2wc3 | pdb_00002wc3

Structure of family 1 beta-glucosidase from Thermotoga maritima in complex with 3-imino-2-oxa-(+)-8-epi-castanospermine

spinqualitylabelsall models 2wc3, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wc3 is a 4 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AM3 Related: 2wc4, 1w3j, 2j78, 2j75, 2j7g, 2jal, 2vrj, 2j7e, 2j7h, 2cbu, 1oin, 2j7c, 1oif, 2j79, 2cet, 2j7b, 1uz1, 1od0, 2ces, 2j7d, 2j7f, 2wbg, 1oim, 2j77, 2cbv Activity: Beta-glucosidase, with EC number 3.2.1.21 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 Synthesis of a panel of iso(thio)urea-type ring-modified castanospermine analogues bearing a freely mutarotating pseudoanomeric hydroxyl group results in tight-binding beta-glucosidase inhibitors with unusual binding signatures; the presence of an N-octyl substituent imparts a remarkable anomeric selectivity, promoting strong binding of the appropriate beta-anomer by the beta-glucosidase. Glycosidase inhibition by ring-modified castanospermine analogues: tackling enzyme selectivity by inhibitor tailoring.,Aguilar-Moncayo M, Gloster TM, Turkenburg JP, Garcia-Moreno MI, Ortiz Mellet C, Davies GJ, Garcia Fernandez JM Org Biomol Chem. 2009 Jul 7;7(13):2738-47. Epub 2009 May 22. PMID:19532990 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-glucosidase MEP cytidylyltransferase

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