Fig. 1: Computer modeling and molecular docking-based structure of PpAAT1.

a Predicted key amino acid residues of PpAAT1 interacting with 4-hydroxydecanoyl–CoA during the internal esterification reaction. A total of 16 amino acid residues were identified. b Stereoview of the substrate binding pocket. Acetyl–CoA and the four alcohols (propanol, hexanol, benzyl alcohol, and decanol) were docked to the active center during the esterification reaction. c Stereoview of the active site. Alcohols were positioned between acetyl–CoA and H165 in the most reasonable binding conformation during the esterification reaction. d Orientation of the key amino acid residues catalyzing the esterification reaction between acetyl–CoA and propanol. e Orientation of the key amino acid residues catalyzing the esterification reaction between acetyl–CoA and hexanol. f Orientation of the key amino acid residues catalyzing the esterification reaction between acetyl–CoA and benzyl alcohol. g Orientation of the key amino acid residues catalyzing the esterification reaction between acetyl–CoA and decanol