Table 3.
List of the complementary amino acid residues which establish interactions with the three more promising inhibitors into the Loxosceles SMase D binding site, according to the findings from molecular docking simulations (CLC Drug Discovery Workbench Software 2.4 (QIAGEN Aarhus A/S, 2014).
| Compound 1 | Compound 5 | Compound 6 |
|---|---|---|
| Asp91 (1) | Tyr169 (1) | Lys93 (1) |
| Ser132 (1) | Pro134 | Tyr169 (1) |
| Tyr169 (2) | Ser166 | Asn200 (1) |
| Ser166 (1) | Gly167 | His47 |
| Ser195 (1) | Pro168 | Pro134 |
| Val89 | Leu170 | Asp135 |
| Lys93 | Leu173 | Ser166 |
| Leu133 | Leu198 | Gly167 |
| Pro134 | Thr199 | Pro168 |
| Asp135 | Asn200 | Leu170 |
| Asp164 | Phe201 | Leu173 |
| Gly167 | Asp206 | Leu198 |
| Pro168 | Thr199 | |
| Leu170 | Phe201 | |
| Leu173 | Ser202 | |
| Pro174 | ||
| Asp196 | ||
| Gly197 | ||
| Leu198 | ||
| Thr199 | ||
| Asp206 | ||
| Asp209 | ||
| Tyr228 | ||
| Trp230 |
The complementary amino acid residues in the SMase D binding site that establish hydrogen bonding interactions are in bold letters followed by the number of H bonds established between parentheses.