› 2afn

X-ray diffraction
2Å resolution

STRUCTURE OF ALCALIGENES FAECALIS NITRITE REDUCTASE AND A COPPER SITE MUTANT, M150E, THAT CONTAINS ZINC

Released:
DOI: 10.2210/pdb2afn/pdb
Model geometry
Fit model/data
PDB entry 2afn coloured by chain, front view.
PDB entry 2afn coloured by chain, side view.
PDB entry 2afn coloured by chain, top view.
Source organism: Alcaligenes faecalis
Primary publication:
Structure of Alcaligenes faecalis nitrite reductase and a copper site mutant, M150E, that contains zinc.
Murphy ME, Turley S, Kukimoto M, Nishiyama M, Horinouchi S, Sasaki H, Tanokura M, Adman ET
Biochemistry 34 12107-17 (1995)
PMID: 7547950

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: 343 amino acids
Theoretical weight: 37.06 KDa
Source organism: Alcaligenes faecalis
UniProt:
  • Canonical: P38501 (Residues: 34-376; Coverage: 100%)
Gene names: nir, nirK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

1 bound ligand:
Ligand CU 6 x CU
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
Spacegroup: P212121
Unit cell:
a: 63.035Å b: 103.61Å c: 146.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.158 0.223

Quick links

Citations

5 review citations

Protein design: toward functional metalloenzymes.
Yu et al. (2014)
4 more

5 mentions without citation

Spectroscopic and computational studies of nitrite reductase: proton induced electron transfer and backbonding contributions to reactivity.
Ghosh et al. (2009)
4 more