6nna

Human Fatty Acid Synthase Psi/KR Tri-Domain with NADPH and Compound 22

spinqualitylabelsall models 6nna, resolution 2.26Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6nna is a 2 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 2.26Å Ligands: CAF, EDO, KUA, NDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FAS_HUMAN Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein. Publication Abstract from PubMed The discovery, structure-activity relationships, and optimization of a novel class of fatty acid synthase (FASN) inhibitors is reported. High throughput screening identified a series of substituted piperazines with structural features that enable interactions with many of the potency-driving regions of the FASN KR domain binding site. Derived from this series was FT113, a compound with potent biochemical and cellular activity, which translated into excellent activity in in vivo models. Discovery and optimization of novel piperazines as potent inhibitors of fatty acid synthase (FASN).,Martin MW, Lancia DR Jr, Li H, Schiller SER, Toms AV, Wang Z, Bair KW, Castro J, Fessler S, Gotur D, Hubbs SE, Kauffman GS, Kershaw M, Luke GP, McKinnon C, Yao L, Lu W, Millan DS Bioorg Med Chem Lett. 2019 Apr 15;29(8):1001-1006. doi:, 10.1016/j.bmcl.2019.02.012. Epub 2019 Feb 11. PMID:30803804 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Fatty acid synthase 3D structures

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