› 2fjs

X-ray diffraction
1.85Å resolution

Crystal Structure of Anaerobically Reduced Wild Type Nitrite Reductase from A. faecalis

Released:
DOI: 10.2210/pdb2fjs/pdb
PDB entry 2fjs coloured by chain, front view.
PDB entry 2fjs coloured by chain, side view.
PDB entry 2fjs coloured by chain, top view.
Source organism: Alcaligenes faecalis
Primary publication:
Effect of the methionine ligand on the reorganization energy of the type-1 copper site of nitrite reductase.
Wijma HJ, MacPherson I, Farver O, Tocheva EI, Pecht I, Verbeet MP, Murphy ME, Canters GW
J Am Chem Soc 129 519-25 (2007)
PMID: 17227014

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: 337 amino acids
Theoretical weight: 36.42 KDa
Source organism: Alcaligenes faecalis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P38501 (Residues: 40-376; Coverage: 98%)
Gene names: nir, nirK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

4 bound ligands:
Ligand CU1 3 x CU1
Ligand CU 3 x CU
Ligand ACT 10 x ACT
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 61.552Å b: 102.428Å c: 145.744Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.152 0.15 0.18
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Mechanisms for control of biological electron transfer reactions.
Williamson et al. (2014)
1 more