EC Number   |
Metals/Ions |
Reference |
|---|
   3.4.21.98 | Zinc |
His149 may be an integral part of zinc coordination, may have a structural rather than a catalytic role, effects on protein folding or post-folding stability |
81432, 81433 |
| 3.4.21.98 | Zn2+ |
both auto-cleavage and NS3 protease activity are zinc-dependent. NS2/3 auto-cleavage activity is more sensitive to zinc chelation by 1,10-phenanthroline than the NS3 protease activity |
681415 |
| 3.4.21.98 | Zn2+ |
in the absence of Zn+2, the NS3 protease adopts a partially-folded inactive conformation |
732738 |
| 3.4.21.98 | Zn2+ |
plays a critical role in maintaining structural stability and integrity of the protein |
691969 |
| 3.4.21.98 | Zn2+ |
zinc-dependent serine protease. zinc ion is not involved in the catalytic mechanism but it is essential for the structural integrity of the protein. The global unfolding heat capacity is dominated by the zinc dissociation step, suggesting that the binding of zinc induces a significant structural rearrangement of the protein. Contrary to other homologous zinc-dependent proteases, the zinc-free NS3 protease is not completely unstructured |
717388 |
