Table 3:
Geometric parameters of the enzyme-inhibitor complexes predicted by molecular dockinga
| Compound | IC50 (µM) | d1 (Å) | α (degree) | d3 (Å) | d2 (Å) | L (Å)b |
|---|---|---|---|---|---|---|
| Xc | 0.015 | 2.601 | 117.0 | 3.302 | 3.218, 4.390 | 6.520 |
| 2d | 3.5 | 3.562 | 41.1 | 2.600 | 2.477, 3.562 | 5.077 |
| 2e | 10.8 | 3.342 | 117.23 | 3.535 | 5.355, 6.141 | 8.890 |
| 14c | 0.05 | 3.084 | 67.33 | 2.466 | 3.964, 5.421 | 6.430 |
| 14g | 0.015 | 4.364 | 117.9 | 3.007 | 4.143, 2.945 | 5.952 |
a
The geometric parameters important for formation of a Michaelis complex in the HNE active site are as reported previously [Crocetti et al., 2011], based on the model of synchronous proton transfer from the oxyanion hole in HNE [Groutas et al., 1997]. According to the docking results, a Michaelis complex with Ser195 is formed with participation of the ester carbonyl group.
b
Length of the channel for proton transfer calculated as d3 + min(d2).