6APD
Crystal structure of RSV F bound by AM22 and the infant antibody ADI-19425
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0019064 | biological_process | fusion of virus membrane with host plasma membrane |
| B | 0019064 | biological_process | fusion of virus membrane with host plasma membrane |
| C | 0019064 | biological_process | fusion of virus membrane with host plasma membrane |
| E | 0002250 | biological_process | adaptive immune response |
| E | 0002376 | biological_process | immune system process |
| E | 0005576 | cellular_component | extracellular region |
| E | 0005886 | cellular_component | plasma membrane |
| E | 0019814 | cellular_component | immunoglobulin complex |
| E | 0046872 | molecular_function | metal ion binding |
| G | 0002250 | biological_process | adaptive immune response |
| G | 0002376 | biological_process | immune system process |
| G | 0005576 | cellular_component | extracellular region |
| G | 0005886 | cellular_component | plasma membrane |
| G | 0019814 | cellular_component | immunoglobulin complex |
| G | 0046872 | molecular_function | metal ion binding |
| I | 0002250 | biological_process | adaptive immune response |
| I | 0002376 | biological_process | immune system process |
| I | 0005576 | cellular_component | extracellular region |
| I | 0005886 | cellular_component | plasma membrane |
| I | 0019814 | cellular_component | immunoglobulin complex |
| I | 0046872 | molecular_function | metal ion binding |
| J | 0002250 | biological_process | adaptive immune response |
| J | 0002376 | biological_process | immune system process |
| J | 0003823 | molecular_function | antigen binding |
| J | 0005576 | cellular_component | extracellular region |
| J | 0005886 | cellular_component | plasma membrane |
| J | 0016064 | biological_process | immunoglobulin mediated immune response |
| J | 0019814 | cellular_component | immunoglobulin complex |
| K | 0002250 | biological_process | adaptive immune response |
| K | 0002376 | biological_process | immune system process |
| K | 0003823 | molecular_function | antigen binding |
| K | 0005576 | cellular_component | extracellular region |
| K | 0005886 | cellular_component | plasma membrane |
| K | 0016064 | biological_process | immunoglobulin mediated immune response |
| K | 0019814 | cellular_component | immunoglobulin complex |
| N | 0002250 | biological_process | adaptive immune response |
| N | 0002376 | biological_process | immune system process |
| N | 0003823 | molecular_function | antigen binding |
| N | 0005576 | cellular_component | extracellular region |
| N | 0005886 | cellular_component | plasma membrane |
| N | 0016064 | biological_process | immunoglobulin mediated immune response |
| N | 0019814 | cellular_component | immunoglobulin complex |
Functional Information from PROSITE/UniProt
| site_id | PS00290 |
| Number of Residues | 7 |
| Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YSCQVTH |
| Chain | Residue | Details |
| L | TYR192-HIS198 | |
| J | TYR194-HIS200 | |
| E | TYR192-HIS198 | |
| D | TYR194-HIS200 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 60 |
| Details | Region: {"description":"Fusion peptide","evidences":[{"source":"UniProtKB","id":"P11209","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 60 |
| 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 | 153 |
| 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 | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"PubMed","id":"21586636","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| 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_FI6 |
| Number of Residues | 3 |
| 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 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 291 |
| Details | Domain: {"description":"Ig-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 72 |
| Details | Region: {"description":"Framework-1","evidences":[{"source":"UniProtKB","id":"P23083","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 21 |
| Details | Region: {"description":"Complementarity-determining-1","evidences":[{"source":"UniProtKB","id":"P23083","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 48 |
| Details | Region: {"description":"Framework-2","evidences":[{"source":"UniProtKB","id":"P23083","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 21 |
| Details | Region: {"description":"Complementarity-determining-2","evidences":[{"source":"UniProtKB","id":"P23083","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 111 |
| Details | Region: {"description":"Framework-3","evidences":[{"source":"UniProtKB","id":"P23083","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 3 |
| Details | Region: {"description":"Complementarity-determining-3","evidences":[{"source":"UniProtKB","id":"P23083","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 285 |
| Details | Domain: {"description":"Ig-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 279 |
| Details | Domain: {"description":"Ig-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Pyrrolidone carboxylic acid","evidences":[{"source":"PubMed","id":"826475","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






