The alteration of one amino acid with a target binding site location to a small molecule does change the binding site, but how much and to what effect can only be understood by examining the protein's interaction with the small molecule. Computational molecular modeling tools such as the CCDC GOLD protein-ligand docking software is used to study these interactions. Fortunately, and only available in the recent 2 years, is the availability of the AlphaFold protein structure modeling software; this computational tool relies on decades of x-ray and NMR data to train a neural network in successfully reproducing and predicting protein structures. While both of these tools are computational, they have passed successfully large numbers of tests in reliability, and in the case of AlphaFold, its structures have proven to be as confidently accurate as typical NMR structures. It is time consuming and costly to create x-ray structures of any plant's enzyme, let alone mutating it and growing it to test. Both AlphaFold and molecular interaction analysis can provide a reasonable and much more efficient understanding of the effects of mutated enzymes.