8EWF
CryoEM structure of Western equine encephalitis virus VLP in complex with the avian MXRA8 receptor
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 |
| C | 0005198 | molecular_function | structural molecule activity |
| C | 0019028 | cellular_component | viral capsid |
| E | 0007155 | biological_process | cell adhesion |
| E | 0016020 | cellular_component | membrane |
| G | 0004252 | molecular_function | serine-type endopeptidase activity |
| G | 0019028 | cellular_component | viral capsid |
| G | 0055036 | cellular_component | virion membrane |
| I | 0005198 | molecular_function | structural molecule activity |
| I | 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 |
| M | 0005198 | molecular_function | structural molecule activity |
| M | 0019028 | cellular_component | viral capsid |
| O | 0004252 | molecular_function | serine-type endopeptidase activity |
| O | 0019028 | cellular_component | viral capsid |
| O | 0055036 | cellular_component | virion membrane |
| Q | 0005198 | molecular_function | structural molecule activity |
| Q | 0019028 | cellular_component | viral capsid |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI2 |
| Number of Residues | 1628 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 160 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 144 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| 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_FI6 |
| Number of Residues | 4 |
| Details | Lipidation: {"description":"S-stearoyl cysteine; by host","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"UniProtKB","id":"Q5Y388","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 56 |
| Details | Region: {"description":"Interaction with host Mxra8 receptor","evidences":[{"source":"PubMed","id":"32783883","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 16 |
| Details | Region: {"description":"Interaction with the capsid protein","evidences":[{"source":"PubMed","id":"32783883","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| 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_FI11 |
| 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_FI12 |
| 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_FI13 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 132 |
| Details | Domain: {"description":"Ig-like V-type 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | Motif: {"description":"RGD 1","evidences":[{"source":"PubMed","id":"18366072","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | Motif: {"description":"RGD 2","evidences":[{"source":"PubMed","id":"18366072","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9BRK3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
