Fig. 2

a The apo structure of PfTyrRS (Class I). The catalytic domain (residues 22–260) is shown as cyan (cartoon) while the anticodon binding domain (residues 261–370) is shown in grey. The highly conserved KMSKS motif (red) and the HIGH motif (yellow) are shown in the structure. ATP and tyrosine binding sites are shown as blue dotted ellipses. Asp61, His70, Ala72, Gln73, Gln210, His235, Met237, Leu238, Met248, Lys250 are involved in ATP binding while residues Tyr60, Glu64, Ala96, Phe99, Ile172, Tyr188, Gln192 and Asp195 are involved in tyrosine binding [26]. b Apo structure of PfLysRS (Class II). The anticodon binding domain (residues 77–226) is shown in grey cartoon while the catalytic domain (residues 227–583) is shown in cyan. Motif I (red), motif II (yellow) and motif III (magenta) are shown by arrows. The ATP binding site and lysine binding site are shown by the blue dotted ellipses. Residues Arg330, His338, Asn339, Phe342, Glu500, Asn503, Gly556 and Arg559 are implicated in binding of ATP while residues Glu308, Asn330, Glu346, Tyr348, Asn503, Tyr505, and Glu507 are involved in binding of lysine [59]