Table 3. Docking Results of Insulin Monomer with Protamine, Displaying the Type of Interactions and Bond Distances between the Residues of Insulin and Protamine.
| residues of the insulin monomer | residue of protamine | type of bonding | bond distance |
|---|---|---|---|
| Glu B21 (COO–) | Arg 10 (NH2) | hydrogen bond | 1.92 |
| Glu B13 (COO–) | Arg 30 (NH2) | electrostatic | 4.23 |
| Phe B24 (CO) | Arg 14 (NH2) | hydrogen bond | 2.13 |
| Tyr B26 (OH) | Arg 15 (NH) | hydrogen bond | 2.55 |
| Leu B17 (CO) | Arg 23 (NH2) | hydrogen bond | 2.43 |
| Ser B9 (CO) | Arg 30 (NH2) | hydrogen bond | 2.09 |
| Val B12 (CH3–CH–CH3) | Pro 18 (ring) | hydrophobic | 4.97 |
| Tyr B16 (aromatic ring) | Val 12 (CH3–CH–CH3) | hydrophobic | 5.11 |
| Tyr B26 (aromatic ring) | Arg 14 (CH2–CH2) | hydrophobic | 4.54 |
| Phe B24 (aromatic ring) | Val 12 (CH3–CH–CH3) | hydrophobic | 4.33 |