The point mutation effect of amino acid P197 to S197 and interaction with CS is investigated here in (Soybean and At) AHAS. This analysis uses x-ray structures as a check on related AlphaFold AHAS structures, but can be regarded as completely computational. The protein-ligand interactions are modeled computationally using CCDC GOLD and the protein structures are generated using AlphaFold2 . AlphaFold structures have been the subject of many tests of reliability and the calculations highly pass ; there is a confidence level given to regions of a generated structure and typically only flexible regions such as a tail or in the orientation of a multi-domain protein have an (expected) problem. AlphaFold uses a neural network trained on decades of x-ray and nmr data, such as from the NESG, and does calculate with this experimental input and homolog structural information from experimental structures. In principle any enzyme and small molecule herbicide can be examined using the methodology in this work, including mutants of enzymes pre-lab work. The computational analysis is very cost and time saving in practicality in narrowing down potential directions of planned field or lab studies of altered plants or the use of herbicides. Of course, there is no substitute to using experimentally determined structures (x-ray, nmr, cryo-em) and the approach in this work is a modeled approximation, however accurate in protein-ligand modeling and AlphaFold structure determination.