9PFR
Cryo-EM structure of the respiratory syncytial virus polymerase (L:P) in NTP-bound elongation state
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 184 |
| Details | Domain: {"description":"RdRp catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU00539","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 188 |
| Details | Domain: {"description":"Mononegavirus-type SAM-dependent 2'-O-MTase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00923","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile; for GDP polyribonucleotidyltransferase activity","evidences":[{"source":"UniProtKB","id":"P03523","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Active site: {"description":"For mRNA (guanine-N(7)-)-methyltransferase and mRNA (nucleoside-2'-O-)-methyltransferase","evidences":[{"source":"UniProtKB","id":"Q6WB93","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31495574","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31953395","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q6WB93","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
