Table 4.
The interactions of the binding site residues of HDAC7 with the complexes
| Complex | Binding energy | Surrounding residues |
|---|---|---|
| 1 | -8.14 | PHE679, PHE737, PHE738, PRO809, LEU810, ARG547, HIS843, ASP626, HIS709, GLY842, GLY841 |
| 2 | -9.6 | PHE679, PHE737, PHE738, PRO809, LEU810, ARG547, HIS843, ASP626, HIS709, GLY842, GLY841, PRO542, GLY673, GLU543 |
| 3 | -7.89 | PHE679, PHE737, PHE738, PRO809, LEU810, GLY842, HIS843, ASP626, HIS709, GLY842, GLY841, PRO542, PRO609, ASP801 |
| 4 | -8.33 | PHE679, PHE737, PHE738, PRO809, LEU810, GLY842, HIS843, ASP626, HIS709, GLY842, GLY841, PRO542, PRO609, ASP801 |
| 5 | -8.2 | PHE679, PHE737, PHE738, PRO809, LEU810, APG547, PRO542, GLU543, GLY676, HIS709, HIS843, GLY841 |
| 6 | -7.5 | PHE679, PHE737, PHE738, PRO809, LEU810, HIS709, THR625, ASP624, ASP626, GLY678 |
| 7 | -7.52 | PHE679, PHE738, PRO809, LEU810, PRO542, GLY678, ASP624, ASP626, HIS709, HIS670, HIS669, GLY841, ASP801 |
| 8 | -8.55 | PHE679, PHE737, PHE738, PRO809, LEU810, HIS843, APG540, PRO542, HIS709, GLY841, ASN739 |
| 9 | -7.05 | PHE679, PHE737, PHE738, LEU810, HIS843, ASN736, GLY678, GLY842, PRO542, ASP801 |
| 10 | -9.5 | PHE679, PHE737, PHE738, PRO809, LEU810, HIS709, ASP626, PRO667, GLU543, PRO542, ARG547, GLY841, GLU840 |
| 11 | -8.31 | PHE679, PHE737, PHE738, PRO809, LEU810, HIS709, ASP626, GLY842, GLY841, HIS843 |
| 12 | -8.06 | PHE679, PHE737, PHE738, PRO809, LEU810, HIS843, ASP626, HIS709, GLY842, GLY678 |
| 13 | -8.94 | PHE679, PHE737, PHE738, PRO809, LEU810, HIS843, HIS709, PRO542, GLY842, GLY678 |
| 14 | -8.87 | PHE679, PHE737, PHE738, PRO809, LEU810, HIS843, HIS709, ASN736, GLY842, GLY678, PRO542, ARG540 |
The last column shows the surrounding residues of the docked complexes. Residues, which form hydrophobic and π-π stacking
interactions with the complexes are highlighted in bold and residues, which form hydrogen bonds are written in italic.