1.6.3.5 | 3D molecular models for mutants m5Ren1 and m6Ren1. Regions on the surface of the enzyme that are significantly changed include Q3R, C47R, R75S, S217D, and T329Q. Each of these mutations contributes to changes in polarity, charge, and hydrophilicity. Relative to wild-type, m6Ren1 exhibits a greater density of positively-charged residues around the active site |