TABLE 2.

Top-ranked poses of the theoretical binding free energies evaluated through the AutoDock Vina scoring function^a

Substratec	Computed ΔG (kcal/mol)b
PA	−4.8
pNPP	−4.7

^aPutative binding site residues were identified (using ChimeraX) as those interacting with the substrate molecule within 3.0 Å and were the same for both substrates, as follows: D242, D244, E245, S250, T299, A300, Y336, D354, N355, and S356. PA’s phosphate group interacts with Y336, while the phosphate group of pNPP interacts with D242.

^bΔG, binding free energy.

^cPA, phosphatidic acid; pNPP, para-nitrophenyl phosphate.