Table 1.
Preferred binding modes after docking of (R)‐1 and (S)‐1 into the active sites of wild‐type and evolved StEH1 enzymes.
| (R)‐1 | (S)‐1 | |||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Enzyme | C‐1[a] [%] | r C−1 [b] [Å] | C‐2[a] [%] | r C−2 ]b] [Å] | Mode[c] | C‐1[a] [%] | r C−1 [b] [Å] | C‐2[a] [%] | r C−2 ]b] [Å] | Mode |
| StEH1 (wt) | 5 | 3.6 | 95 | 2.7 | 3 | 7 | 3.0 | 93 | 2.8 | 3 |
| R‐C1 | 3 | 2.8 | 97 | 2.7 | 1′ | 15 | 3.0 | 85 | 2.6 | 3 |
| R‐C1B1 | 2 | 2.8 | 98 | 2.8 | 1′ | 60 | 2.6 | 40 | 3.0 | 1′ |
| R‐C1B1D33 | 2 | 3.0 | 98 | 2.7 | 3 | 62 | 2.7 | 38 | 2.8 | 2 |
[a] Experimental data from ref. 3 [b] Calculated distance between D105 and C‐1/C‐2 of the epoxide ring of 1. [c] Mode 1′ involves interaction of the phenyl ring and H300; Mode 2 directs the phenyl ring of the substrate towards W/L106; in Mode 3, the phenyl substituent is sandwiched between F189 and F33 (Figure 2). Binding Modes 3 (wild type and R‐C1), 1′ (R‐C1B1), and 2 (R‐C1B1D33) provide distances between the nucleophile and the epoxide carbons in line with experimentally determined product configurations. For calculations see the Supporting Information (all docking poses in Table S2).