8IHP
Structure of Semliki Forest virus VLP in complex with the receptor VLDLR-LA3
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005198 | molecular_function | structural molecule activity |
| A | 0019028 | cellular_component | viral capsid |
| 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 | 0006508 | biological_process | proteolysis |
| D | 0005198 | molecular_function | structural molecule activity |
| D | 0019028 | cellular_component | viral capsid |
| 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 | 0006508 | biological_process | proteolysis |
| G | 0005198 | molecular_function | structural molecule activity |
| G | 0019028 | cellular_component | viral capsid |
| 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 | 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 |
| L | 0004252 | molecular_function | serine-type endopeptidase activity |
| L | 0006508 | biological_process | proteolysis |
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 |
| M | CYS127-CYS149 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027 |
| Chain | Residue | Details |
| C | HIS145 | |
| C | ASP167 | |
| F | HIS145 | |
| F | ASP167 | |
| I | HIS145 | |
| I | ASP167 | |
| L | HIS145 | |
| L | ASP167 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027, ECO:0000269|PubMed:3553612 |
| Chain | Residue | Details |
| C | SER219 | |
| F | SER219 | |
| I | SER219 | |
| L | SER219 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | SITE: Involved in dimerization of the capsid protein => ECO:0000250|UniProtKB:Q86925 |
| Chain | Residue | Details |
| C | TYR193 | |
| C | ASN226 | |
| F | TYR193 | |
| F | ASN226 | |
| I | TYR193 | |
| I | ASN226 | |
| L | TYR193 | |
| L | ASN226 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Cleavage; by autolysis => ECO:0000269|PubMed:3553612 |
| Chain | Residue | Details |
| C | TRP267 | |
| F | TRP267 | |
| I | TRP267 | |
| L | TRP267 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | LIPID: S-palmitoyl cysteine; by host => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS395 | |
| J | CYS395 | |
| J | CYS415 | |
| J | CYS416 | |
| A | CYS415 | |
| A | CYS416 | |
| D | CYS395 | |
| D | CYS415 | |
| D | CYS416 | |
| G | CYS395 | |
| G | CYS415 | |
| G | CYS416 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN200 | |
| A | ASN262 | |
| D | ASN200 | |
| D | ASN262 | |
| G | ASN200 | |
| G | ASN262 | |
| J | ASN200 | |
| J | ASN262 |
