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6AQ7

Structure of POM6 FAB fragment complexed with mouse PrPc

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0051260biological_processprotein homooligomerization
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue GOL A 501
ChainResidue
ATYR148
AARG155
AASN196
AASP201
AHOH637
LTHR31
LTYR36

site_idAC2
Number of Residues4
Detailsbinding site for residue TCE H 301
ChainResidue
HHOH439
HHOH450
HGLU45
HASN60

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL L 401
ChainResidue
LSER28
LSER30
LTHR31
LTHR71
LLYS72

Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
LTYR196-HIS202

site_idPS00706
Number of Residues19
DetailsPRION_2 Prion protein signature 2. EtDvKMMeRVVeQMCvtQY
ChainResidueDetails
AGLU199-TYR217

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

247947

PDB entries from 2026-01-21

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