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2W9E

Structure of ICSM 18 (anti-Prp therapeutic antibody) Fab fragment complexed with human Prp fragment 119-231

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0051260biological_processprotein homooligomerization
L0002250biological_processadaptive immune response
L0005515molecular_functionprotein binding
L0005576cellular_componentextracellular region
L0005886cellular_componentplasma membrane
L0030183biological_processB cell differentiation
L0042105cellular_componentalpha-beta T cell receptor complex
L0071735cellular_componentIgG immunoglobulin complex
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 300
ChainResidue
AARG136
HTYR60
HARG65

Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
LTYR191-HIS197

site_idPS00706
Number of Residues19
DetailsPRION_2 Prion protein signature 2. EtDvKMMeRVVeQMCitQY
ChainResidueDetails
AGLU200-TYR218

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12214108","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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

245663

PDB entries from 2025-12-03

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