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7UN5

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0051260biological_processprotein homooligomerization
B0016020cellular_componentmembrane
B0051260biological_processprotein homooligomerization
C0016020cellular_componentmembrane
C0051260biological_processprotein homooligomerization
D0016020cellular_componentmembrane
D0051260biological_processprotein homooligomerization
E0016020cellular_componentmembrane
E0051260biological_processprotein homooligomerization
F0016020cellular_componentmembrane
F0051260biological_processprotein homooligomerization
G0016020cellular_componentmembrane
G0051260biological_processprotein homooligomerization
H0016020cellular_componentmembrane
H0051260biological_processprotein homooligomerization
I0016020cellular_componentmembrane
I0051260biological_processprotein homooligomerization
J0016020cellular_componentmembrane
J0051260biological_processprotein homooligomerization
Functional Information from PROSITE/UniProt
site_idPS00291
Number of Residues16
DetailsPRION_1 Prion protein signature 1. AGAAAAGAVVGGLGGY
ChainResidueDetails
EALA113-TYR128

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues70
DetailsRepeat: {"description":"5"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11900542","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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