Table 1.
Results of docking simulations of ruxolitinib binding to HSA.
| Site | Free energy (kcal × mol−1) | Hydrophobic interactions | Hydrogen bonds |
|---|---|---|---|
| FA9 | −8.0 | His146, Lys190, Ala191, Ala194, Arg197, Glu425, Asn429, Lys432, Val456, Leu463 | Asp108, Val455, Gln459 |
| −7.6 | Asp108, His146, Lys190, Ala191, Ala194, Arg197, Glu425, Asn429, Lys432,Val456, Gln459, Leu463, | Asp108, Ser193, Tyr452 | |
| FA1 | −7.8 | Asp108, Asn109, Pro110, Arg145, His146, Pro147, Ser193, Arg197, Glu425 | Lys190 |
| −7.6 | Asn109, Pro110, Leu112, Arg145, His146, Pro147, Ser193, Ala194, Glu425 | Asp108, Arg145 | |
| −7.3 | Asp108, Arg145, His146, Pro147, Tyr148, Lys190, Ser193, Ala194, Arg197, Glu425 | Asp108 | |
| −7.2 | Leu115, Phe134, Lys137, Tyr138, Glu141, Ile142, Tyr161, Arg186 | Tyr138, Tyr161 | |
| −7.2 | Leu115, Phe134, Lys137, Tyr138, Ile142, Tyr161, Arg186 | Phe134, Tyr161 | |
| FA6 | −7.7 | Arg209, Lys212, Ala213, Val216, Ser232, Val235, Leu327, Asp324, Ala350, Glu354 | Arg209, Asp324, Glu354 |
| FA7 | −7.1 | Leu103, Glu100, Gln104, Arg197, Gln204, Lys205. Val462 | Tyr148, Glu465 |