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8YWA

The structure of IgE receptor binding to IgE

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0007166biological_processcell surface receptor signaling pathway
A0009897cellular_componentexternal side of plasma membrane
A0009986cellular_componentcell surface
A0016064biological_processimmunoglobulin mediated immune response
A0016068biological_processtype I hypersensitivity
A0019768molecular_functionhigh-affinity IgE receptor activity
A0019863molecular_functionIgE binding
A0038095biological_processFc-epsilon receptor signaling pathway
A0042092biological_processtype 2 immune response
A0043303biological_processmast cell degranulation
A0043308biological_processeosinophil degranulation
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0006955biological_processimmune response
B0007166biological_processcell surface receptor signaling pathway
B0009897cellular_componentexternal side of plasma membrane
B0016020cellular_componentmembrane
B0019863molecular_functionIgE binding
B0032998cellular_componentFc-epsilon receptor I complex
C0004888molecular_functiontransmembrane signaling receptor activity
C0007166biological_processcell surface receptor signaling pathway
C0016020cellular_componentmembrane
C0019767molecular_functionIgE receptor activity
C0032998cellular_componentFc-epsilon receptor I complex
D0004888molecular_functiontransmembrane signaling receptor activity
D0007166biological_processcell surface receptor signaling pathway
D0016020cellular_componentmembrane
D0019767molecular_functionIgE receptor activity
D0032998cellular_componentFc-epsilon receptor I complex
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. FTCRVAH
ChainResidueDetails
HPHE199-HIS205
HTYR413-HIS419
HPHE519-HIS525
hTYR196-HIS202

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues134
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues80
DetailsDomain: {"description":"Ig-like 1"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues82
DetailsDomain: {"description":"Ig-like 2"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10917520","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11531339","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9875849","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11531339","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues46
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues12
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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