› 2xxf

X-ray diffraction
1.5Å resolution

Cu metallated H254F mutant of nitrite reductase

Released:
DOI: 10.2210/pdb2xxf/pdb
PDB entry 2xxf coloured by chain, front view.
PDB entry 2xxf coloured by chain, side view.
PDB entry 2xxf coloured by chain, top view.
Source organism: Achromobacter xylosoxidans
Primary publication:
Proton-coupled electron transfer in the catalytic cycle of Alcaligenes xylosoxidans copper-dependent nitrite reductase.
Leferink NG, Han C, Antonyuk SV, Heyes DJ, Rigby SE, Hough MA, Eady RR, Scrutton NS, Hasnain SS
Biochemistry 50 4121-31 (2011)
PMID: 21469743

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 336 amino acids
Theoretical weight: 36.58 KDa
Source organism: Achromobacter xylosoxidans
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O68601 (Residues: 26-360; Coverage: 100%)
Gene names: O9570_16215, nir, nirK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

5 bound ligands:
Ligand CU 4 x CU
Ligand ZN 6 x ZN
Ligand PEG 7 x PEG
Ligand MES 4 x MES
Ligand PG4 2 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: R3
Unit cell:
a: 89.333Å b: 89.333Å c: 287.851Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.146 0.145 0.176
Expression system: Escherichia coli BL21

Quick links

Citations

9 review citations

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

1 mention without citation

Outlier analyses of the Protein Data Bank archive using a probability-density-ranking approach.
Shao et al. (2018)