7nbj

Co-crystal structure of Human Nicotinamide N-methyltransferase (NNMT) with the bisubstrate-like inhibitor (1)

spinqualitylabelsall models 7nbj, resolution 2.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7nbj is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.275Å Ligands: GOL, U7H Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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