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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5VU2

Electron cryo-microscopy of "immature" Chikungunya VLP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005198molecular_functionstructural molecule activity
A0019028cellular_componentviral capsid
A0055036cellular_componentvirion membrane
B0004252molecular_functionserine-type endopeptidase activity
B0005198molecular_functionstructural molecule activity
B0019028cellular_componentviral capsid
B0055036cellular_componentvirion membrane
C0004252molecular_functionserine-type endopeptidase activity
C0005198molecular_functionstructural molecule activity
C0019028cellular_componentviral capsid
C0055036cellular_componentvirion membrane
D0004252molecular_functionserine-type endopeptidase activity
D0005198molecular_functionstructural molecule activity
D0019028cellular_componentviral capsid
D0055036cellular_componentvirion membrane
E0004252molecular_functionserine-type endopeptidase activity
E0019028cellular_componentviral capsid
E0055036cellular_componentvirion membrane
F0004252molecular_functionserine-type endopeptidase activity
F0019028cellular_componentviral capsid
F0055036cellular_componentvirion membrane
G0004252molecular_functionserine-type endopeptidase activity
G0019028cellular_componentviral capsid
G0055036cellular_componentvirion membrane
H0004252molecular_functionserine-type endopeptidase activity
H0019028cellular_componentviral capsid
H0055036cellular_componentvirion membrane
I0004252molecular_functionserine-type endopeptidase activity
I0006508biological_processproteolysis
J0004252molecular_functionserine-type endopeptidase activity
J0006508biological_processproteolysis
K0004252molecular_functionserine-type endopeptidase activity
K0006508biological_processproteolysis
L0004252molecular_functionserine-type endopeptidase activity
L0006508biological_processproteolysis
M0004252molecular_functionserine-type endopeptidase activity
M0005198molecular_functionstructural molecule activity
M0019028cellular_componentviral capsid
M0055036cellular_componentvirion membrane
N0004252molecular_functionserine-type endopeptidase activity
N0005198molecular_functionstructural molecule activity
N0019028cellular_componentviral capsid
N0055036cellular_componentvirion membrane
O0004252molecular_functionserine-type endopeptidase activity
O0005198molecular_functionstructural molecule activity
O0019028cellular_componentviral capsid
O0055036cellular_componentvirion membrane
P0004252molecular_functionserine-type endopeptidase activity
P0005198molecular_functionstructural molecule activity
P0019028cellular_componentviral capsid
P0055036cellular_componentvirion membrane
Q0005198molecular_functionstructural molecule activity
Q0019028cellular_componentviral capsid
R0005198molecular_functionstructural molecule activity
R0019028cellular_componentviral capsid
S0005198molecular_functionstructural molecule activity
S0019028cellular_componentviral capsid
T0005198molecular_functionstructural molecule activity
T0019028cellular_componentviral capsid
U0004252molecular_functionserine-type endopeptidase activity
U0019028cellular_componentviral capsid
U0055036cellular_componentvirion membrane
V0004252molecular_functionserine-type endopeptidase activity
V0019028cellular_componentviral capsid
V0055036cellular_componentvirion membrane
W0004252molecular_functionserine-type endopeptidase activity
W0019028cellular_componentviral capsid
W0055036cellular_componentvirion membrane
X0004252molecular_functionserine-type endopeptidase activity
X0019028cellular_componentviral capsid
X0055036cellular_componentvirion membrane
Functional Information from PROSITE/UniProt
site_idPS00238
Number of Residues17
DetailsOPSIN Visual pigments (opsins) retinal binding site. CCiRtAKAATyqEAaiY
ChainResidueDetails
MCYS-68-TYR-52
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues592
DetailsDomain: {"description":"Peptidase S3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues20
DetailsRegion: {"description":"Interaction with spike glycoprotein E2","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues56
DetailsRegion: {"description":"Dimerization of the capsid protein","evidences":[{"source":"UniProtKB","id":"P0DOK1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues40
DetailsMotif: {"description":"Nuclear export signal","evidences":[{"source":"UniProtKB","id":"P09592","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues12
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues8
DetailsSite: {"description":"Involved in dimerization of the capsid protein","evidences":[{"source":"UniProtKB","id":"Q86925","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues160
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues144
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsLipidation: {"description":"S-stearoyl cysteine; by host","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues16
DetailsRegion: {"description":"Interaction with the capsid protein","evidences":[{"source":"PubMed","id":"32783883","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues80
DetailsRegion: {"description":"Transient transmembrane before p62-6K protein processing","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsLipidation: {"description":"S-palmitoyl cysteine; by host","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues8
DetailsLipidation: {"description":"S-palmitoyl cysteine; by host","evidences":[{"source":"UniProtKB","id":"Q5Y388","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2025-12-03

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