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3HJX

Human prion protein variant D178N with V129

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0051260biological_processprotein homooligomerization
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD A 300
ChainResidue
AHIS140
AASP147
AHIS177
AHOH302
AHOH350
AHOH354

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 301
ChainResidue
AASN173

Functional Information from PROSITE/UniProt
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 Residues1
DetailsLIPID: GPI-anchor amidated serine => ECO:0000250|UniProtKB:P04273
ChainResidueDetails
ASER230

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12214108
ChainResidueDetails
AASN181

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973
ChainResidueDetails
AASN197

237423

PDB entries from 2025-06-11

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