PMC:7571312 / 16750-17191 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7571312","sourcedb":"PMC","sourceid":"7571312","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7571312","text":"-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, 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