Table 5. Molecular Docking Interaction of 4a–l against Human Ribonucleotide Reductase Active Site.
| aentry | bdocking score | cno. H bonds | dinteracting residues of ABAD |
|---|---|---|---|
| 4a | –4.936 | arene interaction | Tyr 625 |
| 4b | –4.543 | 1 | Gln 609 |
| 4c | –5.075 | 2 | Try 625, Thr 626 |
| 4d | –4.187 | 1 | Asn 144 |
| 4e | –5.212 | 1 and 3 | Gln 615 and Gln 615, Try 625, Gln 609 |
| 4f | –5.589 | arene interaction | Try 625 |
| 4g | –5.303 | 4 | Arg 628, 2 (Thr 150), Gln 609 |
| 4h | –5.361 | 3 and arene interaction | Glu 615, Thr 621, Tyr 625 and Asn 614, Tyr 625 |
| 4i | –5.212 | ||
| 4j | –5.873 | 2 | Phe 146, Gln 609 |
| 4k | –5.352 | ||
| 4l | –5.271 |
a
The novel 3HNC inhibitors.
b
Docking scores predicted from MOE docking in binding domain of docked novel leads and ribonucleotide reductase proteins.
c
Number of hydrogen bonds formed in binding domain among ribonucleotide reductase and the novel leads.
d
The active site residues interacting among ribonucleotide reductase protein and the novel inhibitors in the ligand–receptor complex of the study.