1sui

X-ray diffraction
2.7Å resolution

Alfalfa caffeoyl coenzyme A 3-O-methyltransferase

Released:
Source organism: Medicago sativa
Primary publication:
Crystal structures of alfalfa caffeoyl coenzyme A 3-O-methyltransferase.
Plant Physiol 137 1009-17 (2005)
PMID: 15734921

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)
PDBe Complex ID:
PDB-CPX-174927 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caffeoyl-CoA O-methyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 247 amino acids
Theoretical weight: 28.04 KDa
Source organism: Medicago sativa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q40313 (Residues: 1-247; Coverage: 100%)
Gene name: CCOMT
Sequence domains: O-methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 4 x SAH
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: C2221
Unit cell:
a: 60.854Å b: 136.486Å c: 332.778Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.235 0.285
Expression system: Escherichia coli BL21(DE3)