*2.13. Interaction of the Tertiary Structure of CYP6FD1 and CYP4FD2 with Sulfoxaflor*

The *CYP6FD1* domain included these amino acids ILE97, PHE105-GLY109, TYR111, and HIS122-SER126, and the absolute conserved residues of GLU444 and ARG447 were located near the entrance of the active pocket and the N-segment where heme binding occur. The totals core between *CYP6FD1* and sulfoxaflor was 5.8954 (crash of −0.7686 and polar of 0.0277). However, the domain of *CYP4FD2* was mainly composed of the LEU103, LYS106-LYS108, ALA110-LYS112, and LEU123 amino acids, and the key amino acids PHE317 and ILE459 bind with sulfoxaflor through noncovalent bonds, with a total score of 5.2800 (crash of −1.4457 and polar of 0.5769). Moreover, the absolutely conserved residues of GLU75 and ARG78 were distant from the active pockets and the heme binding region (Figure 8).

**Figure 8.** The tertiary structure of *CYP6FD1* and *CYP4FD2* and their docking structure with sulfoxaflor. (**A**) *CYP6FD1*, (**B**) *CYP4FD2*, (**C**) *CYP6FD1* domain and sulfoxaflor, (**D**) *CYP4FD2* domain and sulfoxaflor (molecular docking between sulfoxaflor and the active sites of the target P450 proteins was predicted using the Surflex-Dock program in software Syby lX-2.0 version (Tripos Inc.).
