Mapping Mutations in Proteins of SARS CoV-2 Indian Isolates on to the Three-Dimensional Structures

22 July 2020, Version 1
This content is a preprint and has not undergone peer review at the time of posting.


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.


SARS CoV-2 Indian isolate proteins
Amino acid mutations
RNA-dependent RNA polymerase
Spike glycoprotein
Secondary structure conformation
drug-binding sites

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