(A) Illustration H-bonding of the docked PcyDHFR-PYR complex of 3 variants P. cynomolgi. Contact residues are shown in the sticks with grey (wild-type), cyan (human), and light green (macaque). The H bonds are represented in grey, cyan, and yellow dashed lines for wild-type, human, and macaque variants, respectively. A unique hydrogen bond forming residues of the human variant is highlighted in the blue box. (B) Display RMSD analysis of the docked complex through molecular simulations. The last 20 ns were selected for further analysis, indicated in the grey area. (C) Heatmap of the hydrogen occupancy at 81–100 ns of simulation. The amino acids with unique hydrogen occupancy are shown in the square box with their occupancy percentages.