PMC:7571312 / 16750-17191 JSONTXT

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    LitCovid-PD-FMA-UBERON

    -site cysteine (Cys145) sulfur forms a covalent bond to the methylene carbon (1.8 Å C–S bond length). The ketone carbonyl is positioned within the oxyanion hole and as such engaging in hydrogen bonds with backbone NH groups of Gly143 and Cys145. A detailed analysis of an extended hydrogen bond network from catalytic His41 reveals that the side-chain imidazole serves as a hydrogen bond donor to the interior of the protease. Specifically,

    LitCovid-PD-CLO

    -site cysteine (Cys145) sulfur forms a covalent bond to the methylene carbon (1.8 Å C–S bond length). The ketone carbonyl is positioned within the oxyanion hole and as such engaging in hydrogen bonds with backbone NH groups of Gly143 and Cys145. A detailed analysis of an extended hydrogen bond network from catalytic His41 reveals that the side-chain imidazole serves as a hydrogen bond donor to the interior of the protease. Specifically,

    LitCovid-PD-CHEBI

    -site cysteine (Cys145) sulfur forms a covalent bond to the methylene carbon (1.8 Å C–S bond length). The ketone carbonyl is positioned within the oxyanion hole and as such engaging in hydrogen bonds with backbone NH groups of Gly143 and Cys145. A detailed analysis of an extended hydrogen bond network from catalytic His41 reveals that the side-chain imidazole serves as a hydrogen bond donor to the interior of the protease. Specifically,

    LitCovid-sentences

    -site cysteine (Cys145) sulfur forms a covalent bond to the methylene carbon (1.8 Å C–S bond length). The ketone carbonyl is positioned within the oxyanion hole and as such engaging in hydrogen bonds with backbone NH groups of Gly143 and Cys145. A detailed analysis of an extended hydrogen bond network from catalytic His41 reveals that the side-chain imidazole serves as a hydrogen bond donor to the interior of the protease. Specifically,

    LitCovid-PubTator

    -site cysteine (Cys145) sulfur forms a covalent bond to the methylene carbon (1.8 Å C–S bond length). The ketone carbonyl is positioned within the oxyanion hole and as such engaging in hydrogen bonds with backbone NH groups of Gly143 and Cys145. A detailed analysis of an extended hydrogen bond network from catalytic His41 reveals that the side-chain imidazole serves as a hydrogen bond donor to the interior of the protease. Specifically,