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6HER

Mouse prion protein in complex with Nanobody 484

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 SO4 A 301
ChainResidue
ASER135
AARG136
ATYR155
AHOH403
BARG27

site_idAC2
Number of Residues4
Detailsbinding site for residue GOL B 201
ChainResidue
BASP112
BHIS113
BTRP114
BHOH301

site_idAC3
Number of Residues9
Detailsbinding site for residue SO4 B 202
ChainResidue
AMET138
AHIS140
AARG151
BGLN39
BGLY44
BARG45
BARG108
BHOH312
BHOH352

site_idAC4
Number of Residues7
Detailsbinding site for residue SO4 B 203
ChainResidue
ASER170
AASN174
BARG38
BTHR61
BSER63
BHOH310
BHOH339

Functional Information from PROSITE/UniProt
site_idPS00706
Number of Residues19
DetailsPRION_2 Prion protein signature 2. EtDvKMMeRVVeQMCvtQY
ChainResidueDetails
AGLU200-TYR218

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

250359

PDB entries from 2026-03-11

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