Table 4.
Hydrophobic interaction between hGS and ligand (aridanin).
| S/N | Amino acid residue with position | Distance between interacting C-atom (Ǻ) | ID of ligand carbon atom | ID of protein carbon atom |
|---|---|---|---|---|
| 1 | TRP 130 | 3.34 | 3548 | 1298 |
| 2 | GLU 134 | 3.85 | 3536 | 1341 |
| 3 | ALA 191 | 3.69 | 3535 | 1862 |
| 4 | ASN 194 | 3.97 | 3529 | 1882 |
| 5 | GLN 205 | 3.52 | 3535 | 1989 |
| 6 | GLN 205 | 3.36 | 3536 | 1990 |
| 7 | PRO 208 | 3.15 | 3540 | 2016 |
| 8 | PRO 208 | 3.18 | 3548 | 2015 |
| 9 | ASN 255 | 3.33 | 3534 | 2448 |
| 10 | TYR 336 | 3.23 | 3534 | 3223 |
The hydrophobic interaction between the amino acids of protein and ligand with the geometry of interaction (distance of interacting atoms). Hydrophobic interaction stabilizes the protein-ligand (hGS-aridanin) complex. C-atom: carbon atom.