Fig. 2: Structural analysis of NUDT15 interaction with acyclovir monophosphate (ACV-MP).
From: NUDT15 polymorphism influences the metabolism and therapeutic effects of acyclovir and ganciclovir
a Ligplot+ representation of the binding of ACV-MP with wild-type NUDT15 protein. ACV-MP is shown in magenta and the ACV-MP interacting residues are shown in salmon red. Hydrophobic interactions are shown as arcs with spokes and hydrogen bonds are shown as dashed lines (Laskowski R et al., 201171). b Three-dimensional view of the ACV-MP interactions with NUDT15. ACV-MP is shown in magenta and the interacting protein residues are shown in salmon red. Magnesium ions are shown in gray and the chloride ion in green. 2Fo−Fc electron density map around ACV-MP is shown as a blue mesh. c Comparison of the ACV-MP structure with the thioguanosine monophosphate (TGMP) bound structure (PDB ID 5LPG). The aligned TGMP bound NUDT15 structure is shown in transparent gray. Residues, which undergo a significant conformational change between the two structures, are highlighted.
