Mutation detail:
| Mutation site | N28A |
| Virus | SARS-CoV |
Mutation level  |
Amino acid level |
| Gene/protein/region type | ORF1ab(3C-like protease) |
| Gene ID | 1489680 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | AAP41036.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
decrease |
| Pathogenicity mechanism | A away from the closest residue in the opposing monomer, is essential for the enzymatic activity and dimerization of SARS 3CLpro. Mutation of this residue to alanine almost completely inactivates the enzyme and results in a 19.2-fold decrease in the dimer |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | ORF1ab polyprotein |
| Uniprot protein ID | P0C6X7 |
| Protein length | 7073 amino acids |
| Protein description | The Orf1ab polyprotein contains the Orf1a polyprotein and 16 non-structural proteins. The Orf1ab polyprotein and its cleavage products carry out a wide range of activities associated with the viral replication, including ATP binding and breaking down of ADP and phosphate, cysteine-directed endopeptidase, leading to the formation of nonstructural proteins, such as exonuclease that produces ribose- 5-phosphate, methyltransferase for the synthesis of new nucleotides, RNA polymerase for the viral replication, RNA helicase for the removal of super twisting, as well as the regulation of the transcription through binding of zinc. However, the functions of the Orf1ab are the collective functions of the non-structural proteins encoded by the gene of Orf1ab |
Literature information:
| Pubmed ID | 20420403 |
| Clinical information | No |
| Disease | - |
| Published year | 2010 |
| Journal | Biochemistry |
| Title | Mutation of Asn28 disrupts the dimerization and enzymatic activity of SARS 3CLpro |
| Author | Jennifer Barrila, Sandra B. Gabelli, Usman Bacha, L. Mario Amzel, Ernesto Freire |
| Evidence | The crystallographic structure of the N28A mutant determined at a 2.35 resolution reveals the critical role of Asn28 in maintaining the structural integrity of the active site and in orienting key residues involved in binding at the dimer interface and su |