Sandbox Reserved 1755

Text To Be DisplayedText 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

(hOAT')

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 == catalyzes the metabolic conversion of ornithine into an intermediate for proline or glutamate synthesis. Catalyzes the second step of the urea cycle, the condensation of carbamoyl phosphate with L-ornithine to form L-citrulline. Important amino acids Amino Acids 300-304 are an important part of protein binding . Structural highlights An image of the helix in HOAT protein. The protein hOAT has three pyrodixal-5'phosphate ligands (PLP).93/933999/Ligands_of_interest/1 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. An image of the alpha carbon.