Sandbox Reserved 1757

Text To Be Displayed

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

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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 Mevalonate 3,5-bisphosphate decarboxylase is a protein that originates from members of the order Thermoplasmatales, however in this article specifically the Mevalonate 3,5-bisphosphate being studied originated from the species Picrophilus Torridus. The purpose of this protein is to catalyze an elimination reaction in order to remove the 3-phosphate group from mevalonate 3,5-biphosphate and further goes on to decarboxylate the substrate produced thereby removing carboxyl groups from the acidic substrate. Important amino acids The article only really talks about how the ligand, like a fatty acid, lacks an ATP binding site. It also talks about the necessity of the ligand being amphipathic as there are hydrophilic and hydrophobic charges found in the binding site. Structural highlights The protein is a dimer that contains 14 helices and 15 beta sheets per linked molecule. The ARG 148 forms hydrogen bonds that allow it to pair with Oleic Acid, the protein’s ligand. Protein also requires H2O to be present in order to bind its ligand. I found it really interesting that the protein only actually attaches to the ligand via small interaction between ARG 148 and water molecules. 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.