2xfi | pdb_00002xfi

HUMAN BACE-1 IN COMPLEX WITH N-((1S,2R)-3-(((1S)-2-(CYCLOHEXYLAMINO)-1-METHYL-2-OXOETHYL)AMINO)-2-HYDROXY-1-(PHENYLMETHYL)PROPYL)-3-((METHYLSULFONYL)(PHENYL)AMINO) BENZAMIDE

spinqualitylabelsall models 2xfi, resolution 1.73Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xfi is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: XFI Related: 1xn3, 2wf3, 2wf1, 2vnm, 2wf4, 2fdp, 2vj6, 1ym4, 2wf2, 1sgz, 1ujk, 2va7, 2wjo, 2wez, 1ym2, 1py1, 1w50, 2vj7, 2wf0, 1w51, 1tqf, 1m4h, 1xn2, 2viy, 2va6, 2vie, 2viz, 2b8l, 2va5, 2b8v, 1fkn, 1xs7, 2vij, 2vj9, 2vkm, 2vnn, 1ujj, 2xfj, 2xfk Activity: Memapsin 2, with EC number 3.4.23.46 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Inhibition of the aspartyl protease BACE-1 has the potential to deliver a disease-modifying therapy for Alzheimer's disease. Herein, is described a series of potent inhibitors based on an hydroxyethylamine (HEA) transition state mimetic template. These inhibitors interact with the non prime side of the enzyme using a novel edge-to-face interaction with Arg-296. BACE-1 hydroxyethylamine inhibitors using novel edge-to-face interaction with Arg-296.,Clarke B, Cutler L, Demont E, Dingwall C, Dunsdon R, Hawkins J, Howes C, Hussain I, Maile G, Matico R, Mosley J, Naylor A, O'Brien A, Redshaw S, Rowland P, Soleil V, Smith KJ, Sweitzer S, Theobald P, Vesey D, Walter DS, Wayne G Bioorg Med Chem Lett. 2010 Aug 1;20(15):4639-44. Epub 2010 Jun 8. PMID:20579874 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta secretase

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