Abstract
The amino acid residue mutations observed in SARS CoV-2 RNA dependent RNA polymerase, helicase, endoRNAse and spike proteins from Indian isolates, relative to the reference SARS CoV-2 proteins from the Wuhan Hu-1 isolate, were mapped onto the protein three-dimensional structure templates available in the Protein Data Bank. The secondary structure conformations corresponding to the mutations, their locations and proximity to functionally important residues in these proteins and to the drug binding sites in RNA dependent RNA polymerase and endoRNAse targets were analysed. Our analyses provide structural insights into the mutations in these SARS CoV-2 proteins.



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