7UN5

Structure of Type II Prion filaments from Gerstmann-Straussler-Scheinker disease

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016020	cellular_component	membrane
A	0051260	biological_process	protein homooligomerization
B	0016020	cellular_component	membrane
B	0051260	biological_process	protein homooligomerization
C	0016020	cellular_component	membrane
C	0051260	biological_process	protein homooligomerization
D	0016020	cellular_component	membrane
D	0051260	biological_process	protein homooligomerization
E	0016020	cellular_component	membrane
E	0051260	biological_process	protein homooligomerization
F	0016020	cellular_component	membrane
F	0051260	biological_process	protein homooligomerization
G	0016020	cellular_component	membrane
G	0051260	biological_process	protein homooligomerization
H	0016020	cellular_component	membrane
H	0051260	biological_process	protein homooligomerization
I	0016020	cellular_component	membrane
I	0051260	biological_process	protein homooligomerization
J	0016020	cellular_component	membrane
J	0051260	biological_process	protein homooligomerization

Functional Information from PROSITE/UniProt

site_id	PS00291
Number of Residues	16
Details	PRION_1 Prion protein signature 1. AGAAAAGAVVGGLGGY

Chain	Residue	Details
E	ALA113-TYR128

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	BINDING: BINDING => ECO:0000305|PubMed:11900542

Chain	Residue	Details
E	HIS85
C	HIS85
C	GLY86
C	GLY87
D	HIS85
D	GLY86
D	GLY87
H	HIS85
H	GLY86
H	GLY87
F	HIS85
E	GLY86
F	GLY86
F	GLY87
G	HIS85
G	GLY86
G	GLY87
I	HIS85
I	GLY86
I	GLY87
J	HIS85
J	GLY86
E	GLY87
J	GLY87
A	HIS85
A	GLY86
A	GLY87
B	HIS85
B	GLY86
B	GLY87

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