1RER
Crystal structure of the homotrimer of fusion glycoprotein E1 from Semliki Forest Virus.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004252 | molecular_function | serine-type endopeptidase activity |
A | 0019028 | cellular_component | viral capsid |
A | 0055036 | cellular_component | virion membrane |
B | 0004252 | molecular_function | serine-type endopeptidase activity |
B | 0019028 | cellular_component | viral capsid |
B | 0055036 | cellular_component | virion membrane |
C | 0004252 | molecular_function | serine-type endopeptidase activity |
C | 0019028 | cellular_component | viral capsid |
C | 0055036 | cellular_component | virion membrane |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 51 |
Details | Region: {"description":"E1 fusion peptide loop","evidences":[{"source":"UniProtKB","id":"Q8JUX5","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 240 |
Details | Region: {"description":"E1-DIII; interaction with host receptor VLDLR","evidences":[{"source":"PubMed","id":"16407067","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37098345","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Site: {"description":"Interaction with host receptor VLDLR","evidences":[{"source":"PubMed","id":"37098345","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39095394","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | Site: {"description":"Interaction with host receptor VLDLR","evidences":[{"source":"PubMed","id":"37098345","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | Site: {"description":"Interaction with host receptor VLDLR","evidences":[{"source":"PubMed","id":"39095394","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":"14737160","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6985476","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"UniProtKB","id":"Q5Y388","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |