1OK0
Crystal Structure of Tendamistat
Summary for 1OK0
| Entry DOI | 10.2210/pdb1ok0/pdb |
| Related | 1BVN 1HOE 2AIT 3AIT 4AIT |
| Descriptor | ALPHA-AMYLASE INHIBITOR HOE-467A, GLYCEROL, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | inhibitor, alpha amylase inhibitor |
| Biological source | STREPTOMYCES TENDAE |
| Total number of polymer chains | 1 |
| Total formula weight | 8187.38 |
| Authors | Koenig, V.,Vertesy, L.,Schneider, T.R. (deposition date: 2003-07-16, release date: 2004-01-15, Last modification date: 2024-10-09) |
| Primary citation | Koenig, V.,Vertesy, L.,Schneider, T.R. Crystal Structure of the Alpha-Amylase Inhibitor Tendamistat at 0.93 A Acta Crystallogr.,Sect.D, 59:1737-, 2003 Cited by PubMed Abstract: 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. PubMed: 14501112DOI: 10.1107/S0907444903015828 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.93 Å) |
Structure validation
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