<p>Despite the fact that the Y-X<sub>8</sub>-K motif of xoFabV has two more residues than the Y-X<sub>6</sub>-K motif of ecFabI, the conformations of the conserved tyrosine and lysine residues are similar. The distance between the conserved tyrosine (Y236) and lysine (K245) residues in the Y-X<sub>8</sub>-K motif of xoFabV (shown in green) is 10.4 Å, while the distance between Y156 and K163 in the Y-X<sub>6</sub>-K motif of ecFabI (magenta) is 4.5 Å.</p