4kdc

X-ray diffraction
2.09Å resolution

Crystal Structure of UBIG

Released:

Function and Biology Details

Reactions catalysed:
S-adenosyl-L-methionine + 3-(all-trans-polyprenyl)benzene-1,2-diol = S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-polyprenyl)phenol
S-adenosyl-L-methionine + 3-demethylubiquinone-n = S-adenosyl-L-homocysteine + ubiquinone-n
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-148239 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquinone biosynthesis O-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 246 amino acids
Theoretical weight: 27.42 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P17993 (Residues: 1-240; Coverage: 100%)
Gene names: JW2226, b2232, pufX, ubiG, yfaB
Sequence domains: Methyltransferase domain
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: C2
Unit cell:
a: 119.848Å b: 58.584Å c: 40.168Å
α: 90° β: 105.26° γ: 90°
R-values:
R R work R free
0.185 0.183 0.225
Expression system: Escherichia coli