182 0.212
Expression system: Escherichia coli

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Citations

6 review citations

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