Table 2. Electrostatic interactions of promirolysin at the PS–mature enzyme interface.
The first residue/atom belongs to the PS, the second to the CD. The distances are from the native promirolysin structure (PDB entry 6r7v).
| Salt bridges (Å) | |
| Arg21 Nη2–Asp289 Oδ1 | 2.81 |
| Glu47 O∊1–Arg302 Nη2 | 2.77 |
| Glu47 O∊2–Arg302 Nη1 | 2.86 |
| Metallorganic interactions (Å) | |
| Cys23 Sγ–Zn999 | 2.22 |
| Hydrogen bonds (Å) | |
| Arg21 N⋯Tyr216 Oη | 3.11 |
| Arg21 N⋯Tyr286 O | 3.32 |
| Arg21 N∊⋯Thr287 O | 3.44 |
| Arg21 Nη1⋯Thr221 Oγ1 | 3.02 |
| Arg21 Nη2⋯Thr287 O | 2.95 |
| Thr22 Oγ1⋯Asp179 O | 2.55 |
| Thr22 Oγ1⋯Leu181 N | 2.90 |
| Thr22 O⋯Gly182 N | 3.98 |
| Gly24 N⋯Gly182 O | 3.05 |
| Gly24 O⋯Met147 Sδ | 3.24 |
| Ser25 Oγ⋯Ala184 N | 2.86 |
| Ser25 Oγ⋯Ala184 O | 2.84 |
| Glu26 O∊1⋯Tyr286 Oη | 2.73 |
| Leu27 N⋯Asp238 Oδ2 | 2.87 |
| Asn28 Nδ2⋯Asp238 O | 3.25 |
| Trp46 N∊1⋯Asp231 Oδ1 | 3.46 |
| Trp46 N∊1⋯Asp231 Oδ2 | 2.92 |