The crystal structure of Arabidopsis Thaliana AtAHAS has been determined in the absence of any bound inhibitors, PDB ID: 5K6Q . The structure of Soybean AHAS has not been crystallized and was instead determined by using AlphaFold2. AHAS structurally has strong similarities across species; most of its sequence across plant species is the same. The overlay of the x-ray AtAHAS and that of Soybean is overlayed in Figure . There are no noticeable differences in the secondary structure and the RMSD between the 2 is .299 A, well below the x-ray resolution of 2.9 A for 5K6Q. The global structural difference of .3 Angstroms is not significant in view of a conformation change. Furthermore, in it was pointed out that in the x-ray structures there are side-chain angular changes when bound versus unbound. This is very reasonable because side-chains, the tertiary structure, is flexible and a small molecule bound to a protein is going to disrupt it (energy minimum). Protein side-chains in GOLD were treated as flexible in this work, and the output files annotate any angular rotation from the input structure. Backbone phi, psi angles are fixed in the software GOLD, however, and these angles changing would potentially result in a conformational change. A short Amber pre-minimization of the complex did not show any change.