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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8YW0

Semliki Forest virus viron

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
D0004252molecular_functionserine-type endopeptidase activity
D0006508biological_processproteolysis
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
I0005198molecular_functionstructural molecule activity
I0019028cellular_componentviral capsid
J0005198molecular_functionstructural molecule activity
J0019028cellular_componentviral capsid
K0005198molecular_functionstructural molecule activity
K0019028cellular_componentviral capsid
L0004252molecular_functionserine-type endopeptidase activity
L0019028cellular_componentviral capsid
L0055036cellular_componentvirion membrane
M0004252molecular_functionserine-type endopeptidase activity
M0019028cellular_componentviral capsid
M0055036cellular_componentvirion membrane
N0004252molecular_functionserine-type endopeptidase activity
N0019028cellular_componentviral capsid
N0055036cellular_componentvirion membrane
O0004252molecular_functionserine-type endopeptidase activity
O0006508biological_processproteolysis
P0004252molecular_functionserine-type endopeptidase activity
P0006508biological_processproteolysis
Q0004252molecular_functionserine-type endopeptidase activity
Q0006508biological_processproteolysis
Functional Information from PROSITE/UniProt
site_idPS01209
Number of Residues25
DetailsLDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIpiswv.CDddaDCsdq.SDEsleq.C
ChainResidueDetails
ECYS205-CYS229
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues160
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues132
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues68
DetailsRegion: {"description":"E1 fusion peptide loop","evidences":[{"source":"UniProtKB","id":"Q8JUX5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues320
DetailsRegion: {"description":"E1-DIII; interaction with host receptor VLDLR","evidences":[{"source":"PubMed","id":"16407067","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37098345","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Interaction with host receptor VLDLR","evidences":[{"source":"PubMed","id":"37098345","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39095394","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues16
DetailsSite: {"description":"Interaction with host receptor VLDLR","evidences":[{"source":"PubMed","id":"37098345","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues8
DetailsSite: {"description":"Interaction with host receptor VLDLR","evidences":[{"source":"PubMed","id":"39095394","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsLipidation: {"description":"S-stearoyl cysteine; by host","evidences":[{"source":"PubMed","id":"3143715","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"PubMed","id":"14737160","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6985476","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues12
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"UniProtKB","id":"Q5Y388","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues16
DetailsRegion: {"description":"Interaction with the capsid protein","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]}
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 Residues8
DetailsLipidation: {"description":"S-stearoyl cysteine; by host","evidences":[{"source":"UniProtKB","id":"Q5Y388","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
site_idSWS_FT_FI15
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues592
DetailsDomain: {"description":"Peptidase S3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues20
DetailsRegion: {"description":"Interaction with spike glycoprotein E2","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues56
DetailsRegion: {"description":"Dimerization of the capsid protein","evidences":[{"source":"UniProtKB","id":"P0DOK1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues40
DetailsMotif: {"description":"Nuclear export signal","evidences":[{"source":"UniProtKB","id":"P09592","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues8
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues4
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3553612","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues8
DetailsSite: {"description":"Involved in dimerization of the capsid protein","evidences":[{"source":"UniProtKB","id":"Q86925","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2025-12-24

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