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3oe4
From Proteopedia
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===Rat catechol O-methyltransferase in complex with a bisubstrate inhibitor - humanized form=== | ===Rat catechol O-methyltransferase in complex with a bisubstrate inhibitor - humanized form=== | ||
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| + | <!-- | ||
| + | The line below this paragraph, {{ABSTRACT_PUBMED_21538606}}, adds the Publication Abstract to the page | ||
| + | (as it appears on PubMed at http://www.pubmed.gov), where 21538606 is the PubMed ID number. | ||
| + | --> | ||
| + | {{ABSTRACT_PUBMED_21538606}} | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Catechol O-methyltransferase]] | [[Category: Catechol O-methyltransferase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| + | [[Category: Benz, J.]] | ||
| + | [[Category: Ehler, A.]] | ||
[[Category: Rudolph, M G.]] | [[Category: Rudolph, M G.]] | ||
| + | [[Category: Schlatter, D.]] | ||
| + | [[Category: Stihle, M.]] | ||
| + | [[Category: Alternative initiation]] | ||
| + | [[Category: Catecholamine metabolism]] | ||
| + | [[Category: Cell membrane]] | ||
| + | [[Category: Magnesium]] | ||
| + | [[Category: Membrane]] | ||
| + | [[Category: Metal-binding]] | ||
| + | [[Category: Methyltransferase]] | ||
| + | [[Category: Neurotransmitter degradation]] | ||
| + | [[Category: Phosphoprotein]] | ||
| + | [[Category: S-adenosyl-l-methionine]] | ||
| + | [[Category: Signal-anchor]] | ||
| + | [[Category: Transferase]] | ||
| + | [[Category: Transferase-transferase inhibitor complex]] | ||
| + | [[Category: Transmembrane]] | ||
Revision as of 05:12, 23 May 2012
Rat catechol O-methyltransferase in complex with a bisubstrate inhibitor - humanized form
Template:ABSTRACT PUBMED 21538606
About this Structure
3oe4 is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
- Ellermann M, Paulini R, Jakob-Roetne R, Lerner C, Borroni E, Roth D, Ehler A, Schweizer WB, Schlatter D, Rudolph MG, Diederich F. Molecular Recognition at the Active Site of Catechol-O-methyltransferase (COMT): Adenine Replacements in Bisubstrate Inhibitors. Chemistry. 2011 May 27;17(23):6369-81. doi: 10.1002/chem.201003648. Epub, 2011 Apr 27. PMID:21538606 doi:10.1002/chem.201003648
Categories: Catechol O-methyltransferase | Rattus norvegicus | Benz, J. | Ehler, A. | Rudolph, M G. | Schlatter, D. | Stihle, M. | Alternative initiation | Catecholamine metabolism | Cell membrane | Magnesium | Membrane | Metal-binding | Methyltransferase | Neurotransmitter degradation | Phosphoprotein | S-adenosyl-l-methionine | Signal-anchor | Transferase | Transferase-transferase inhibitor complex | Transmembrane
