Fig. 5

SNP profiles of cytoplasmic PfKRS. a Domain diagram of Plasmodium KRS. Aminoacylation and anticodon domains are shown in pink and brown respectively; the N-terminal is shown in grey; and the disordered region in three-dimensional structures of PfKRS is shown as grey patterning. b The percentage distribution of SNPs (amino acid mutations) across the domains in PfKRS (left) and PvKRS (right). c The percentage frequency of amino acid mutations per domain in PfKRS and PvKRS [(total number of amino acid mutations divided by total number of residues in the enzyme) × 100]. d Structure of the PfKRS dimer surface (PDB ID: 4PG3). For simplicity, the aminoacylation domain of only one monomer is coloured light pink. The sequence patch 1 (amino acids 287–354), with no mutations, is colored dark pink. Substrate/inhibitor binding pocket is indicated with a blue box. e Close-up view of the primary binding pocket of PfKRS with the bound inhibitor cladosporin (magenta stick) and substrate L-Lys (blue stick). The binding residues of PfKRS are shown as pink sticks. The two SNPs which lie in the binding pocket, L555I and V501I, are shown as a green surface. Abbreviations: PvKRS, P. vivax lysyl-tRNA synthetase