From the docking simulations it is predicted that C0STU6 possesses several structural features that may aid in binding AFB1 in a catalytically competent orientation for oxidation when compared to P07788 (Figure ). For example, when AFB1 is docked into C0STU6 using constraints to C12, the ketones flanking C12 are predicted to form hydrogen bonds with asparagine 107 and glutamate 110. These bonds may aid in positioning the AFB1 in the correct orientation as well as ensure both electron transfers can occur. C0STU6 also has a large hydrophobic leucine that is predicted to have favorable van der Waals interactions with the hydrophobic ring portion of AFB1. For P07788, all predicted AFB1 binding modes, except when C14 was constrained, did not have distinct molecular interactions such as hydrogen bonding or extensive van der Waals interaction. When C14 was constrained to P07788, our modeling predicted a hydrogen bond with a backbone Nitrogen. Future research using site directed mutagenesis can begin to probe the active site features of these enzymes to understand how specific primary and secondary structures contribute to optimal binding for both SET reactions.