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![[Figure 6]](ni5019fig6mag.jpg)
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Figure 6
Displacements at the intra-protomer interface. New-inactive Mpro is in green and active Mpro is in magenta. (a) The new oxyanion loop of one protomer pushes away residues 1′–3′ of the other protomer; however, the key salt bridge between Arg4′ and Glu290, which is important for dimer stabilization, is conserved. (b) Overall superposition of active and new-inactive Mpro shows that besides those in the oxyanion loop (red ellipsoid), major differences are located in the N-finger and in the C-terminal tail, which is not visible in new-inactive Mpro. |
![[Figure 6]](ni5019fig6.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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