9RBR
Semliki Forest virus trimer 2 in complex with ApoER2 LA5
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0019028 | cellular_component | viral capsid |
| D | 0055036 | cellular_component | virion membrane |
| E | 0004252 | molecular_function | serine-type endopeptidase activity |
| E | 0019028 | cellular_component | viral capsid |
| E | 0055036 | cellular_component | virion membrane |
| F | 0004252 | molecular_function | serine-type endopeptidase activity |
| F | 0019028 | cellular_component | viral capsid |
| F | 0055036 | cellular_component | virion membrane |
| G | 0004252 | molecular_function | serine-type endopeptidase activity |
| G | 0019028 | cellular_component | viral capsid |
| G | 0055036 | cellular_component | virion membrane |
| H | 0004252 | molecular_function | serine-type endopeptidase activity |
| H | 0019028 | cellular_component | viral capsid |
| H | 0055036 | cellular_component | virion membrane |
| I | 0004252 | molecular_function | serine-type endopeptidase activity |
| I | 0019028 | cellular_component | viral capsid |
| I | 0055036 | cellular_component | virion membrane |
| J | 0005198 | molecular_function | structural molecule activity |
| J | 0019028 | cellular_component | viral capsid |
| K | 0005198 | molecular_function | structural molecule activity |
| K | 0019028 | cellular_component | viral capsid |
| L | 0005198 | molecular_function | structural molecule activity |
| L | 0019028 | cellular_component | viral capsid |
| M | 0004252 | molecular_function | serine-type endopeptidase activity |
| M | 0006508 | biological_process | proteolysis |
| N | 0004252 | molecular_function | serine-type endopeptidase activity |
| N | 0006508 | biological_process | proteolysis |
| O | 0004252 | molecular_function | serine-type endopeptidase activity |
| O | 0006508 | biological_process | proteolysis |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 60 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 60 |
| Details | Region: {"description":"Transient transmembrane before p62-6K protein processing","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine; by host","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 9 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine; by host","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 444 |
| Details | Domain: {"description":"Peptidase S3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"P0DOK0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
