 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 3]](dw5035fig3mag.jpg)
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Figure 3
Comparisons with the monomeric structure of the R298A mutant of Mpro. (a) Overlay of the current structure of the R298A dimer (in cyan and green) with that of the R298A monomer (grey; Shi et al., 2008  ). The orientation of domain III shows a 33° change compared with that in the monomer. The red lines represent the positions of residues 193–200 in the two structures. The region in the box is enlarged in (b). (b) Detailed interactions at the dimer interface of the R298A mutant. The red dashed lines indicate hydrogen bonds associated with the dimer, while black dashed lines indicate hydrogen bonds in the monomer. (c) Substrate-binding cavities mapped onto the current structure. Both protomers show a large and deep cavity (magenta surface representation) near the catalytic dyad, which is essentially the same as that in wild-type Mpro at pH 7.6, although wild-type Mpro at pH 6.0 shows one active protomer and one inactive protomer (Yang et al., 2003). The cavity was calculated using DS Modeling 1.7 (Accelrys) and was drawn using Discovery Studio Visualizer 2.5 (Accelrys). |
![[Figure 3]](dw5035fig3.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
