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Fig. 8 | Malaria Journal

Fig. 8

From: Genetic diversity of Plasmodium vivax and Plasmodium falciparum lactate dehydrogenases in Myanmar isolates

Fig. 8

Polymorphism sites mapped to the 3D structure of PvLDH. Front and back views of the surface of PvLDH with mutated amino acid residues. The two views are rotated with respect to each other by 180° around the vertical axis. The 36 amino acid changes identified in global PvLDH are indicated with magenta sticks. The mutated residues, which were located on the external or internal regions, are depicted in bold or underlined, respectively. The functional residues of PvLDH are 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

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