The inhibition process investigated in this work is that of obstructing molecular transport of molecules such as pyruvate, 2ketobutyrate, or acetolactate/other components of V,L,I into or out of the site of catalytic activity. Proline 197 is the point of mutation and a fixed monomer AHAS backbone structure (with flexible amino acid side-chains) is used in the binding modeling. Rather than add in the completion of the dimer, only one monomer unit of the dimer is used to quantify the binding near P197 and in its change to S197. The entry point and region in the 6U9H tunnel is large enough to use only one monomer unit of the dimer, that containing P197, without sacrificing too much in the interaction with the opposite monomer. If investigating the mutation of W574 then the other monomer could be used and the binding examining near W574 and its mutant. In a more complete approximation of altering an amino acid in the herbicide site both monomers of the dimer would be used. In this case AlphaFold would be required to get the dimer orientation and interface correct, and this introduces a possible error in the modeling; AF is very robustly accurate with x-ray and nmr structures with monomers.