› 6wh6

X-ray diffraction
2.25Å resolution

Crystal structure of human sulfide quinone oxidoreductase in complex with coenzyme Q (cyanide soaked)

Released:
DOI: 10.2210/pdb6wh6/pdb
PDB entry 6wh6 coloured by chain, front view.
PDB entry 6wh6 coloured by chain, side view.
PDB entry 6wh6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Dismantling and Rebuilding the Trisulfide Cofactor Demonstrates Its Essential Role in Human Sulfide Quinone Oxidoreductase.
Landry AP, Moon S, Bonanata J, Cho US, Coitiño EL, Banerjee R
J Am Chem Soc 142 14295-14306 (2020)
PMID: 32787249

Function and Biology Details

Reaction catalysed: 
Hydrogen sulfide + glutathione + a quinone = S-sulfanylglutathione + a quinol
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195376 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sulfide:quinone oxidoreductase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 418 amino acids
Theoretical weight: 47.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y6N5 (Residues: 42-450; Coverage: 91%)
Gene names: CGI-44, SQOR, SQRDL
Sequence domains: Pyridine nucleotide-disulphide oxidoreductase

Ligands and Environments

3 bound ligands:
Ligand FAD 2 x FAD
Ligand CYN 2 x CYN
Ligand UQ1 3 x UQ1
1 modified residue:
Ligand CSS 2 x CSS

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P212121
Unit cell:
a: 78.393Å b: 111.746Å c: 134.046Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.216
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Hydrogen Sulfide Oxidation by Sulfide Quinone Oxidoreductase.
Landry et al. (2021)
3 more

2 mentions without citation

Structural perspectives on H2S homeostasis.
Landry et al. (2021)
1 more