6NK6

Electron Cryo-Microscopy Of Chikungunya VLP in complex with mouse Mxra8 receptor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0019028	cellular_component	viral capsid
A	0055036	cellular_component	virion membrane
B	0004252	molecular_function	serine-type endopeptidase activity
B	0019028	cellular_component	viral capsid
B	0055036	cellular_component	virion membrane
C	0004252	molecular_function	serine-type endopeptidase activity
C	0019028	cellular_component	viral capsid
C	0055036	cellular_component	virion membrane
D	0004252	molecular_function	serine-type endopeptidase activity
D	0019028	cellular_component	viral capsid
D	0055036	cellular_component	virion membrane
E	0005198	molecular_function	structural molecule activity
E	0019028	cellular_component	viral capsid
F	0005198	molecular_function	structural molecule activity
F	0019028	cellular_component	viral capsid
G	0005198	molecular_function	structural molecule activity
G	0019028	cellular_component	viral capsid
H	0005198	molecular_function	structural molecule activity
H	0019028	cellular_component	viral capsid
I	0004252	molecular_function	serine-type endopeptidase activity
I	0006508	biological_process	proteolysis
J	0004252	molecular_function	serine-type endopeptidase activity
J	0006508	biological_process	proteolysis
K	0004252	molecular_function	serine-type endopeptidase activity
K	0006508	biological_process	proteolysis
L	0004252	molecular_function	serine-type endopeptidase activity
L	0006508	biological_process	proteolysis
M	0007155	biological_process	cell adhesion
M	0016020	cellular_component	membrane
N	0007155	biological_process	cell adhesion
N	0016020	cellular_component	membrane
O	0007155	biological_process	cell adhesion
O	0016020	cellular_component	membrane
P	0007155	biological_process	cell adhesion
P	0016020	cellular_component	membrane

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027

Chain	Residue	Details
I	HIS139
L	HIS139
L	ASP161
L	SER213
I	ASP161
I	SER213
J	HIS139
J	ASP161
J	SER213
K	HIS139
K	ASP161
K	SER213

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site_id	SWS_FT_FI2
Number of Residues	8
Details	SITE: Involved in dimerization of the capsid protein => ECO:0000250|UniProtKB:Q86925

Chain	Residue	Details
I	TYR187
I	ASN220
J	TYR187
J	ASN220
K	TYR187
K	ASN220
L	TYR187
L	ASN220

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site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Cleavage; by autolysis => ECO:0000250|UniProtKB:P03315

Chain	Residue	Details
I	TRP261
J	TRP261
K	TRP261
L	TRP261

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site_id	SWS_FT_FI4
Number of Residues	12
Details	LIPID: S-palmitoyl cysteine; by host => ECO:0000250

Chain	Residue	Details
E	CYS396
H	CYS396
H	CYS416
H	CYS417
E	CYS416
E	CYS417
F	CYS396
F	CYS416
F	CYS417
G	CYS396
G	CYS416
G	CYS417

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site_id	SWS_FT_FI5
Number of Residues	8
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255

Chain	Residue	Details
E	ASN263
E	ASN345
F	ASN263
F	ASN345
G	ASN263
G	ASN345
H	ASN263
H	ASN345

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