7NBQ
Co-crystal structure of Human Nicotinamide N-methyltransferase (NNMT) with the tricyclic inhibitor (4)
Summary for 7NBQ
| Entry DOI | 10.2210/pdb7nbq/pdb |
| Related | 7BKG 7BLE 7NJB 7NMB |
| Descriptor | Nicotinamide N-methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, 2-methyl-1,2,6,7-tetrahydro-3H,5H-pyrido[3,2,1-ij]quinazolin-3-imine, ... (4 entities in total) |
| Functional Keywords | methyl transferase, drug discovery, inhibitor complex, nicotinamide, metabolic disorders, transferase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 128206.85 |
| Authors | Schreuder, H.A.,Liesum, A. (deposition date: 2021-01-27, release date: 2021-03-17, Last modification date: 2024-01-31) |
| Primary citation | Kannt, A.,Rajagopal, S.,Hallur, M.S.,Swamy, I.,Kristam, R.,Dhakshinamoorthy, S.,Czech, J.,Zech, G.,Schreuder, H.,Ruf, S. Novel Inhibitors of Nicotinamide- N -Methyltransferase for the Treatment of Metabolic Disorders. Molecules, 26:-, 2021 Cited by PubMed Abstract: Nicotinamide--methyltransferase (NNMT) is a cytosolic enzyme catalyzing the transfer of a methyl group from -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. PubMed: 33668468DOI: 10.3390/molecules26040991 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.479 Å) |
Structure validation
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