› 3sy4

X-ray diffraction
1.91Å resolution

Crystal structure of sulfide:quinone oxidoreductase Ser126Ala variant from Acidithiobacillus ferrooxidans

Released:
DOI: 10.2210/pdb3sy4/pdb
PDB entry 3sy4 coloured by chain, front view.
PDB entry 3sy4 coloured by chain, side view.
PDB entry 3sy4 coloured by chain, top view.
Source organism: Acidithiobacillus ferrooxidans ATCC 23270
Primary publication:
Structure-activity characterization of sulfide:quinone oxidoreductase variants.
Cherney MM, Zhang Y, James MN, Weiner JH
J Struct Biol 178 319-28 (2012)
PMID: 22542586

Function and Biology Details

Reaction catalysed: 
n sulfide + n quinone = polysulfide + n quinol
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110497 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sulfide-quinone reductase Chain: A
Molecule details ›
Chain: A
Length: 437 amino acids
Theoretical weight: 47.75 KDa
Source organism: Acidithiobacillus ferrooxidans ATCC 23270
Expression system: Escherichia coli
UniProt:
  • Canonical: B7JBP8 (Residues: 2-434; Coverage: 100%)
Gene name: AFE_1792
Sequence domains: Pyridine nucleotide-disulphide oxidoreductase
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
3 bound ligands:
Ligand LMT 1 x LMT
Ligand H2S 5 x H2S
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P6222
Unit cell:
a: 149.766Å b: 149.766Å c: 81.73Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.175 0.173 0.215
Expression system: Escherichia coli

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Citations

5 review citations

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