Fig. 3 BRD1389 occupies the L-Phe site and an auxiliary site on Plasmodium cFRS. a Two dimensional representation (Ligplot) of BRD1389 binding to Pv cFRS. BRD1389 is shown as ball-and-stick representation and interaction symbols of residues engaging in hydrophobic interactions with the ligand are highlighted in red. b Close-up view of bound BRD1389 in the active site of α -subunit of Pv cFRS. Labelled residues show hydrophobic interactions with BRD1389. c Surface view of the active site and pockets within L-Phe site (purple circle), ATP site (yellow circle) and auxiliary site (black circle). Superimposed structures of L-Phe (purple, PDB “ 3L4G [https://www.rcsb.org/structure/3l4g] ” ) and phenylalanyl-adenylate (yellow, PDB “ 2IY5 [https:// www.rcsb.org/structure/2IY5] ” ) are depicted. d Close-up view of amino acid and ATP pocket of Pv cFRS (corn fl ower blue) that is superimposed on Hs cFRS-L-Phe (grey, PDB “ 3L4G [https://www.rcsb.org/structure/3l4g] ” ). e Close-up view of auxiliary site occupied by BRD1389. Auxiliary site residues are shown which are involved in protein-ligand hydrophobic