8DEE
Asymmetric Unit of Western Equine Encephalitis Virus
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 |
E | 0004252 | molecular_function | serine-type endopeptidase activity |
E | 0006508 | biological_process | proteolysis |
F | 0004252 | molecular_function | serine-type endopeptidase activity |
F | 0019028 | cellular_component | viral capsid |
F | 0055036 | cellular_component | virion membrane |
G | 0005198 | molecular_function | structural molecule activity |
G | 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 |
M | 0004252 | molecular_function | serine-type endopeptidase activity |
M | 0006508 | biological_process | proteolysis |
N | 0004252 | molecular_function | serine-type endopeptidase activity |
N | 0019028 | cellular_component | viral capsid |
N | 0055036 | cellular_component | virion membrane |
O | 0005198 | molecular_function | structural molecule activity |
O | 0019028 | cellular_component | viral capsid |
R | 0004252 | molecular_function | serine-type endopeptidase activity |
R | 0006508 | biological_process | proteolysis |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1580 |
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 | 36 |
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 | 16 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"UniProtKB","id":"Q5Y388","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 16 |
Details | Region: {"description":"Interaction with the capsid protein","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 80 |
Details | Region: {"description":"Transient transmembrane before p62-6K protein processing","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | Lipidation: {"description":"S-palmitoyl cysteine; by host","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 8 |
Details | Lipidation: {"description":"S-palmitoyl cysteine; by host","evidences":[{"source":"UniProtKB","id":"Q5Y388","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
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_FI12 |
Number of Residues | 36 |
Details | Region: {"description":"Interaction with spike glycoprotein E2","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
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_FI14 |
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_FI15 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P09592","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P09592","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |