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8ZGT

Structure of the ige-fc bound to its high affinity receptor fc(epsilon)ri state3

Functional Information from GO Data
ChainGOidnamespacecontents
B0005768cellular_componentendosome
B0005886cellular_componentplasma membrane
B0006955biological_processimmune response
B0007165biological_processsignal transduction
B0007166biological_processcell surface receptor signaling pathway
B0009897cellular_componentexternal side of plasma membrane
B0016020cellular_componentmembrane
B0019863molecular_functionIgE binding
B0019901molecular_functionprotein kinase binding
B0032998cellular_componentFc-epsilon receptor I complex
B0042169molecular_functionSH2 domain binding
B0043306biological_processpositive regulation of mast cell degranulation
B0051219molecular_functionphosphoprotein binding
B0051279biological_processregulation of release of sequestered calcium ion into cytosol
C0004888molecular_functiontransmembrane signaling receptor activity
C0007166biological_processcell surface receptor signaling pathway
C0016020cellular_componentmembrane
C0019767molecular_functionIgE receptor activity
C0032998cellular_componentFc-epsilon receptor I complex
G0004888molecular_functiontransmembrane signaling receptor activity
G0007166biological_processcell surface receptor signaling pathway
G0016020cellular_componentmembrane
G0019767molecular_functionIgE receptor activity
G0032998cellular_componentFc-epsilon receptor I complex
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YQCRVDH
ChainResidueDetails
ETYR287-HIS293
EPHE394-HIS400

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 Residues75
DetailsDomain: {"description":"Ig-like 1"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues68
DetailsDomain: {"description":"Ig-like 2"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues7
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues45
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues196
DetailsDomain: {"description":"Ig-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues200
DetailsDomain: {"description":"Ig-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues200
DetailsDomain: {"description":"Ig-like 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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