3c3y

X-ray diffraction
1.37Å resolution

Crystal Structure of PFOMT, Phenylpropanoid and Flavonoid O-methyltransferase from M. crystallinum

Released:

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + caffeoyl-CoA = S-adenosyl-L-homocysteine + feruloyl-CoA
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
O-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 237 amino acids
Theoretical weight: 26.62 KDa
Source organism: Mesembryanthemum crystallinum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6YI95 (Residues: 1-237; Coverage: 100%)
Sequence domains: O-methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 2 x SAH
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P212121
Unit cell:
a: 48.89Å b: 71.83Å c: 128.12Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.187 0.222
Expression system: Escherichia coli