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. 2020 Jan 1;7(Pt 1):18–29. doi: 10.1107/S2052252519013848

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