Table 1.
Recently released structures, their active sites, and potential drug targets
| Proteins or complex | PDB id | Function | Active site/essential residues | Ref. | Some other drug targets |
|---|---|---|---|---|---|
| N | 6YI3 | RNA binding | Ala50, Thr57, His59, R89, Arg92, Ile94, Ser105, Arg107, Arg149, and Tyr172 | [14, 43] | Nsp3-N interaction site RTCs |
| Nsp9 | 6W9Q | RNA binding | Asn33, Gly100, Met101, Val102, Leu103, Gly104, and Ser105 | [91] | Helical GxxxG interaction motif β2–3- and β3–4-loops are glycine rich and integral for RNA-binding |
| Nsp15 | 6VWW | RNA binding | His235, His250, Lys290, Thr341, Tyr343, and Ser294 | [65] | Ser294 and Tyr343 govern “U” specificity RNA base recognition residues, Phe120 and Thr45 |
| Mpro | 6M03, 6LU7 | Cleaving pp1a and pp1ab | Cys145 and His41 | [83] | Residues involved in dimerization Residues A285 and L286, render enhanced catalytic property Sequence recognition site LQ▼(S, A, and G) |
| RdRp | 7BV1 (apo RdRp complex) 7BV2 (template RNA and Remdesivir bound RdRp complex) |
SARS-CoV-2 RNA synthesis | S759, D760, and D761 | [86] | Nsp7-Nsp8 heterodimer Catalytic active center (residues 759–761) |
SARS-CoV-2, severe acute respiratory syndrome coronavirus-2; RTC, replication-transcription complex; N, nucleocapsid; Mpro, main protease; Nsp, nonstructural protein.