› 2vmj

X-ray diffraction
2.5Å resolution

Type 1 Copper-Binding Loop of Nitrite Reductase mutant: 130- CAPEGMVPWHVVSGM-144 to 130-CTPHPFM-136

Released:
DOI: 10.2210/pdb2vmj/pdb
PDB entry 2vmj coloured by chain, front view.
PDB entry 2vmj coloured by chain, side view.
PDB entry 2vmj coloured by chain, top view.
Source organism: Achromobacter xylosoxidans
Primary publication:
The importance of the long type 1 copper-binding loop of nitrite reductase for structure and function.
Sato K, Firbank SJ, Li C, Banfield MJ, Dennison C
Chemistry 14 5820-8 (2008)
PMID: 18491346

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: 329 amino acids
Theoretical weight: 35.93 KDa
Source organism: Achromobacter xylosoxidans
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O68601 (Residues: 25-360; Coverage: 98%)
Gene names: O9570_16215, nir, nirK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

2 bound ligands:
Ligand ZN 3 x ZN
Ligand EPE 1 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: R3
Unit cell:
a: 89.813Å b: 89.813Å c: 143.099Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.181 0.232
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.
Van Stappen et al. (2022)
1 other article