› 3hyw

X-ray diffraction
2Å resolution

3-D X-Ray structure of the sulfide:quinone oxidoreductase of the hyperthermophilic bacterium Aquifex aeolicus in complex with decylubiquinone

Released:
DOI: 10.2210/pdb3hyw/pdb
PDB entry 3hyw coloured by chain, front view.
PDB entry 3hyw coloured by chain, side view.
PDB entry 3hyw coloured by chain, top view.
Source organism: Aquifex aeolicus
Primary publication:
The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration.
Marcia M, Ermler U, Peng G, Michel H
Proc Natl Acad Sci U S A 106 9625-30 (2009)
PMID: 19487671

Function and Biology Details

Reaction catalysed: 
n sulfide + n quinone = polysulfide + n quinol
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-130591 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sulfide-quinone reductase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 430 amino acids
Theoretical weight: 47.57 KDa
Source organism: Aquifex aeolicus
UniProt:
  • Canonical: O67931 (Residues: 1-430; Coverage: 100%)
Gene names: aq_2186, sqr
Sequence domains: Pyridine nucleotide-disulphide oxidoreductase
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments


Cofactor: Ligand FAD 6 x FAD
5 bound ligands:
Ligand DCQ 6 x DCQ
Ligand LMT 6 x LMT
Ligand H2S 6 x H2S
Ligand PS9 8 x PS9
Ligand SO4 24 x SO4
1 modified residue:
Ligand CSS 12 x CSS

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 110.78Å b: 154.01Å c: 175.55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.2 0.236

Quick links

Citations

14 review citations

Chemical Biology of H2S Signaling through Persulfidation.
Filipovic et al. (2018)
13 more

9 mentions without citation

Enzymology of H2S biogenesis, decay and signaling.
Kabil et al. (2014)
8 more