 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 4]](dw5035fig4mag.jpg)
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Figure 4
Comparisons with the structure of wild-type Mpro. (a) An overlay of the current structure of the R298A dimer (cyan and green) with that of wild-type Mpro in complex with peptidyl aldehyde inhibitor (magenta; PDB entry 3snd ; Zhu et al., 2011  ). The red arrows show the orientation change affecting the two domain IIIs. The region in the box is enlarged in (b). (b) The hydrogen-bonding interaction between the two domain IIIs. The red dashed line indicates the hydrogen bond between Ser284 and Thr285′ in the R298A mutant, while the black dashed lines show hydrogen bonds between the two Thr285 residues and the associated water (red sphere) in wild-type Mpro. (c) and (d) show the detailed interactions of the two protomers near the active sites of subunit A (cyan) and subunit B (green), respectively. The red dashed lines indicate hydrogen bonds and ion pairs for the R298A mutant, while wild-type Mpro (magenta) shows the same interactions (PDB entry 3snd
; Zhu et al., 2011). Overlay of the P2–P1 residues in the two structures (orange in R298A structures and grey in wild-type Mpro, respectively) confirmed that one O atom of the carboxyl group of P1 Gln was located in the oxyanion hole. |
![[Figure 4]](dw5035fig4.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
