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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7CW3

Cryo-EM structure of Chikungunya virus in complex with mAb CHK-263 IgG (subregion around icosahedral 2-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
C0019028cellular_componentviral capsid
C0055036cellular_componentvirion membrane
D0005198molecular_functionstructural molecule activity
D0019028cellular_componentviral capsid
E0004252molecular_functionserine-type endopeptidase activity
E0019028cellular_componentviral capsid
E0055036cellular_componentvirion membrane
F0005198molecular_functionstructural molecule activity
F0019028cellular_componentviral capsid
G0004252molecular_functionserine-type endopeptidase activity
G0019028cellular_componentviral capsid
G0055036cellular_componentvirion membrane
H0005198molecular_functionstructural molecule activity
H0019028cellular_componentviral capsid
I0004252molecular_functionserine-type endopeptidase activity
I0019028cellular_componentviral capsid
I0055036cellular_componentvirion membrane
J0005198molecular_functionstructural molecule activity
J0019028cellular_componentviral capsid
K0004252molecular_functionserine-type endopeptidase activity
K0019028cellular_componentviral capsid
K0055036cellular_componentvirion membrane
L0005198molecular_functionstructural molecule activity
L0019028cellular_componentviral capsid
M0004252molecular_functionserine-type endopeptidase activity
M0019028cellular_componentviral capsid
M0055036cellular_componentvirion membrane
N0005198molecular_functionstructural molecule activity
N0019028cellular_componentviral capsid
O0004252molecular_functionserine-type endopeptidase activity
O0019028cellular_componentviral capsid
O0055036cellular_componentvirion membrane
P0005198molecular_functionstructural molecule activity
P0019028cellular_componentviral capsid
Q0004252molecular_functionserine-type endopeptidase activity
Q0019028cellular_componentviral capsid
Q0055036cellular_componentvirion membrane
R0005198molecular_functionstructural molecule activity
R0019028cellular_componentviral capsid
S0004252molecular_functionserine-type endopeptidase activity
S0019028cellular_componentviral capsid
S0055036cellular_componentvirion membrane
T0005198molecular_functionstructural molecule activity
T0019028cellular_componentviral capsid
U0004252molecular_functionserine-type endopeptidase activity
U0019028cellular_componentviral capsid
U0055036cellular_componentvirion membrane
V0005198molecular_functionstructural molecule activity
V0019028cellular_componentviral capsid
W0004252molecular_functionserine-type endopeptidase activity
W0019028cellular_componentviral capsid
W0055036cellular_componentvirion membrane
X0005198molecular_functionstructural molecule activity
X0019028cellular_componentviral capsid
Y0004252molecular_functionserine-type endopeptidase activity
Y0019028cellular_componentviral capsid
Y0055036cellular_componentvirion membrane
Z0005198molecular_functionstructural molecule activity
Z0019028cellular_componentviral capsid
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
d0005198molecular_functionstructural molecule activity
d0019028cellular_componentviral capsid
e0004252molecular_functionserine-type endopeptidase activity
e0019028cellular_componentviral capsid
e0055036cellular_componentvirion membrane
f0005198molecular_functionstructural molecule activity
f0019028cellular_componentviral capsid
g0004252molecular_functionserine-type endopeptidase activity
g0019028cellular_componentviral capsid
g0055036cellular_componentvirion membrane
h0005198molecular_functionstructural molecule activity
h0019028cellular_componentviral capsid
i0004252molecular_functionserine-type endopeptidase activity
i0019028cellular_componentviral capsid
i0055036cellular_componentvirion membrane
j0005198molecular_functionstructural molecule activity
j0019028cellular_componentviral capsid
s0004252molecular_functionserine-type endopeptidase activity
s0006508biological_processproteolysis
t0004252molecular_functionserine-type endopeptidase activity
t0006508biological_processproteolysis
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
nTYR192-HIS198
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7326
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues720
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues648
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues306
DetailsRegion: {"description":"E1 fusion peptide loop","evidences":[{"source":"PubMed","id":"22978677","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues18
DetailsLipidation: {"description":"S-stearoyl cysteine; by host","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues54
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"UniProtKB","id":"Q5Y388","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues252
DetailsRegion: {"description":"Interaction with host Mxra8 receptor","evidences":[{"source":"UniProtKB","id":"P08491","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues72
DetailsRegion: {"description":"Interaction with the capsid protein","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues360
DetailsRegion: {"description":"Transient transmembrane before p62-6K protein processing","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues18
DetailsLipidation: {"description":"S-palmitoyl cysteine; by host","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues36
DetailsLipidation: {"description":"S-palmitoyl cysteine; by host","evidences":[{"source":"UniProtKB","id":"Q5Y388","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues18
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues296
DetailsDomain: {"description":"Peptidase S3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues6
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues10
DetailsRegion: {"description":"Interaction with spike glycoprotein E2","evidences":[{"source":"UniProtKB","id":"P03316","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues28
DetailsRegion: {"description":"Dimerization of the capsid protein","evidences":[{"source":"UniProtKB","id":"P0DOK1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues20
DetailsMotif: {"description":"Nuclear export signal","evidences":[{"source":"UniProtKB","id":"P09592","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues4
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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