Table 3.
Docking details of BSA and phosphodiesterase-I receptors with compounds 1 and 2.
| Compound | Hydrogen bonding residues and distance | Hydrophobic interacting residues | B. affinity (kcal/mol) | ||
|---|---|---|---|---|---|
| 1 | His145 Glu424 Ser428 |
3.06 Å 2.84 Å 2.75 Å |
Leu189, Thr190, Ala193, Arg196, Lys431, Tyr451 and Arg458 | –8.8 | |
| 2 | Arg194 Ser428 Arg458 |
3.09 Å 2.34 Å 2.99 Å |
His145, Val188, Thr190, Ser191, Val425 and Ile455 | –8.5 | |
| Rutin (standard) |
–9.4 | ||||
| 1 | Tyr378 Thr455 Arg456 |
3.21 Å 2.90 Å 2.83 Å |
Lys184, His309, Leu363, GLu379, Gly380, Pro381, Trp446, Met447 and Thr461 | –8.4 | |
| 2 | Lys184, Trp446 His462 |
3.34 Å 3.01 Å 3.05 Å 3.16 Å |
His309, Leu363, Glu379 and Gly380 | –8 | |
| EDTA (standard) | –4.9 | ||||