7SFU
CryoEM structure of Venezuelan Equine Encephalitis virus (VEEV) TC-83 strain VLP
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 | 0005198 | molecular_function | structural molecule activity |
| B | 0019028 | cellular_component | viral capsid |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0019028 | cellular_component | viral capsid |
| D | 0055036 | cellular_component | virion membrane |
| E | 0005198 | molecular_function | structural molecule activity |
| E | 0019028 | cellular_component | viral capsid |
| 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 |
| H | 0005198 | molecular_function | structural molecule activity |
| H | 0019028 | cellular_component | viral capsid |
| I | 0004252 | molecular_function | serine-type endopeptidase activity |
| I | 0006508 | biological_process | proteolysis |
| J | 0004252 | molecular_function | serine-type endopeptidase activity |
| J | 0019028 | cellular_component | viral capsid |
| J | 0055036 | cellular_component | virion membrane |
| K | 0005198 | molecular_function | structural molecule activity |
| K | 0019028 | cellular_component | viral capsid |
| L | 0004252 | molecular_function | serine-type endopeptidase activity |
| L | 0006508 | biological_process | proteolysis |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1628 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 160 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 168 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 68 |
| Details | Region: {"description":"E1 fusion peptide loop","evidences":[{"source":"UniProtKB","id":"Q8JUX5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 24 |
| Details | Site: {"description":"Interaction with host receptor LDLRAD3","evidences":[{"source":"PubMed","id":"34646020","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine; by host","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 596 |
| Details | Domain: {"description":"Peptidase S3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 12 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| 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_FI11 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P09592","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P09592","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
