Biochemical and Structural Characterization of Mycobacterial Aspartyl-tRNA Synthetase AspS, a Promising TB Drug Target
Figure 9
Induced Fit docked pose of compound 1 at the M. smegmatis AspS crystal structure.
Only amino acids forming direct interactions with compound 1 are shown. Carbon atoms of AspS are colored light green except for carbons of resistance conferring mutant site residues, which are colored purple. Carbons of compound 1 are shown in orange; all other atoms are colored by atom type (Oxygen red, Nitrogen blue, Sulphur yellow, Chlorine dark green, Hydrogen white). Labels of residues participating in polar interactions are colored brown, labels of all other residues are in black. Polar interactions are indicated with dashed lines and are numbered. Distances between heavy atoms of the atoms groups participating in polar interactions are as follows: 1. 3.1 Å; 2. 3.8 Å; 3. 3.0 Å; 4. 3.2 Å; 5. 3.1 Å; 6. 3.7 Å.