This study used molecular computational tools and methods to examine one amino acid point mutation in the Soybean AHAS enzyme. The approach is generally applicable to any other setup of mutation and protein. Although experimental x-ray structures were not used directly, known xray structures of AtAHAS were compared against. The computational aspect could allow for a faster analysis of enzymes involved in crop research and development genetically, and in the discovery and development of herbicides for combined benefit. There are a number of amino acids interacting in the herbicide site of AHAS -a potential computational study of mutating one at a time and analyzing the effect with a set of herbicides individually could elucidate an optimal choice of point mutation for individual or collective herbicidal resistance (not just CS used in this work).