› 5dpm

X-ray diffraction
2.1Å resolution

Crystal structure of UbiG mutant in complex with SAH

Released:
DOI: 10.2210/pdb5dpm/pdb
PDB entry 5dpm coloured by chain, front view.
PDB entry 5dpm coloured by chain, side view.
PDB entry 5dpm coloured by chain, top view.
Source organism: Escherichia coli HS
Entry authors: Zhu Y, Jiang X, Li X, Teng M

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
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: 225 amino acids
Theoretical weight: 25.02 KDa
Source organism: Escherichia coli HS
Expression system: Escherichia coli
UniProt:
  • Canonical: P17993 (Residues: 1-240; Coverage: 90%)
Gene names: JW2226, b2232, pufX, ubiG, yfaB
Sequence domains: Methyltransferase domain
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: C2
Unit cell:
a: 139.842Å b: 39.326Å c: 40.112Å
α: 90° β: 94.34° γ: 90°
R-values:
R R work R free
0.178 0.176 0.215
Expression system: Escherichia coli

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