Research Article
Impact of Different Extraction Methods on Furanosesquiterpenoids Content and Antibacterial Activity of Commiphora myrrha Resin
Table 6
Molecular docking parameters for the interaction of CM-1 and CM-1 with the ATP binding domain of bacterial DNA Gyrase B.
| | Donor-acceptor pair | Distance (Å) | Nature of interaction | Docking energy (kcal m−1) | Binding affinity, Kd (m−1) |
| | Control | | LIG:H–ASP73:OD1 | 1.9066 | Conventional H-bond | −9.3 | 6.62 × 106 | | LIG:H–ASP73:OD1 | 1.9014 | Conventional H-bond | | LIG:C–GLY77:O | 3.3299 | Carbon H-bond | | LIG:C–ASN46:OD1 | 3.5462 | Carbon H-bond | | LIG:C–VAL71:O | 3.6145 | Carbon H-bond | | ASN46:CG–LIG:F | 3.6104 | Halogen bond | | THR165:CG2–LIG | 3.8251 | Hydrophobic (pi-sigma) | | ASN46:C, O; ALA47:N–LIG | 4.4879 | Hydrophobic (amide-pi) | | ASN46:C, O; ALA47:N–LIG | 4.5389 | Hydrophobic (amide-pi) | | GLY77:C, O; ILE78:N–LIG | 4.7710 | Hydrophobic (amide-pi) | | LIG–ILE78 | 5.1181 | Hydrophobic (pi-alkyl) | | LIG–ILE78 | 4.6140 | Hydrophobic (pi-alkyl) | | LIG–ILE78 | 4.3432 | Hydrophobic (pi-alkyl) |
| | CM-1 | | ARG76:NH1–LIG | 4.0868 | Electrostatic (pi-cation) | −7.5 | 3.17 × 105 | | GLU50:OE1–LIG | 4.3017 | Electrostatic (pi-anion) | | GLY77:C, O; ILE78:N–LIG | 4.4654 | Hydrophobic (amide-pi) | | ILE78–LIG | 4.0246 | Hydrophobic (alkyl) | | LIG:C–ILE78 | 4.5502 | Hydrophobic (alkyl) | | LIG:C–ILE90 | 3.8908 | Hydrophobic (alkyl) | | LIG:C–PRO79 | 4.3208 | Hydrophobic (alkyl) | | LIG–ARG76 | 5.0625 | Hydrophobic (pi-alkyl) | | LIG–PRO79 | 4.6901 | Hydrophobic (pi-alkyl) |
| | CM-2 | | ARG76:HH12–LIG:O | 2.6933 | Conventional H-bond | −7.9 | 6.23 × 105 | | ILE78–LIG | 4.1178 | Hydrophobic (alkyl) | | LIG:C–ILE90 | 4.1266 | Hydrophobic (alkyl) | | LIG:C–ILE78 | 5.0569 | Hydrophobic (alkyl) | | LIG:C–ILE78 | 5.1356 | Hydrophobic (alkyl) | | LIG:C–VAL167 | 4.6831 | Hydrophobic (alkyl) | | LIG–ILE78 | 5.0433 | Hydrophobic (pi-alkyl) |
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