4pyo

X-ray diffraction
2.1Å resolution

Humanized rat COMT bound to SAH, semi-holo form

Released:
Source organism: Rattus norvegicus
Primary publication:
Mapping the conformational space accessible to catechol-O-methyltransferase.
OpenAccess logo Acta Crystallogr. D Biol. Crystallogr. 70 2163-74 (2014)
PMID: 25084335

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Catechol O-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 221 amino acids
Theoretical weight: 24.69 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P22734 (Residues: 44-264; Coverage: 84%)
Gene name: Comt
Sequence domains: O-methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 58.369Å b: 60.38Å c: 148.415Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.189 0.233
Expression system: Escherichia coli