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. 2010 Aug 28;148(3):349–358. doi: 10.1093/jb/mvq071

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© The Authors 2010. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved

This article is made available via the PMC Open Access Subset for unrestricted re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the COVID-19 pandemic or until permissions are revoked in writing. Upon expiration of these permissions, PMC is granted a perpetual license to make this article available via PMC and Europe PMC, consistent with existing copyright protections.

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Fig. 1 — Structural features of the SARS-CoV M^pro. (A) The three structural domains of SARS-CoV M^pro (pdb code: 1uk3) are shown in ribbon representation. The N-terminal domain (residues 1–183) is shown in green, C-terminal domain (residues 200–306) in blue, the loop (residues 184–199) connecting the two domains in red, the deletion region (residues 297–306) of in violet. The tryptophanyl residues Trp³¹, Trp²⁰⁷ and Trp²¹⁸ are shown in orange, yellow and pink, respectively, as bond model. Generate with Pymol. (B) Secondary structure features of the enzyme and the truncated regions of the various truncation mutants. (C) The structural flexibility of the enzyme is shown as a variable worm of the polypeptide chain based on the B factor of the pdb file (pdb code: 1uk3). The rigid structure is shown as a thinner worm in blue. The more flexible peripheral regions are shown in red. Only one of the subunits is shown. This figure was generated with SPOCK (http://quorum.tamu.edu).

Inline graphic — Structural features of the SARS-CoV M^pro. (A) The three structural domains of SARS-CoV M^pro (pdb code: 1uk3) are shown in ribbon representation. The N-terminal domain (residues 1–183) is shown in green, C-terminal domain (residues 200–306) in blue, the loop (residues 184–199) connecting the two domains in red, the deletion region (residues 297–306) of in violet. The tryptophanyl residues Trp³¹, Trp²⁰⁷ and Trp²¹⁸ are shown in orange, yellow and pink, respectively, as bond model. Generate with Pymol. (B) Secondary structure features of the enzyme and the truncated regions of the various truncation mutants. (C) The structural flexibility of the enzyme is shown as a variable worm of the polypeptide chain based on the B factor of the pdb file (pdb code: 1uk3). The rigid structure is shown as a thinner worm in blue. The more flexible peripheral regions are shown in red. Only one of the subunits is shown. This figure was generated with SPOCK (http://quorum.tamu.edu).