Sandbox Reserved 1804

This Sandbox is Reserved from Mar 1 through Jun 1, 2023 for use in the course CHEM 351 Biochemistry taught by Bonnie_Hall at the Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1796 through Sandbox Reserved 1811.

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Beta-Propeller Protein

spinqualitylabelsall models Beta-Propeller Protein Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Function of your protein Transport protein that hydrolyzes aliphatic and aromatic lactones and esters. Is from Rhodopseudomonas palustris which is relevant because it prefers hydrophobic substances. Biological relevance and broader implications It has an X-ray structure and the secondary structure is also called a blade. It produces toroids of between four and twelve repeats which are almost always rearranged sequentially in a single peptide chain. Has three main ligands and those are phosphate ion, calcium ion and sodium ion. Important amino acids Amino Acids 300-304 are an important part of the drug binding site . Amino Acids 290-294 are an important part of the drug binding site .