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9IIK

Cryo-EM structure of BTN2A1-BTN3A1-BTN3A2

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
C0001817biological_processregulation of cytokine production
C0002250biological_processadaptive immune response
C0002376biological_processimmune system process
C0002456biological_processT cell mediated immunity
C0005102molecular_functionsignaling receptor binding
C0005515molecular_functionprotein binding
C0005886cellular_componentplasma membrane
C0009897cellular_componentexternal side of plasma membrane
C0016020cellular_componentmembrane
C0032729biological_processpositive regulation of type II interferon production
C0050852biological_processT cell receptor signaling pathway
D0001817biological_processregulation of cytokine production
D0001819biological_processpositive regulation of cytokine production
D0002250biological_processadaptive immune response
D0002376biological_processimmune system process
D0005102molecular_functionsignaling receptor binding
D0005515molecular_functionprotein binding
D0005886cellular_componentplasma membrane
D0009897cellular_componentexternal side of plasma membrane
D0032729biological_processpositive regulation of type II interferon production
D0050798biological_processactivated T cell proliferation
D0050852biological_processT cell receptor signaling pathway
E0001817biological_processregulation of cytokine production
E0005102molecular_functionsignaling receptor binding
E0005886cellular_componentplasma membrane
E0006629biological_processlipid metabolic process
E0009897cellular_componentexternal side of plasma membrane
E0016020cellular_componentmembrane
E0050852biological_processT cell receptor signaling pathway
G0001817biological_processregulation of cytokine production
G0005102molecular_functionsignaling receptor binding
G0005886cellular_componentplasma membrane
G0006629biological_processlipid metabolic process
G0009897cellular_componentexternal side of plasma membrane
G0016020cellular_componentmembrane
G0050852biological_processT cell receptor signaling pathway
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues880
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues76
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues333
DetailsDomain: {"description":"Ig-like V-type"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues583
DetailsDomain: {"description":"B30.2/SPRY","evidences":[{"source":"PROSITE-ProRule","id":"PRU00548","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues305
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues47
DetailsCoiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues109
DetailsDomain: {"description":"Ig-like V-type 1"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues91
DetailsDomain: {"description":"Ig-like V-type 2"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22846996","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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