7FFL
Cryo-EM structure of VEEV VLP-LDLRAD3-D1 complex at the 2-fold axes
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| 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 |
| F | 0004252 | molecular_function | serine-type endopeptidase activity |
| F | 0006508 | biological_process | proteolysis |
| 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 | 0019028 | cellular_component | viral capsid |
| I | 0055036 | cellular_component | virion membrane |
| J | 0005198 | molecular_function | structural molecule activity |
| J | 0019028 | cellular_component | viral capsid |
| P | 0004252 | molecular_function | serine-type endopeptidase activity |
| P | 0019028 | cellular_component | viral capsid |
| P | 0055036 | cellular_component | virion membrane |
| Q | 0005198 | molecular_function | structural molecule activity |
| Q | 0019028 | cellular_component | viral capsid |
| R | 0005198 | molecular_function | structural molecule activity |
| R | 0019028 | cellular_component | viral capsid |
| S | 0004252 | molecular_function | serine-type endopeptidase activity |
| S | 0006508 | biological_process | proteolysis |
| T | 0004252 | molecular_function | serine-type endopeptidase activity |
| T | 0019028 | cellular_component | viral capsid |
| T | 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. CIpgawq.CDglpDCfdk.SDEke...C |
| Chain | Residue | Details |
| D | CYS42-CYS64 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 60 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| F | HIS152 | |
| F | ASP174 | |
| F | SER226 | |
| S | HIS152 | |
| S | ASP174 | |
| S | SER226 | |
| J | ILE368-LEU388 | |
| Q | ILE368-LEU388 | |
| R | ILE368-LEU388 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 102 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
| Chain | Residue | Details |
| R | PHE389-ALA423 | |
| F | ASN233 | |
| S | TYR200 | |
| S | ASN233 | |
| J | PHE389-ALA423 | |
| Q | PHE389-ALA423 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | SITE: Cleavage; by host signal peptidase => ECO:0000250 |
| Chain | Residue | Details |
| R | ALA423 | |
| J | ALA423 | |
| Q | ALA423 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 9 |
| Details | LIPID: S-palmitoyl cysteine; by host => ECO:0000250 |
| Chain | Residue | Details |
| Q | CYS396 | |
| Q | CYS416 | |
| Q | CYS417 | |
| R | CYS396 | |
| R | CYS416 | |
| R | CYS417 | |
| J | CYS396 | |
| J | CYS416 | |
| J | CYS417 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255 |
| Chain | Residue | Details |
| J | ASN318 | |
| Q | ASN212 | |
| Q | ASN318 | |
| R | ASN212 | |
| R | ASN318 | |
| J | ASN212 |
