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7ble
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Co-crystal structure of Human Nicotinamide N-methyltransferase (NNMT) with the tricyclic inhibitor (3)== | |
| + | <StructureSection load='7ble' size='340' side='right'caption='[[7ble]], [[Resolution|resolution]] 2.81Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7ble]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BLE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BLE FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.809Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=U1W:3-ethyl-1,3-diazatricyclo[6.3.1.0^{4,12}]dodeca-4,6,8(12)-trien-2-imine'>U1W</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7ble FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ble OCA], [https://pdbe.org/7ble PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ble RCSB], [https://www.ebi.ac.uk/pdbsum/7ble PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ble ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/NNMT_HUMAN NNMT_HUMAN] Catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is important for biotransformation of many drugs and xenobiotic compounds. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Nicotinamide-N-methyltransferase (NNMT) is a cytosolic enzyme catalyzing the transfer of a methyl group from S-adenosyl-methionine (SAM) to nicotinamide (Nam). It is expressed in many tissues including the liver, adipose tissue, and skeletal muscle. Its expression in several cancer cell lines has been widely discussed in the literature, and recent work established a link between NNMT expression and metabolic diseases. Here we describe our approach to identify potent small molecule inhibitors of NNMT featuring different binding modes as elucidated by X-ray crystallographic studies. | ||
| - | + | Novel Inhibitors of Nicotinamide-N-Methyltransferase for the Treatment of Metabolic Disorders.,Kannt A, Rajagopal S, Hallur MS, Swamy I, Kristam R, Dhakshinamoorthy S, Czech J, Zech G, Schreuder H, Ruf S Molecules. 2021 Feb 13;26(4). pii: molecules26040991. doi:, 10.3390/molecules26040991. PMID:33668468<ref>PMID:33668468</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Liesum | + | <div class="pdbe-citations 7ble" style="background-color:#fffaf0;"></div> |
| - | [[Category: Schreuder | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Liesum A]] | ||
| + | [[Category: Schreuder HA]] | ||
Current revision
Co-crystal structure of Human Nicotinamide N-methyltransferase (NNMT) with the tricyclic inhibitor (3)
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