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Table 2 Effect of the novel mutations in protein stability, function, and structure

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.