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4H88

Structure of POM1 FAB fragment complexed with mouse PrPc Fragment 120-230

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_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
DetailsLIPID: GPI-anchor amidated serine => ECO:0000250|UniProtKB:P04273
ChainResidueDetails
ASER230

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305
ChainResidueDetails
AASN180

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973
ChainResidueDetails
AASN196

218853

PDB entries from 2024-04-24

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