› 1w9m

X-ray diffraction
1.35Å resolution

AS-isolated hybrid cluster protein from Desulfovibrio vulgaris X-ray structure at 1.35A resolution using iron anomalous signal

Released:
DOI: 10.2210/pdb1w9m/pdb
PDB entry 1w9m coloured by chain, front view.
PDB entry 1w9m coloured by chain, side view.
PDB entry 1w9m coloured by chain, top view.
Source organism: Desulfovibrio vulgaris str. Hildenborough
Primary publication:
Structural and functional relationships in the hybrid cluster protein family: structure of the anaerobically purified hybrid cluster protein from Desulfovibrio vulgaris at 1.35 A resolution.
Aragão D, Mitchell EP, Frazão CF, Carrondo MA, Lindley PF
Acta Crystallogr D Biol Crystallogr 64 665-74 (2008)
PMID: 18560155

Function and Biology Details

Reaction catalysed: 
NH(3) + H(2)O + acceptor = hydroxylamine + reduced acceptor
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151906 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydroxylamine reductase Chain: A
Molecule details ›
Chain: A
Length: 553 amino acids
Theoretical weight: 60.07 KDa
Source organism: Desulfovibrio vulgaris str. Hildenborough
Expression system: Desulfovibrio vulgaris str. Hildenborough
UniProt:
  • Canonical: P31101 (Residues: 1-553; Coverage: 100%)
Gene names: DVU_2013, hcp
Sequence domains: Prismane/CO dehydrogenase family
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SF4 1 x SF4
Ligand FS2 1 x FS2
1 modified residue:
Ligand CSS 1 x CSS

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 64.27Å b: 66.843Å c: 134.764Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.125 not available 0.177
Expression system: Desulfovibrio vulgaris str. Hildenborough

Quick links

Citations

1 review citation

Molecular understanding of heteronuclear active sites in heme-copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling.
Reed et al. (2021)
8 other articles

4 mentions without citation

Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.
Liu et al. (2014)
3 more