5C6B
Crystal Structure of Prefusion-stabilized RSV F variant SC-TM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| F | 0019064 | biological_process | fusion of virus membrane with host plasma membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue NHE F 601 |
| Chain | Residue |
| F | PHE387 |
| F | PHE477 |
| F | TYR478 |
| F | ASP479 |
| F | VAL482 |
| F | ASN496 |
| F | HOH771 |
| F | HOH796 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 F 602 |
| Chain | Residue |
| F | ASN277 |
| F | ARG364 |
| F | ASN276 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 F 603 |
| Chain | Residue |
| F | LYS498 |
| F | LYS498 |
| F | LYS498 |
| F | HOH701 |
| F | HOH701 |
| F | HOH701 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 F 604 |
| Chain | Residue |
| F | SER443 |
| F | LYS445 |
| F | GLY464 |
| F | SER466 |
| F | HOH725 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 F 605 |
| Chain | Residue |
| F | LEU193 |
| F | ASP194 |
| F | LYS226 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CL F 606 |
| Chain | Residue |
| F | TRP52 |
| F | MET370 |
| F | TYR458 |
| F | HOH728 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue CL F 607 |
| Chain | Residue |
| F | ASN216 |
| F | ASN216 |
| F | ILE217 |
| F | ILE217 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Region: {"description":"Fusion peptide","evidences":[{"source":"UniProtKB","id":"P11209","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Coiled coil: {"evidences":[{"source":"PubMed","id":"10846072","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29212939","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 51 |
| Details | Coiled coil: {"evidences":[{"source":"PubMed","id":"19966279","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31268705","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10846072","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Cleavage; by host furin-like protease","evidences":[{"source":"PubMed","id":"11369882","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12127793","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"PubMed","id":"21586636","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"PubMed","id":"21586636","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28469033","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"PubMed","id":"21586636","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24179220","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
