1ok0 | pdb_00001ok0

CRYSTAL STRUCTURE OF TENDAMISTAT

spinqualitylabelsall models 1ok0, resolution 0.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ok0 is a 1 chain structure with sequence from Streptomyces tendae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, GOL Related: 1bvn, 1hoe, 2ait, 3ait, 4ait 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 The crystal structure of the proteinaceous alpha-amylase inhibitor tendamistat has been determined at 100 K to a resolution of 0.93 A. The final R factor for all reflections with F > 4sigma(F) is 9.26%. The mean coordinate error for fully occupied protein atoms as derived from full-matrix inversion is 0.018 A. An extended network of multiple discrete conformations has been identified on the side of tendamistat that binds to the target molecule. Most notably, residue Tyr15, which interacts with the glycine-rich loop characteristic of mammalian amylases, and a cluster of amino-acid side chains surrounding it are found in two well defined conformations. The flexibility observed in this crystal structure together with information about residues fixed by lattice contacts in the crystal but found to be mobile in a previous NMR study supports a model in which most of the residues involved in binding are not fixed in the free form of the inhibitor, suggesting an induced-fit type of binding. Structure of the alpha-amylase inhibitor tendamistat at 0.93 A.,Konig V, Vertesy L, Schneider TR Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1737-43. Epub 2003, Sep 19. PMID:14501112 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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