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8SQN

CryoEM structure of Western equine encephalitis virus VLP in complex with the chimeric Du-D1-Mo-D2 MXRA8 receptor

Functional Information from GO Data
ChainGOidnamespacecontents
A0007155biological_processcell adhesion
A0016020cellular_componentmembrane
B0004252molecular_functionserine-type endopeptidase activity
B0019028cellular_componentviral capsid
B0055036cellular_componentvirion membrane
D0005198molecular_functionstructural molecule activity
D0019028cellular_componentviral capsid
F0004252molecular_functionserine-type endopeptidase activity
F0019028cellular_componentviral capsid
F0055036cellular_componentvirion membrane
H0005198molecular_functionstructural molecule activity
H0019028cellular_componentviral capsid
J0004252molecular_functionserine-type endopeptidase activity
J0019028cellular_componentviral capsid
J0055036cellular_componentvirion membrane
L0005198molecular_functionstructural molecule activity
L0019028cellular_componentviral capsid
N0004252molecular_functionserine-type endopeptidase activity
N0019028cellular_componentviral capsid
N0055036cellular_componentvirion membrane
P0005198molecular_functionstructural molecule activity
P0019028cellular_componentviral capsid
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues132
DetailsDomain: {"description":"Ig-like V-type 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsMotif: {"description":"RGD 1","evidences":[{"source":"PubMed","id":"18366072","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsMotif: {"description":"RGD 2","evidences":[{"source":"PubMed","id":"18366072","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9BRK3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1580
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues160
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues68
DetailsRegion: {"description":"E1 fusion peptide loop","evidences":[{"source":"UniProtKB","id":"Q8JUX5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues16
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"UniProtKB","id":"Q5Y388","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues16
DetailsRegion: {"description":"Interaction with the capsid protein","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues4
DetailsLipidation: {"description":"S-palmitoyl cysteine; by host","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues4
DetailsLipidation: {"description":"S-palmitoyl cysteine; by host","evidences":[{"source":"UniProtKB","id":"Q5Y388","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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