Results of docking studiesa.
| Sample | Binding energy (kcal mol−1) | Binding residues/bond lengths (Å) | ||||
|---|---|---|---|---|---|---|
| α-Glucosidase | α-Amylase | Urease | α-Glucosidase | α-Amylase | Urease | |
| 6a | −3.6 | −6.1 | −5.2 | Arg-609 = 3.5 | Ser-4 = 2.9, Thr-6 = 3.0 | Arg-145 = 3.1 |
| 1 interaction | 2 interactions | 1 interaction | ||||
| 6b | - | - | −6.1 | - | - | Arg-141 = 3.1 and 3.0 |
| 2 interactions | ||||||
| 6c | −0.7 | −5.6 | Thr-384 = 2.5 | - | Asn-16 = 3.5 | |
| 1 interaction | 1 interaction | |||||
| 6d | −1.1 | −5.6 | - | Arg-420 = 2.8 | Tyr-143 = 3.0 | |
| 1 interaction | 1 interaction | |||||
| 6e | −1.5 | - | −6.1 | Arg-587 = 3.1 | - | Asn-16 = 5.1, Arg-142 = 3.3 |
| 1 interaction | 2 interactions | |||||
“-” in table refers to compounds that are inactive for respective enzyme inhibition.