Figure 5
(a) Stereoview of the hydrogen-bonding interactions (within 3.2 Å) between the C-terminal residues 301–306 of MERS-CoV 3CLpro protomer D (crystal form II, C atoms in green) and the active site of protomer A (C atoms in gray). Residue Ser1 (C atoms in yellow) is from protomer B of the homodimer. (b) Stereoview of the active-site residues from protomer A of the free enzyme form (crystal form I, C atoms in magenta) superimposed onto the active site of product-bound protomer A (crystal form II, C atoms in gray). |