TABLE 2.
Location of consensus mutations.
| Mutation | Domain | Secondary structure motif | Relative position | Distance to the T1Cu Site (Å) | Distance to the T2/T3Cu cluster (Å) |
| I25V | D1 | β-sheet | Buried | 23.7 | 15.8 |
| V27A | D1 | β-sheet | Buried | 25.7 | 15.6 |
| S33G | D1 | Loop | Surface | 23.7 | 14.7 |
| D50N | D1 | β-sheet | Partially buried | 26.1 | 18.0 |
| M52L | D1 | Loop | Partially buried | 24.2 | 17.6 |
| A92S | D1 | β-sheet | Surface | 31.8 | 21.2 |
| D142E | D2 | Loop | Surface | 29.3 | 19.7 |
| T179G | D2 | Loop | Surface | 29.2 | 29.2 |
| Y208F | D2 | β-sheet | Close to Asp205 that interacts with phenols | 14.3 | 13.9 |
| L217M | D2 | β-sheet | Partially buried | 24.5 | 22.2 |
| V219I | D2 | β-sheet | Buried | 23.2 | 19.1 |
| Q230L | D2 | β-sheet | Surface | 24.7 | 23.1 |
| A240G | D2 | β-sheet | Close to T2/T3 and His-Cys-His pathway | 11.4 | 5.3 |
| D250N | D2 | Loop | Surface | 38.0 | 34.4 |
| N268G | D2 | Loop | Surface | 23.1 | 27.0 |
| T306P | D2 | Loop | Buried | 20.3 | 25.8 |
| M327L | D3 | β-sheet | Partially buried | 11.9 | 13.1 |
| Y421R | D3 | Loop | Surface | 20.1 | 13.7 |
| F454W | D3 | α-helix | Surface, at the vicinity of the binding pocket | 7.3 | 11.1 |
| M464F | D3 | β-sheet | Buried | 10.7 | 17.1 |