Amino acid sequence alignments within the benzyl and quinolone pocket of <i>Bm</i>MetRS, <i>Tb</i>MetRS and <i>Lm</i>MetRS.

<p>Inhibitor binding residues in <i>Bm</i>MetRS compared to <i>Tb</i>MetRS and <i>Lm</i>MetRS are highlighted in red boxes. The most significant differences can be found in residues 211–213 (TTF) of the <i>Bm</i>MetRS which are analogous to a larger run of residues (<i>Tb</i>MetRS: KRETLH <i>Lm</i>MetRS: KRESVM) in the trypanosome structures. Inhibitor interaction with Phe213 within the <i>Bm</i>MetRS complex led to different protein geometry relative to the <i>Tb</i>MetRS complex. Table shows list of residues within the benzyl and quinolone pockets interacting with inhibitors relative to other MetRS. Sequence numbers refer to the <i>Bm</i>MetRS sequence. # LR = linker region, BP = benzyl pocket, QP = quinolone pocket.