1ok0
From Proteopedia
CRYSTAL STRUCTURE OF TENDAMISTAT
Overview
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.
About this Structure
1OK0 is a Single protein structure of sequence from Streptomyces tendae. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 03:56:55 2008
