› 1vid

X-ray diffraction
2Å resolution

CATECHOL O-METHYLTRANSFERASE

Released:
DOI: 10.2210/pdb1vid/pdb
PDB entry 1vid coloured by chain, front view.
PDB entry 1vid coloured by chain, side view.
PDB entry 1vid coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structure of catechol O-methyltransferase.
Vidgren J, Svensson LA, Liljas A
Nature 368 354-8 (1994)
PMID: 8127373

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149780 (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
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 SAM 1 x SAM
2 bound ligands:
Ligand MG 1 x MG
Ligand DNC 1 x DNC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: P3221
Unit cell:
a: 51.3Å b: 51.3Å c: 168.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.194 not available
Expression system: Escherichia coli

Quick links

Citations

27 review citations

Creatine and creatinine metabolism.
Wyss et al. (2000)
26 more

29 mentions without citation

Many paths to methyltransfer: a chronicle of convergence.
Schubert et al. (2003)
28 more