Analysis of the molecular docking model predicts that MPA binds in the cleft created by the closure of the N-terminal and Cterminal domains. The space-filling model suggests that the molecular structure of MPA is sterically complementary to the cleft between the domains (Fig. 4B) . The molecular docking model provides instructive findings on the interaction between specific residues of the enzyme and MPA (Fig. 4B ). Arg106 and Asp213 of the N-terminal NT domain and Lys234, Asp244, Gln293, Arg295, Asp297, and Glu281 of the C-terminal OB fold domain would be involved in the coordination of the MPA through hydrogenbonding (Fig. 4C) . Ile86 (N-terminal) is predicted to make a hydrophobic interaction with MPA, which is located 4.0 Å away from the bound GMP (Fig. 4D) .