Table 2.

The protein residues of SARS-CoV-2 Nsp13 that are involved in hydrogen bond and hydrophobic interaction with the top ten potential phytochemical inhibitors H1 to H10 in the best-docked pose

Protein–ligand complex	Docking binding energy (kcal/mol)	Number of hydrogen bonds	Hydrogen bond interaction residues	Hydrophobic interaction residues
Nsp13-H1	− 10.2	9	P284, G285, S289, S310, Q404, R443, R567	G285, G287, K288, S289, A312, A313, E375, M378, G538
Nsp13-H2	− 9	7	G287, K288, S289, S310, R443, S535	P284, K288, A312, A313, A316, E375, G538
Nsp13-H3	− 8.9	7	K288, S289, E375, Q404, R443, R567	G285, K288
Nsp13-H4	− 8.9	15	P284, G285, K288, S289, D374, E375, R443, R567	K288, A313, A316, D374, G538
Nsp13-H5	− 8.9	13	P284, G285, G287, S289, K320, Q404, R443, G538, R567	G285, K288, K320, E375, E540
Nsp13-H6	− 8.8	4	D374, Q404, R443, R567	G285, K288, A316, E375, G538
Nsp13-H7	− 8.8	7	S289, A316, Q404, R443, R567	K288, S289, G538
Nsp13-H8	− 8.6	11	G285, K288, S289, A316, Q404, R443, G538, R567	K288, A313, A316, E375
Nsp13-H9	− 8.6	17	G285, G287, S289, A316, E375, Q404, R443, G538, R567	G285, G287, K288, E375
Nsp13-H10	− 8.6	10	S264, G287, S289, D374, E375, Q404, R442	S264, G285, G287, K288, H290, E375, G400, Q404, L438, R442, G538

For each protein–ligand complex the table lists the docking binding energy in kcal/mol, number of hydrogen bonds, and the residues forming hydrogen bond and hydrophobic interactions with the ligand atoms. Note that the hydrophobic interactions listed here are between the carbon atom of the protein residue and the carbon, halogen or sulfur atom of the ligand