Fig. 10

Structural changes on the TgROP18 protein caused by the action of the 30C ligand in one of the two possible states. Representative structures of the ATP-TgROP18 (a) and TgROP18/30C (b) complexes after the MD simulations; the G-loop is show in yellow, the disordered region is show in green, the residuals of the catalytic triad are shown in cyan blue, the A-loop is show in red and the Chelix is show in blue. The regions in gray are schematics. c Active site of the TgROP18 model protein, delimited by adenine pocket (AP), ribose pocket (RP), and binding phosphates region (BPR). From left to right, the active site is described with the hydrophobic AP that interacts with hydrophobic substituent groups, and RP that might interact with electron donor groups, and describes the BPR with a hydrophilic profile and tends to form H-bonds with acceptor atoms. d Change over the electrostatic surface of the active site of TgROP18 caused by the 30C ligand after the MD simulation