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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8YW2

Semliki Forest virus viron in complex with VLDLR

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
00004252molecular_functionserine-type endopeptidase activity
00019028cellular_componentviral capsid
00055036cellular_componentvirion membrane
10004252molecular_functionserine-type endopeptidase activity
10006508biological_processproteolysis
20004252molecular_functionserine-type endopeptidase activity
20019028cellular_componentviral capsid
20055036cellular_componentvirion membrane
30004252molecular_functionserine-type endopeptidase activity
30006508biological_processproteolysis
40004252molecular_functionserine-type endopeptidase activity
40019028cellular_componentviral capsid
40055036cellular_componentvirion membrane
50004252molecular_functionserine-type endopeptidase activity
50019028cellular_componentviral capsid
50055036cellular_componentvirion membrane
60004252molecular_functionserine-type endopeptidase activity
60019028cellular_componentviral capsid
60055036cellular_componentvirion membrane
70005198molecular_functionstructural molecule activity
70019028cellular_componentviral capsid
80005198molecular_functionstructural molecule activity
80019028cellular_componentviral capsid
90005198molecular_functionstructural molecule activity
90019028cellular_componentviral capsid
AA0004252molecular_functionserine-type endopeptidase activity
AA0019028cellular_componentviral capsid
AA0055036cellular_componentvirion membrane
AB0004252molecular_functionserine-type endopeptidase activity
AB0019028cellular_componentviral capsid
AB0055036cellular_componentvirion membrane
AC0004252molecular_functionserine-type endopeptidase activity
AC0006508biological_processproteolysis
AD0004252molecular_functionserine-type endopeptidase activity
AD0006508biological_processproteolysis
AE0004252molecular_functionserine-type endopeptidase activity
AE0006508biological_processproteolysis
B0005198molecular_functionstructural molecule activity
B0019028cellular_componentviral capsid
D0004252molecular_functionserine-type endopeptidase activity
D0006508biological_processproteolysis
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
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
R0005198molecular_functionstructural molecule activity
R0019028cellular_componentviral capsid
S0004252molecular_functionserine-type endopeptidase activity
S0019028cellular_componentviral capsid
S0055036cellular_componentvirion membrane
T0004252molecular_functionserine-type endopeptidase activity
T0006508biological_processproteolysis
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
X0005198molecular_functionstructural molecule activity
X0019028cellular_componentviral capsid
Y0005198molecular_functionstructural molecule activity
Y0019028cellular_componentviral capsid
Z0005198molecular_functionstructural molecule activity
Z0019028cellular_componentviral capsid
a0004252molecular_functionserine-type endopeptidase activity
a0019028cellular_componentviral capsid
a0055036cellular_componentvirion membrane
b0004252molecular_functionserine-type endopeptidase activity
b0019028cellular_componentviral capsid
b0055036cellular_componentvirion membrane
c0004252molecular_functionserine-type endopeptidase activity
c0019028cellular_componentviral capsid
c0055036cellular_componentvirion membrane
d0004252molecular_functionserine-type endopeptidase activity
d0006508biological_processproteolysis
e0004252molecular_functionserine-type endopeptidase activity
e0006508biological_processproteolysis
f0004252molecular_functionserine-type endopeptidase activity
f0006508biological_processproteolysis
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
i0019028cellular_componentviral capsid
i0055036cellular_componentvirion membrane
j0005198molecular_functionstructural molecule activity
j0019028cellular_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
n0006508biological_processproteolysis
o0004252molecular_functionserine-type endopeptidase activity
o0019028cellular_componentviral capsid
o0055036cellular_componentvirion membrane
p0004252molecular_functionserine-type endopeptidase activity
p0019028cellular_componentviral capsid
p0055036cellular_componentvirion membrane
q0004252molecular_functionserine-type endopeptidase activity
q0019028cellular_componentviral capsid
q0055036cellular_componentvirion membrane
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
x0006508biological_processproteolysis
y0004252molecular_functionserine-type endopeptidase activity
y0006508biological_processproteolysis
z0005198molecular_functionstructural molecule activity
z0019028cellular_componentviral capsid
Functional Information from PROSITE/UniProt
site_idPS01209
Number of Residues25
DetailsLDLRA_1 LDL-receptor class A (LDLRA) domain signature. CVpsrwk.CDgdpDCedg.SDEspeq.C
ChainResidueDetails
ACYS84-CYS108
ACYS127-CYS149
ACYS166-CYS188
ACYS205-CYS229
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2368
DetailsDomain: {"description":"Peptidase S3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues80
DetailsRegion: {"description":"Interaction with spike glycoprotein E2","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues224
DetailsRegion: {"description":"Dimerization of the capsid protein","evidences":[{"source":"UniProtKB","id":"P0DOK1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues160
DetailsMotif: {"description":"Nuclear export signal","evidences":[{"source":"UniProtKB","id":"P09592","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues32
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues16
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_FI8
Number of Residues32
DetailsSite: {"description":"Involved in dimerization of the capsid protein","evidences":[{"source":"UniProtKB","id":"Q86925","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues640
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues528
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues272
DetailsRegion: {"description":"E1 fusion peptide loop","evidences":[{"source":"UniProtKB","id":"Q8JUX5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1280
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_FI13
Number of Residues16
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_FI14
Number of Residues64
DetailsSite: {"description":"Interaction with host receptor VLDLR","evidences":[{"source":"PubMed","id":"37098345","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues32
DetailsSite: {"description":"Interaction with host receptor VLDLR","evidences":[{"source":"PubMed","id":"39095394","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues16
DetailsLipidation: {"description":"S-stearoyl cysteine; by host","evidences":[{"source":"PubMed","id":"3143715","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues16
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_FI18
Number of Residues48
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"UniProtKB","id":"Q5Y388","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues64
DetailsRegion: {"description":"Interaction with the capsid protein","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues320
DetailsRegion: {"description":"Transient transmembrane before p62-6K protein processing","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues32
DetailsLipidation: {"description":"S-stearoyl cysteine; by host","evidences":[{"source":"UniProtKB","id":"Q5Y388","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues32
DetailsLipidation: {"description":"S-palmitoyl cysteine; by host","evidences":[{"source":"UniProtKB","id":"Q5Y388","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues40
DetailsDomain: {"description":"LDL-receptor class A 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00124","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues40
DetailsDomain: {"description":"LDL-receptor class A 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00124","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues38
DetailsDomain: {"description":"LDL-receptor class A 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00124","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues40
DetailsDomain: {"description":"LDL-receptor class A 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00124","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues22
DetailsRegion: {"description":"(Microbial infection) Interaction with Semliki virus spike glycoprotein E1","evidences":[{"source":"PubMed","id":"37098345","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

244693

PDB entries from 2025-11-12

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