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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7CW2

Cryo-EM structure of Chikungunya virus in complex with Fab fragments of mAb CHK-263 (subregion around icosahedral 5-fold vertex)

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
C0006508biological_processproteolysis
D0004252molecular_functionserine-type endopeptidase activity
D0019028cellular_componentviral capsid
D0055036cellular_componentvirion membrane
E0005198molecular_functionstructural molecule activity
E0019028cellular_componentviral capsid
F0004252molecular_functionserine-type endopeptidase activity
F0006508biological_processproteolysis
G0004252molecular_functionserine-type endopeptidase activity
G0019028cellular_componentviral capsid
G0055036cellular_componentvirion membrane
H0005198molecular_functionstructural molecule activity
H0019028cellular_componentviral capsid
I0004252molecular_functionserine-type endopeptidase activity
I0006508biological_processproteolysis
J0004252molecular_functionserine-type endopeptidase activity
J0019028cellular_componentviral capsid
J0055036cellular_componentvirion membrane
K0005198molecular_functionstructural molecule activity
K0019028cellular_componentviral capsid
L0004252molecular_functionserine-type endopeptidase activity
L0006508biological_processproteolysis
M0004252molecular_functionserine-type endopeptidase activity
M0019028cellular_componentviral capsid
M0055036cellular_componentvirion membrane
N0005198molecular_functionstructural molecule activity
N0019028cellular_componentviral capsid
O0004252molecular_functionserine-type endopeptidase activity
O0006508biological_processproteolysis
P0004252molecular_functionserine-type endopeptidase activity
P0019028cellular_componentviral capsid
P0055036cellular_componentvirion membrane
Q0005198molecular_functionstructural molecule activity
Q0019028cellular_componentviral capsid
R0004252molecular_functionserine-type endopeptidase activity
R0006508biological_processproteolysis
S0004252molecular_functionserine-type endopeptidase activity
S0006508biological_processproteolysis
a0004252molecular_functionserine-type endopeptidase activity
a0019028cellular_componentviral capsid
a0055036cellular_componentvirion membrane
b0005198molecular_functionstructural molecule activity
b0019028cellular_componentviral capsid
c0004252molecular_functionserine-type endopeptidase activity
c0006508biological_processproteolysis
d0004252molecular_functionserine-type endopeptidase activity
d0019028cellular_componentviral capsid
d0055036cellular_componentvirion membrane
e0005198molecular_functionstructural molecule activity
e0019028cellular_componentviral capsid
f0004252molecular_functionserine-type endopeptidase activity
f0006508biological_processproteolysis
g0004252molecular_functionserine-type endopeptidase activity
g0019028cellular_componentviral capsid
g0055036cellular_componentvirion membrane
h0005198molecular_functionstructural molecule activity
h0019028cellular_componentviral capsid
i0004252molecular_functionserine-type endopeptidase activity
i0006508biological_processproteolysis
j0004252molecular_functionserine-type endopeptidase activity
j0019028cellular_componentviral capsid
j0055036cellular_componentvirion membrane
k0005198molecular_functionstructural molecule activity
k0019028cellular_componentviral capsid
l0004252molecular_functionserine-type endopeptidase activity
l0006508biological_processproteolysis
m0004252molecular_functionserine-type endopeptidase activity
m0019028cellular_componentviral capsid
m0055036cellular_componentvirion membrane
n0005198molecular_functionstructural molecule activity
n0019028cellular_componentviral capsid
o0004252molecular_functionserine-type endopeptidase activity
o0006508biological_processproteolysis
p0004252molecular_functionserine-type endopeptidase activity
p0019028cellular_componentviral capsid
p0055036cellular_componentvirion membrane
q0005198molecular_functionstructural molecule activity
q0019028cellular_componentviral capsid
r0004252molecular_functionserine-type endopeptidase activity
r0006508biological_processproteolysis
s0004252molecular_functionserine-type endopeptidase activity
s0019028cellular_componentviral capsid
s0055036cellular_componentvirion membrane
t0005198molecular_functionstructural molecule activity
t0019028cellular_componentviral capsid
u0004252molecular_functionserine-type endopeptidase activity
u0006508biological_processproteolysis
v0004252molecular_functionserine-type endopeptidase activity
v0019028cellular_componentviral capsid
v0055036cellular_componentvirion membrane
w0005198molecular_functionstructural molecule activity
w0019028cellular_componentviral capsid
x0004252molecular_functionserine-type endopeptidase activity
x0006508biological_processproteolysis
y0004252molecular_functionserine-type endopeptidase activity
y0019028cellular_componentviral capsid
y0055036cellular_componentvirion membrane
z0005198molecular_functionstructural molecule activity
z0019028cellular_componentviral capsid
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
TTYR192-HIS198
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6105
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues600
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues540
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues255
DetailsRegion: {"description":"E1 fusion peptide loop","evidences":[{"source":"PubMed","id":"22978677","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues15
DetailsLipidation: {"description":"S-stearoyl cysteine; by host","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues45
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"UniProtKB","id":"Q5Y388","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues210
DetailsRegion: {"description":"Interaction with host Mxra8 receptor","evidences":[{"source":"UniProtKB","id":"P08491","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues60
DetailsRegion: {"description":"Interaction with the capsid protein","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues300
DetailsRegion: {"description":"Transient transmembrane before p62-6K protein processing","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues15
DetailsLipidation: {"description":"S-palmitoyl cysteine; by host","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues30
DetailsLipidation: {"description":"S-palmitoyl cysteine; by host","evidences":[{"source":"UniProtKB","id":"Q5Y388","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues15
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2220
DetailsDomain: {"description":"Peptidase S3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues45
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues75
DetailsRegion: {"description":"Interaction with spike glycoprotein E2","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues210
DetailsRegion: {"description":"Dimerization of the capsid protein","evidences":[{"source":"UniProtKB","id":"P0DOK1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues150
DetailsMotif: {"description":"Nuclear export signal","evidences":[{"source":"UniProtKB","id":"P09592","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues30
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 2025-12-03

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