A molecular analysis of the binding of a popular herbicide Chlorsulfuron (CS) is done on the Soybean AHAS enzyme and a mutant to explain its immunity change from susceptible to resistant. Determining the source of resistance of plants to herbicides is important in the discovery and development of herbicides, and AHAS is a common target in particular by the sulfonylureas. The X-ray structure of AHAS was first determined in Saccharomyces cervisiae (budding yeast) , followed by five molecules from this class in complex with ScAHAS [13,CE 1N0H][14, TB 1T9A,CS 1T9B,SM 1T9C,MM 1T9D]. Due to problems with crystallizing Arabidopsis Thaliana the x-ray structures of complexes with the sulfunyureas were first , MM 1YHY, CS 1YHZ, SM 1YI0, 1YI1, IQ 1Z8N] (together with one inimidazolinone IQ) and then followed by the free AtAHAS . The history of inhibiting the AHAS's function is that the herbicides were developed first, before the binding sites were discovered, and then it was found that there are 2 nearby sites: catalytic site having the function of the enzyme and an herbicide receptor site , the latter of which these small molecules bind to and are considered in this work. Developing pharmaceutical drugs traditionally has followed this pipeline and without much information about a binding site. There are now a plethora of xray structures of different AHAS's complexed with small molecules. 1 The complete cryo-em tetramer structure of AtAHAS in the presence and absence of valine was recently determined . Due to advances in molecular modeling and force fields, the developments in docking software such as what is used in this , including an important use of large scale sampling with distributions , and the advent of AlphaFold for computationally generating protein structures , it is possible to find valuable information about the immunity of plant species to herbicides solely in computation and efficiently.