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9DQY

Structure of western equine encephalitis virus Imperial 181 VLP in complex with house sparrow PCDH10 EC1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0019028cellular_componentviral capsid
A0055036cellular_componentvirion membrane
B0005198molecular_functionstructural molecule activity
B0019028cellular_componentviral capsid
C0004252molecular_functionserine-type endopeptidase activity
C0019028cellular_componentviral capsid
C0055036cellular_componentvirion membrane
D0005198molecular_functionstructural molecule activity
D0019028cellular_componentviral capsid
E0004252molecular_functionserine-type endopeptidase activity
E0019028cellular_componentviral capsid
E0055036cellular_componentvirion membrane
F0005198molecular_functionstructural molecule activity
F0019028cellular_componentviral capsid
G0005509molecular_functioncalcium ion binding
G0005886cellular_componentplasma membrane
G0007155biological_processcell adhesion
G0007156biological_processhomophilic cell-cell adhesion
G0016020cellular_componentmembrane
H0005509molecular_functioncalcium ion binding
H0005886cellular_componentplasma membrane
H0007155biological_processcell adhesion
H0007156biological_processhomophilic cell-cell adhesion
H0016020cellular_componentmembrane
I0005509molecular_functioncalcium ion binding
I0005886cellular_componentplasma membrane
I0007155biological_processcell adhesion
I0007156biological_processhomophilic cell-cell adhesion
I0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. IeVlDiNDNpP
ChainResidueDetails
GILE92-PRO102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues790
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues120
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues51
DetailsRegion: {"description":"E1 fusion peptide loop","evidences":[{"source":"UniProtKB","id":"Q8JUX5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"UniProtKB","id":"Q5Y388","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues12
DetailsRegion: {"description":"Interaction with the capsid protein","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsLipidation: {"description":"S-palmitoyl cysteine; by host","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

251801

PDB entries from 2026-04-08

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