8UFB

Eastern equine encephalitis virus (PE-6) VLP in complex with full-length VLDLR (asymmetric unit)

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	0019028	cellular_component	viral capsid
A	0055036	cellular_component	virion membrane
B	0005198	molecular_function	structural molecule activity
B	0019028	cellular_component	viral capsid
C	0004252	molecular_function	serine-type endopeptidase activity
C	0006508	biological_process	proteolysis
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	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
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	0019028	cellular_component	viral capsid
J	0055036	cellular_component	virion membrane
K	0005198	molecular_function	structural molecule activity
K	0019028	cellular_component	viral capsid
L	0004252	molecular_function	serine-type endopeptidase activity
L	0006508	biological_process	proteolysis
R	0005509	molecular_function	calcium ion binding
S	0005509	molecular_function	calcium ion binding
T	0005509	molecular_function	calcium ion binding
U	0005509	molecular_function	calcium ion binding
V	0005509	molecular_function	calcium ion binding
W	0005509	molecular_function	calcium ion binding
X	0005509	molecular_function	calcium ion binding
Y	0005509	molecular_function	calcium ion binding

Functional Information from PROSITE/UniProt

site_id	PS00010
Number of Residues	12
Details	ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDlvigYeCdC

Chain	Residue	Details
V	CYS371-CYS382
V	CYS410-CYS421

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site_id	PS01186
Number of Residues	15
Details	EGF_2 EGF-like domain signature 2. CdCaaGFelidrkt.C

Chain	Residue	Details
V	CYS380-CYS394
V	CYS419-CYS434
V	CYS734-CYS749

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site_id	PS01187
Number of Residues	24
Details	EGF_CA Calcium-binding EGF-like domain signature. DiDECqnpgi.........Csqi....CiNlkggYkC

Chain	Residue	Details
V	ASP396-CYS419

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site_id	PS01209
Number of Residues	23
Details	LDLRA_1 LDL-receptor class A (LDLRA) domain signature. CItllwk.CDgdeDCvdg.SDEkn...C

Chain	Residue	Details
V	CYS45-CYS67
V	CYS84-CYS108
V	CYS127-CYS149
V	CYS166-CYS188
V	CYS205-CYS229
V	CYS251-CYS273
V	CYS290-CYS312
V	CYS331-CYS355

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
V	ASN151
R	PRO765
S	ASN151
S	PRO765
T	ASN151
T	PRO765
U	ASN151
U	PRO765
V	PRO765
W	ASN151
W	PRO765
X	ASN151
X	PRO765
Y	ASN151
Y	PRO765
R	ASN151

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