1vid: Difference between revisions
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|PDB= 1vid |SIZE=350|CAPTION= <scene name='initialview01'>1vid</scene>, resolution 2.Å | |PDB= 1vid |SIZE=350|CAPTION= <scene name='initialview01'>1vid</scene>, resolution 2.Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=DNC:3,5-DINITROCATECHOL'>DNC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Catechol_O-methyltransferase Catechol O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.6 2.1.1.6] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Catechol_O-methyltransferase Catechol O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.6 2.1.1.6] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vid OCA], [http://www.ebi.ac.uk/pdbsum/1vid PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vid RCSB]</span> | |||
}} | }} | ||
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[[Category: Svensson, L A.]] | [[Category: Svensson, L A.]] | ||
[[Category: Vidgren, J.]] | [[Category: Vidgren, J.]] | ||
[[Category: methyltransferase]] | [[Category: methyltransferase]] | ||
[[Category: neurotransmitter degradation]] | [[Category: neurotransmitter degradation]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:24:53 2008'' |
Revision as of 00:24, 31 March 2008
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, resolution 2.Å | |||||||
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Ligands: | , , | ||||||
Activity: | Catechol O-methyltransferase, with EC number 2.1.1.6 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CATECHOL O-METHYLTRANSFERASE
OverviewOverview
Catechol O-methyltransferase (COMT, EC 2.1.1.6) 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.
About this StructureAbout this Structure
1VID is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of catechol O-methyltransferase., Vidgren J, Svensson LA, Liljas A, Nature. 1994 Mar 24;368(6469):354-8. PMID:8127373
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