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3HER

Human prion protein variant F198S with V129

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0051260biological_processprotein homooligomerization
B0016020cellular_componentmembrane
B0051260biological_processprotein homooligomerization
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 300
ChainResidue
AHIS140
AASP147
AHOH324
AHOH325
BHIS177

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD B 301
ChainResidue
AHIS177
BHIS140
BASP147
BHOH438

Functional Information from PROSITE/UniProt
site_idPS00291
Number of Residues16
DetailsPRION_1 Prion protein signature 1. AGAAAAGAVVGGLGGY
ChainResidueDetails
AALA113-TYR128

site_idPS00706
Number of Residues19
DetailsPRION_2 Prion protein signature 2. EtDvKMMeRVVeQMCitQY
ChainResidueDetails
AGLU200-TYR218

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12214108","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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