Sandbox Reserved 1852

This Sandbox is Reserved from March 18 through September 1, 2025 for use in the course CH462 Biochemistry II taught by R. Jeremy Johnson and Mark Macbeth at the Butler University, Indianapolis, USA. This reservation includes Sandbox Reserved 1828 through Sandbox Reserved 1846.

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

Diels-Alderase

spinqualitylabelsall models Diels-Alderase 4o5t Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Introduction Impact of Scaffold Rigidity General Structure Active Site Residues Y134 and Q208 are the important residues in the binding site. Figure 1. The coolest image of this protein EVAH!! Mechanism Figure #. Active site mechanism Development and Evolution DA_20_10 Mutated Q162 to R162 in for improved h-bonding with the diene. CE20 In this generation, it was found that the most catalytically efficient models had mutated T34, P48, and R56 to I43,L48, and S56. These mutations further tightened the binding pocket and create a more hydrophobic environment. 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.

Student Contributors

Taylor Donahue Kate Thuma Micah Zile