› 2gmj

X-ray diffraction
2.6Å resolution

Structure of Porcine Electron Transfer Flavoprotein-Ubiquinone Oxidoreductase

Released:
DOI: 10.2210/pdb2gmj/pdb
PDB entry 2gmj coloured by chain, front view.
PDB entry 2gmj coloured by chain, side view.
PDB entry 2gmj coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool.
Zhang J, Frerman FE, Kim JJ
Proc Natl Acad Sci U S A 103 16212-7 (2006)
PMID: 17050691

Function and Biology Details

Reaction catalysed: 
Reduced electron-transferring flavoprotein + ubiquinone = electron-transferring flavoprotein + ubiquinol
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157362 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 584 amino acids
Theoretical weight: 64.93 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P55931 (Residues: 34-617; Coverage: 95%)
Gene name: ETFDH
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
2 bound ligands:
Ligand SF4 2 x SF4
Ligand TBU 6 x TBU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P4212
Unit cell:
a: 154.839Å b: 154.839Å c: 130.199Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.228 0.255

Quick links

Citations

26 review citations

The function and the role of the mitochondrial glycerol-3-phosphate dehydrogenase in mammalian tissues.
Mráček et al. (2013)
25 more

2 mentions without citation

On the Natural History of Flavin-Based Electron Bifurcation.
Baymann et al. (2018)
1 more