Docking score and important interaction shown by ligands and metal complex.
| Ligands/complex | Binding affinity (kcal mol−1) | H-Bonds (Å) | Π-Interactions (stacking, anion and alkyl) | Hydrophobic/van der Waals |
|---|---|---|---|---|
| L1 | −7.5 | 4. Asp202, Gly228, Glu271, Arg400 | 2. Tyr65, Asp33 (Π–anion) | 8. Asp62, Ile146, Phe166, Arg200, Thr203, Phe206, Gly228, Tyr235, His332 |
| L2 | −7.2 | 3. Asp202, Glu271, His332, Arg400 | 1. Tyr65 | 5. Asp33, Thr203, Phe206, Gly288, Tyr235 |
| L3 | −6.9 | 3. Asp62, His105, His332 | — | Asp62, Tyr65, Ile146, Phe166, Arg200, Thr203, Phe206, Gly228, Tyr235, His332 |
| L4 | −7.5 | 4. Tyr65, Arg200, His332, Arg400 | Asp333 (Π–anion) | Phe166, Arg200, Thr203, Phe206, Gly228, Tyr235 |
| L5 | −7.1 | 4. Asp62, Gln170, His105, His332 | — | Ile146, Phe166, Arg200, Thr203, Phe206, Gly228, Tyr235 |
| L6 | −7.0 | 2. 2× Gly228 | — | Ile146, Phe166, Arg200, Thr203, Phe206 |
| L7 | −6.0 | 2. Glu271, Arg400 | — | Phe206, Gly228, Tyr235, His332 |
| L8 | −5.8 | — | — | Ile146, Phe166, Arg200, Thr203, Phe206 |
| 1 | — | |||
| 2 | — | |||
| 3 | 1.56 | — | Tyr65, Phe147, Phe166, Pro230 | |
| 4 | −6.04 | 1. lle272 | lle146, Phe147, Phe166, Pro230, Tyr389 (Π–alkyl) | Phe166, Arg200, Thr203, Phe206 |
| 5 | −0.71 | — | Lle146, Ala229, Val334 (Π–alkyl) | Phe166, Arg200, Thr203 |
| 6 | −1.70 | 1. Gly228 | Ala229, Tyr235 (Π–anion) | Arg200, Thr203, Phe206 |
| 7 | — | |||
| 8 | — | |||
| 9 | 13.59 | Tyr65, Arg200, Thr226, Asp274 | Gly228, Asp333, Phe297, Tyr389 | lle146, Phe147, Phe166, Pro230, Tyr389 |
| 10 | −5.64 | — | lle146, Phe147, Phe166, Pro230, Tyr389 (Π–alkyl) | |
| 11 | −0.61 | 2. Gln170, Asp274 | Tyr65 | |
| 12 | −1.60 | — | Phe147, Phe166, Pro230, Tyr389 (Π–alkyl) | |
| PAAa | −6.70 | 6. Arg200, Asp202, Gly273, His332, Asp333, Arg400 | — | Asp62, His105, Phe166, Thr226, Gly228 |
a
PAA = polyacrylic acid natural ligand of α-glucosidase enzyme.