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2KUN

Three dimensional structure of HuPrP(90-231 M129 Q212P)

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0051260biological_processprotein homooligomerization
Functional Information from PROSITE/UniProt
site_idPS00291
Number of Residues16
DetailsPRION_1 Prion protein signature 1. AGAAAAGAVVGGLGGY
ChainResidueDetails
AALA113-TYR128

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsLipidation: {"description":"GPI-anchor amidated serine","evidences":[{"source":"UniProtKB","id":"P04273","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12214108","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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