4P58
Crystal structure of mouse comt bound to an inhibitor
Summary for 4P58
| Entry DOI | 10.2210/pdb4p58/pdb |
| Descriptor | Catechol O-methyltransferase, 1',3'-dimethyl-1H,1'H-3,4'-bipyrazole (3 entities in total) |
| Functional Keywords | sam binding site, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| Biological source | Mus musculus (Mouse) |
| Cellular location | Isoform Soluble: Cytoplasm. Isoform Membrane-bound: Cell membrane; Single-pass type II membrane protein; Extracellular side: O88587 |
| Total number of polymer chains | 1 |
| Total formula weight | 23996.55 |
| Authors | Lanier, M. (deposition date: 2014-03-15, release date: 2014-06-25, Last modification date: 2023-09-27) |
| Primary citation | Lanier, M.,Ambrus, G.,Cole, D.C.,Davenport, R.,Ellery, J.,Fosbeary, R.,Jennings, A.J.,Kadotani, A.,Kamada, Y.,Kamran, R.,Matsumoto, S.,Mizukami, A.,Okubo, S.,Okada, K.,Saikatendu, K.,Walsh, L.,Wu, H.,Hixon, M.S. A fragment-based approach to identifying S-adenosyl-l-methionine -competitive inhibitors of catechol O-methyl transferase (COMT). J.Med.Chem., 57:5459-5463, 2014 Cited by PubMed Abstract: Catechol O-methyl transferase belongs to the diverse family of S-adenosyl-l-methionine transferases. It is a target involved in the treatment of Parkinson's disease. Here we present a fragment-based screening approach to discover noncatechol derived COMT inhibitors which bind at the SAM binding pocket. We describe the identification and characterization of a series of highly ligand efficient SAM competitive bisaryl fragments (LE = 0.33-0.58). We also present the first SAM-competitive small-molecule COMT co-complex crystal structure. PubMed: 24847974DOI: 10.1021/jm500475k PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.06 Å) |
Structure validation
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