5emy

Human Pancreatic Alpha-Amylase in complex with the mechanism based inactivator glucosyl epi-cyclophellitol

spinqualitylabelsall models 5emy, resolution 1.23Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5emy 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. Method: X-ray diffraction, Resolution 1.231Å Ligands: 5QP, CA, CL, PCA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AMYP_HUMAN Publication Abstract from PubMed As part of a search for selective, mechanism-based covalent inhibitors of human pancreatic alpha-amylase we describe the chemoenzymatic synthesis of the disaccharide analog alpha-glucosyl epi-cyclophellitol, demonstrate its stoichiometric reaction with human pancreatic alpha-amylase and evaluate the time dependence of its inhibition. X-ray crystallographic analysis of the covalent derivative so formed confirms its reaction at the active site with formation of a covalent bond to the catalytic nucleophile D197. The structure illuminates the interactions with the active site and confirms OH4' on the nonreducing end sugar as a good site for attachment of fluorescent tags in generating probes for localization and quantitation of amylase in vivo. Glucosyl epi-cyclophellitol allows mechanism-based inactivation and structural analysis of human pancreatic alpha-amylase.,Caner S, Zhang X, Jiang J, Chen HM, Nguyen NT, Overkleeft H, Brayer GD, Withers SG FEBS Lett. 2016 Apr;590(8):1143-51. doi: 10.1002/1873-3468.12143. Epub 2016 Apr, 3. PMID:27000970 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Amylase 3D structures

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