Literature summary for 3.4.22.69 extracted from

Zhou, J.; Fang, L.; Yang, Z.; Xu, S.; Lv, M.; Sun, Z.; Chen, J.; Wang, D.; Gao, J.; Xiao, S.
Identification of novel proteolytically inactive mutations in coronavirus 3C-like protease using a combined approach (2019), FASEB J., 33, 14575-14587 .

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Protein Variants

Protein Variants	Comment	Organism
F139A	loss in protease activity. Significant disruption of the intermolecular hydrogen bonding network and intermolecular dynamic correlations for the active sites, thus affecting the intermolecular hydrogen bond network and the substrate binding affinity	porcine epidemic diarrhea virus
G142A	loss in protease activity. Significant disruption of the intermolecular hydrogen bonding network and intermolecular dynamic correlations for the active sites, thus affecting the intermolecular hydrogen bond network and the substrate binding affinity	porcine epidemic diarrhea virus
H162A	loss in protease activity. Significant disruption of the intermolecular hydrogen bonding network and intermolecular dynamic correlations for the active sites, thus affecting the intermolecular hydrogen bond network and the substrate binding affinity	porcine epidemic diarrhea virus
W31A	loss in protease activity. Mutation might cause subtle but significant rearrangements in the structure resulting in altered interactions with the bound substrate, as well as impacting the dynamic assemblies of the complexes	porcine epidemic diarrhea virus

Organism

Organism	UniProt	Comment	Textmining
porcine epidemic diarrhea virus	-	-	-

Synonyms

Synonyms	Comment	Organism
3cLpro	-	porcine epidemic diarrhea virus

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Release 2023.1 (January 2023)