7FFQ

Cryo-EM structure of VEEV VLP at the 2-fold axes

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0006508	biological_process	proteolysis
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
F	0004252	molecular_function	serine-type endopeptidase activity
F	0006508	biological_process	proteolysis
G	0004252	molecular_function	serine-type endopeptidase activity
G	0019028	cellular_component	viral capsid
G	0055036	cellular_component	virion membrane
I	0004252	molecular_function	serine-type endopeptidase activity
I	0019028	cellular_component	viral capsid
I	0055036	cellular_component	virion membrane
J	0005198	molecular_function	structural molecule activity
J	0019028	cellular_component	viral capsid
P	0004252	molecular_function	serine-type endopeptidase activity
P	0019028	cellular_component	viral capsid
P	0055036	cellular_component	virion membrane
Q	0005198	molecular_function	structural molecule activity
Q	0019028	cellular_component	viral capsid
R	0005198	molecular_function	structural molecule activity
R	0019028	cellular_component	viral capsid
S	0004252	molecular_function	serine-type endopeptidase activity
S	0006508	biological_process	proteolysis
T	0004252	molecular_function	serine-type endopeptidase activity
T	0019028	cellular_component	viral capsid
T	0055036	cellular_component	virion membrane

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	60
Details	TRANSMEM: Helical => ECO:0000255

Chain	Residue	Details
J	ILE368-LEU388
Q	ILE368-LEU388
R	ILE368-LEU388
F	HIS152
F	ASP174
F	SER226
S	HIS152
S	ASP174
S	SER226

---

site_id	SWS_FT_FI2
Number of Residues	102
Details	TOPO_DOM: Cytoplasmic => ECO:0000255

Chain	Residue	Details
J	PHE389-ALA423
Q	PHE389-ALA423
R	PHE389-ALA423
F	ASN233
S	TYR200
S	ASN233

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site_id	SWS_FT_FI3
Number of Residues	3
Details	SITE: Cleavage; by host signal peptidase => ECO:0000250

Chain	Residue	Details
J	ALA423
Q	ALA423
R	ALA423

---

site_id	SWS_FT_FI4
Number of Residues	9
Details	LIPID: S-palmitoyl cysteine; by host => ECO:0000250

Chain	Residue	Details
J	CYS396
J	CYS416
J	CYS417
Q	CYS396
Q	CYS416
Q	CYS417
R	CYS396
R	CYS416
R	CYS417

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site_id	SWS_FT_FI5
Number of Residues	6
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255

Chain	Residue	Details
J	ASN212
J	ASN318
Q	ASN212
Q	ASN318
R	ASN212
R	ASN318

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