› 2bw5

X-ray diffraction
1.12Å resolution

Atomic Resolution Structure of NO-bound Achromobacter cycloclastes Cu Nitrite Reductase

Released:
DOI: 10.2210/pdb2bw5/pdb
PDB entry 2bw5 coloured by chain, front view.
PDB entry 2bw5 coloured by chain, side view.
PDB entry 2bw5 coloured by chain, top view.
Source organism: Achromobacter cycloclastes
Primary publication:
Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism.
Antonyuk SV, Strange RW, Sawers G, Eady RR, Hasnain SS
Proc Natl Acad Sci U S A 102 12041-6 (2005)
PMID: 16093314

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-150327 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-containing nitrite reductase Chain: A
Molecule details ›
Chain: A
Length: 340 amino acids
Theoretical weight: 37.06 KDa
Source organism: Achromobacter cycloclastes
UniProt:
  • Canonical: P25006 (Residues: 39-378; Coverage: 100%)
Gene name: nirK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

5 bound ligands:
Ligand CU 2 x CU
Ligand HOA 1 x HOA
Ligand MLI 1 x MLI
Ligand ACT 4 x ACT
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P213
Unit cell:
a: 95.334Å b: 95.334Å c: 95.334Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.129 0.128 0.164

Quick links

Citations

12 review citations

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

3 mentions without citation

Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism.
Antonyuk et al. (2005)
2 more