Sandbox Reserved 1759

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This Sandbox is Reserved from November 4, 2022 through January 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 1755 through Sandbox Reserved 1764.

To get started: Click the edit this page tab at the top. Click on Show preview and then Save the page after each step, then edit it again. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing

Mevalonate 3,5-Bisphosphate Decarboxylase Structure

spinqualitylabelsall models Caption for this structure 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 The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase. The MVA3,5-bisphosphate decarboxylase enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The basic function of MVA3,5-bisphosphate decarboxylase is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MVA 3,5-bisphosphate decarboxylase acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction. Ligand of interest, Oleic Acid (OLA) Important amino acids Ligand OLA is hydrogen bonded to Arg128. OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128. Structural highlights The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains. The first domain contains 9 alpha helix and 15 beta sheets. The second domain contains 9 alpha helix and 15 beta sheets. In the first domain, the amino acid Arg148 that hydrogen bonds to the OLA ligand is contained within a beta sheet. This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.