› 1oa1

X-ray diffraction
1.55Å resolution

REDUCED HYBRID CLUSTER PROTEIN (HCP) FROM DESULFOVIBRIO VULGARIS HILDENBOROUGH STRUCTURE AT 1.55A RESOLUTION USING SYNCHROTRON RADIATION.

Released:
DOI: 10.2210/pdb1oa1/pdb
PDB entry 1oa1 coloured by chain, front view.
PDB entry 1oa1 coloured by chain, side view.
PDB entry 1oa1 coloured by chain, top view.
Source organism: Desulfovibrio vulgaris
Primary publication:
Reduced hybrid cluster proteins (HCP) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at high resolution using synchrotron radiation.
Aragão D, Macedo S, Mitchell EP, Romão CV, Liu MY, Frazão C, Saraiva LM, Xavier AV, LeGall J, van Dongen WMAM, Hagen WR, Teixeira M, Carrondo MA, Lindley P
J Biol Inorg Chem 8 540-548 (2003)
PMID: 12764602

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: 60.04 KDa
Source organism: Desulfovibrio vulgaris
Expression system: Desulfovibrio vulgaris
UniProt:
  • Canonical: P31101 (Residues: 1-553; Coverage: 100%)
Gene names: DVU_2013, hcp
Sequence domains: Prismane/CO dehydrogenase family
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand SF4 1 x SF4
Ligand SF3 1 x SF3
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 64.053Å b: 67.464Å c: 134.955Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.132 0.131 0.153
Expression system: Desulfovibrio vulgaris

Quick links

Citations

1 review citation

Occurrence, Evolution and Specificities of Iron-Sulfur Proteins and Maturation Factors in Chloroplasts from Algae.
Przybyla-Toscano et al. (2021)
12 other articles

3 mentions without citation

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