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1I4M

Crystal structure of the human prion protein reveals a mechanism for oligomerization

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0051260biological_processprotein homooligomerization
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 300
ChainResidue
AHOH2
AHOH3
AHOH4
AHIS140
AASP147

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD A 301
ChainResidue
AHOH9
AHIS177
AHOH5
AHOH6
AHOH7
AHOH8

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1
ChainResidue
ASER132
ALYS185
AGLN217

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

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973
ChainResidueDetails
AASN197

223166

PDB entries from 2024-07-31

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