File:Diels-AlderaseSurfaces.png
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Shown is the binding pocket of the enzyme shown as surface, highlighting the electrostatics of the two catalytic residues, Tyr134 and Glu208. The ligand is color coded based on original structure: the diene is in yellow and the dienophile is in green. The reaction proceeds via attack of the C6 on the C5, shifting electron density to C2, which attacks C1.
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
|---|---|---|---|---|---|
| current | 18:52, 17 April 2025 | | 1,079 × 732 (601 KB) | Micah Zile (talk | contribs) | Shown is the binding pocket of the enzyme shown as surface, highlighting the electrostatics of the two catalytic residues, Tyr134 and Glu208. The ligand is color coded based on original structure: the diene is in yellow and the dienophile is in green. The |
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