Fig. 9

Polymorphism sites mapped to the 3D structure of PfLDH. Front and back views of the surface of PfLDH with mutated amino acid residues. The two views are rotated with respect to each other by 180° around the vertical axis. The 19 amino acid changes identified in global PfLDH are indicated with orange sticks. The mutation residues, which were located on the external or internal regions, were depicted in bold or underlined, respectively. The functional residues of PfLDH sre depicted as colored spheres: catalytic residues (R95, D155, R158 and H182) in red, the active site (K84) and cofactor-binding site (P235 and P239) in blue, and the substrate-specific loop (D90–N94) in green