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4YXL

Crystal structure of Syrian hamster prion protein complexed with POM1 FAB

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 NA L 301
ChainResidue
HSER191
HSER195
HGLU196
LGLU79
LGLU81

Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
LTYR192-HIS198

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. EtDiKIMeRVVeQMCttQY
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":"3138115","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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