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.

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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. 50% transparency 60% Figure 1. The coolest image of this protein EVAH!! Mechanism Figure #. Active site mechanism Development and Evolution DA_20_10 Q162R Residue 162 resides near the top of the binding entrance to the enzyme, and is within 3A in most models on the enzyme. It can act as a hydrogen bond donor to the terminal phosphate on the ligand when in proximity. To increase this interaction, the group chose a Q to R mutation, which decreased the length of the potential hydrogen bond to within 2.5A, increasing the strength of the interaction. A285N Residue 285, as follows, is also buried within the binding pocket. The group introduced this mutation to increase steric hindrance with the catalytic tyrosine, reducing the number of rotamers the residue has to increase the reactivity of the enzyme by lowering the distance between Y134 and the ligand. 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