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1vid, resolution 2.00Å ()
Ligands: , ,
Activity: Catechol O-methyltransferase, with EC number
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Publication Abstract from PubMed

Catechol O-methyltransferase (COMT, EC is important in the central nervous system because it metabolizes catecholamine neurotransmitters such as dopamine. The enzyme catalyses the transfer of the methyl group from S-adenosyl-L-methionine (AdoMet) to one hydroxyl group of catechols. COMT also inactivates catechol-type compounds such as L-DOPA. With selective inhibitors of COMT in combination with L-DOPA, a new principle has been realized in the therapy of Parkinson's disease. Here we solve the atomic structure of COMT to 2.0 A resolution, which provides new insights into the mechanism of the methyl transfer reaction. The co-enzyme-binding domain is strikingly similar to that of an AdoMet-dependent DNA methylase, indicating that all AdoMet methylases may have a common structure.

Crystal structure of catechol O-methyltransferase., Vidgren J, Svensson LA, Liljas A, Nature. 1994 Mar 24;368(6469):354-8. PMID:8127373

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1vid is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.


  • Vidgren J, Svensson LA, Liljas A. Crystal structure of catechol O-methyltransferase. Nature. 1994 Mar 24;368(6469):354-8. PMID:8127373 doi:http://dx.doi.org/10.1038/368354a0
  • Bhattacharyya R, Samanta U, Chakrabarti P. Aromatic-aromatic interactions in and around alpha-helices. Protein Eng. 2002 Feb;15(2):91-100. PMID:11917145

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