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7FFQ

Cryo-EM structure of VEEV VLP at the 2-fold axes

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0004252molecular_functionserine-type endopeptidase activity
B0019028cellular_componentviral capsid
B0055036cellular_componentvirion membrane
C0004252molecular_functionserine-type endopeptidase activity
C0019028cellular_componentviral capsid
C0055036cellular_componentvirion membrane
F0004252molecular_functionserine-type endopeptidase activity
F0006508biological_processproteolysis
G0004252molecular_functionserine-type endopeptidase activity
G0019028cellular_componentviral capsid
G0055036cellular_componentvirion membrane
I0004252molecular_functionserine-type endopeptidase activity
I0019028cellular_componentviral capsid
I0055036cellular_componentvirion membrane
J0005198molecular_functionstructural molecule activity
J0019028cellular_componentviral capsid
P0004252molecular_functionserine-type endopeptidase activity
P0019028cellular_componentviral capsid
P0055036cellular_componentvirion membrane
Q0005198molecular_functionstructural molecule activity
Q0019028cellular_componentviral capsid
R0005198molecular_functionstructural molecule activity
R0019028cellular_componentviral capsid
S0004252molecular_functionserine-type endopeptidase activity
S0006508biological_processproteolysis
T0004252molecular_functionserine-type endopeptidase activity
T0019028cellular_componentviral capsid
T0055036cellular_componentvirion membrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues447
DetailsDomain: {"description":"Peptidase S3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsSite: {"description":"Involved in dimerization of the capsid protein","evidences":[{"source":"UniProtKB","id":"Q86925","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P09592","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P09592","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1221
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues120
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues16
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues51
DetailsRegion: {"description":"E1 fusion peptide loop","evidences":[{"source":"UniProtKB","id":"Q8JUX5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues12
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues18
DetailsSite: {"description":"Interaction with host receptor LDLRAD3","evidences":[{"source":"PubMed","id":"34646020","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues9
DetailsLipidation: {"description":"S-palmitoyl cysteine; by host","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2025-08-27

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