Table 5. Molecular docking results of HSA-HA interaction.
Binding site | Amino acid | Forces involved | ΔG (kcal mol−1) | K b (M−1) |
Site I | Lys199 | H-bonding and Hydrophobic | −5.6 | 1.28×104 |
Arg222 | H-bonding and Hydrophobic | |||
Tyr150 | Hydrophobic | |||
Glu153 | Hydrophobic | |||
Ser192 | Hydrophobic | |||
Lys195 | Hydrophobic | |||
Gln196 | Hydrophobic | |||
Trp214 | Hydrophobic | |||
His242 | Hydrophobic | |||
Arg257 | Hydrophobic | |||
Ala291 | Hydrophobic | |||
Glu292 | Hydrophobic | |||
Site II | Leu387 | Hydrophobic | −5.9 | 2.12×104 |
Ile388 | Hydrophobic | |||
Asn391 | Hydrophobic | |||
Cys392 | Hydrophobic | |||
Leu407 | Hydrophobic | |||
Arg410 | Hydrophobic | |||
Tyr411 | Hydrophobic | |||
Leu430 | Hydrophobic | |||
Val433 | Hydrophobic | |||
Cys438 | Hydrophobic | |||
Ala449 | Hydrophobic | |||
Leu453 | Hydrophobic |