Sandbox Reserved 1851

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

Novel Diels-Alder Catalyst Identified Using de novo Design

spinqualitylabelsall models Diels-Alderase shown as cartoon with substrate analog bound Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

Introduction

Diels-Alder Reaction

General Structure

Active Site

In the active state, there are two catalytic residues that aim to stabilize the transition state of the Diels-Alder reaction. Y134 acts as a hydrogen bond donor to the oxygen on the ligand. Q208 acts as a hydrogen bond acceptor to the nitrogen on the ligand as well as a donor to the neighboring oxygen. These interactions help reduce the energetic gap between orbitals allowing the reaction to proceed, outlined in HOMO/LUMO.

Structural Details

Active Site

Figure 1. The coolest image of this protein EVAH!!!

Active Site Residues

Relevance

Improvements

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.

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Student Collaborators

Micah Zile Kate Thuma Taylor Donahue