Table 5.
Distances (Å) of some amino acid residues of BSA from baicalein in the docked pose and the change in accessible surface area (ΔASA) of the interacting residues of BSA (uncomplexed) and their complex with baicalein.
| Residues | Distance (Å) | ΔASA (Å2) |
|---|---|---|
| Arg 194 Nη1 | 5.0 [4-C=O] | 25.11 |
| Nη2 | 5.3 [4-C=O] | |
| Leu 197 | 14.93 | |
| Trp 213 (Nε) | 6.6 [1-O] | 23.65 |
| 7.8 [4-C=O ] | ||
| Arg 217 Nη1 | 2.7 [4-C=O] | 29.14 |
| Nη2 | 3.8 [4-C=O] | |
| Nη1 | 4.6 [5-O] | |
| Nη2 | 5.4 [5-O] | |
| Val 342 | – | 26.01 |
| Asp 450 Oδ1 | 4.8 [1-O] | 30.47 |
| Oδ2 | 5.3 [1-O] | |
| Ser 453 | – | 5.32 |