Table 3. Equivalent poses of compound (I) in the active hfXa site, as a result of molecular coupling calculations (kcal mol−1).
| Compound | Bond energya | No. of hydrogen bondsb | Hydrogen-bonding interaction residuesb | van der Waals interaction residuesb |
|---|---|---|---|---|
| (I) (pose 1) | −7.7 | 1 | Gly218 | Trp215, Cys191, Ser195, Gln192, Cys220, Gly218, Ala190, Gly216, Gly 226, Asp189, Val213, Phe174, Glu217, Glu 146 |
| (I) (pose 2) | −7.6 | 1 | Gly192 | Phe174, Tyr99, Val213, Gly226, Trp215, Ser195, Asp189, Ala190, Gly218, Gly216, Cys191, Gln192, Ile 227, Lys96 |
| (I) (pose 3) | −7.4 | 2 | Gly 216, Gln192 | Cys220, Glu217, Phe174, Val213, Gly226, Cys191, Ser195, Ala190, Trp215, Gly218, Ile227 |
Notes: (a) The binding energy indicates the affinity and binding capacity for the active site of the enzyme protein fXa; (b) The number of hydrogen bonds and all amino acid residues involved in the enzyme-inhibitor complex were determined using AutoDock 4.2.6 (Trott & Olson, 2010 ▸); (c) The Apixaban molecule was used as a positive control ligand for the active site.