8X0M
Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(5-fold)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| B | 0005198 | molecular_function | structural molecule activity |
| B | 0019028 | cellular_component | viral capsid |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0019028 | cellular_component | viral capsid |
| C | 0055036 | cellular_component | virion membrane |
| E | 0004252 | molecular_function | serine-type endopeptidase activity |
| E | 0006508 | biological_process | proteolysis |
| F | 0005198 | molecular_function | structural molecule activity |
| F | 0019028 | cellular_component | viral capsid |
| G | 0004252 | molecular_function | serine-type endopeptidase activity |
| G | 0019028 | cellular_component | viral capsid |
| G | 0055036 | cellular_component | virion membrane |
| I | 0004252 | molecular_function | serine-type endopeptidase activity |
| I | 0006508 | biological_process | proteolysis |
| J | 0005198 | molecular_function | structural molecule activity |
| J | 0019028 | cellular_component | viral capsid |
| K | 0004252 | molecular_function | serine-type endopeptidase activity |
| K | 0019028 | cellular_component | viral capsid |
| K | 0055036 | cellular_component | virion membrane |
Functional Information from PROSITE/UniProt
| site_id | PS01209 |
| Number of Residues | 23 |
| Details | LDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIpvswr.CDgenDCdsgeDEEn....C |
| Chain | Residue | Details |
| D | CYS97-CYS119 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| 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_FI2 |
| Number of Residues | 15 |
| Details | Region: {"description":"Interaction with spike glycoprotein E2","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 42 |
| Details | Region: {"description":"Dimerization of the capsid protein","evidences":[{"source":"UniProtKB","id":"P0DOK1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 30 |
| Details | Motif: {"description":"Nuclear export signal","evidences":[{"source":"UniProtKB","id":"P09592","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| 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_FI6 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3553612","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Site: {"description":"Involved in dimerization of the capsid protein","evidences":[{"source":"UniProtKB","id":"Q86925","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 44 |
| Details | Region: {"description":"(Microbial infection) Interaction with Semliki virus spike glycoprotein E1","evidences":[{"source":"PubMed","id":"37098345","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
