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6HHD

Mouse Prion Protein in complex with Nanobody 484

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0051260biological_processprotein homooligomerization
C0016020cellular_componentmembrane
C0051260biological_processprotein homooligomerization
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue SO4 B 201
ChainResidue
BGLN39
DHOH340
BGLY44
BARG45
BARG108
BHOH301
BHOH333
DGLY44
DARG45
DARG108

site_idAC2
Number of Residues4
Detailsbinding site for residue CL B 202
ChainResidue
BGLN116
BHOH306
BHOH382
CNA303

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL C 301
ChainResidue
CSER222
CTYR225
CHOH418

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 C 302
ChainResidue
AHIS140
CMET138
CHIS140
CARG151
CHOH415

site_idAC5
Number of Residues6
Detailsbinding site for residue NA C 303
ChainResidue
BCL202
BHOH382
CARG164
CGLN168
DGLY109
DHOH310

site_idAC6
Number of Residues5
Detailsbinding site for residue SO4 D 201
ChainResidue
DGLN1
DVAL2
DARG98
DHIS113
DHOH302

site_idAC7
Number of Residues6
Detailsbinding site for residue SO4 D 202
ChainResidue
BASP112
BHIS113
BHOH305
DCL203
DHOH328
DHOH342

site_idAC8
Number of Residues2
Detailsbinding site for residue CL D 203
ChainResidue
DHIS113
DSO4202

Functional Information from PROSITE/UniProt
site_idPS00706
Number of Residues19
DetailsPRION_2 Prion protein signature 2. EtDvKMMeRVVeQMCvtQY
ChainResidueDetails
CGLU200-TYR218
AGLU200-TYR218

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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