5lqc

X-ray diffraction
1.9Å resolution

Crystal Structure of COMT in complex with N-[(E)-3-[(2R,3S,4R,5R)-3,4-dihydroxy-5-[6-(methylamino)purin-9-yl]oxolan-2-yl]prop-2-enyl]-5-(4-fluorophenyl)-2,3-dihydroxybenzamide

Released:
Source organism: Rattus norvegicus
Entry authors: Ehler A, Ellermann M, Lerner C, Rudolph MG

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Catechol O-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 221 amino acids
Theoretical weight: 24.77 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P22734 (Residues: 44-264; Coverage: 84%)
Gene name: Comt
Sequence domains: O-methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P3221
Unit cell:
a: 50.758Å b: 50.758Å c: 170.215Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.199 0.25
Expression system: Escherichia coli BL21(DE3)