Sandbox Reserved 1802

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.

To get started: Click the edit this page tab at the top. 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

Chorismate dehydratase (MqnA)

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 specific function of my protein is catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), which is the initial step in the biosynthesis of menaquinone via the futalosine pathway. Biological relevance and broader implications Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for potential antimicrobials and herbicides. Important amino acids The three amnio acids involved in the catalytic triad. Important amino acids for binding are the following: I13, N17, C18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, Y242 Structural highlights 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.