From: Novel mutations in NSP-1 and PLPro of SARS-CoV-2 NIB-1 genome mount for effective therapeutics
SL no. | Change of amino acid | Protein stability (MUpro) | Protein function (PROVEAN; cutoff = − 2.5) | Protein structural properties (HOPE) |
---|---|---|---|---|
1 | V121D | Decrease | Deleterious | Change of amino acid: Neutral → Negative Change in structural stability: Slight destabilization of NSP-1 Level of conservation: Highly conserved |
2 | V843F | Decrease | Neutral | Change of amino acid size: Mutant residue size is bigger Change in structural stability: Disturbing the domain and might abolish its function Level of conservation: Highly conserved |
3 | A889V | Increase | Neutral | Change of amino acid size: Mutant residue size is bigger. Change in structural stability: Disturbing the domain and might abolish its function Level of conservation: Located near a highly conserved position, this mutation might occur without damaging the protein. |
4 | G1691C | Decrease | Deleterious | Change of amino acid size: Mutant residue size is bigger and more hydrophobic. Change in structural stability: The wild-type residue is a glycine that might be necessary to give the protein essential flexibility. Mutation of this glycine might abolish the function of the protein. Level of conservation: The mutant residue is located near a highly conserved position. The mutant and wild-type residue are not very similar. Based on this conservation information, this mutation is probably damaging to the protein. |