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8AE2

Cryo-EM structure of full-length human immunoglobulin M - F(ab')2 conformation 5

Functional Information from GO Data
ChainGOidnamespacecontents
J0002250biological_processadaptive immune response
J0003094biological_processglomerular filtration
J0003697molecular_functionsingle-stranded DNA binding
J0003823molecular_functionantigen binding
J0005576cellular_componentextracellular region
J0005615cellular_componentextracellular space
J0006955biological_processimmune response
J0006959biological_processhumoral immune response
J0019731biological_processantibacterial humoral response
J0019862molecular_functionIgA binding
J0030674molecular_functionprotein-macromolecule adaptor activity
J0031210molecular_functionphosphatidylcholine binding
J0034987molecular_functionimmunoglobulin receptor binding
J0042803molecular_functionprotein homodimerization activity
J0042834molecular_functionpeptidoglycan binding
J0045087biological_processinnate immune response
J0060267biological_processpositive regulation of respiratory burst
J0065003biological_processprotein-containing complex assembly
J0070062cellular_componentextracellular exosome
J0071748cellular_componentmonomeric IgA immunoglobulin complex
J0071750cellular_componentdimeric IgA immunoglobulin complex
J0071751cellular_componentsecretory IgA immunoglobulin complex
J0071752cellular_componentsecretory dimeric IgA immunoglobulin complex
J0071756cellular_componentpentameric IgM immunoglobulin complex
J0071757cellular_componenthexameric IgM immunoglobulin complex
J0072562cellular_componentblood microparticle
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
ChainResidueDetails
LTYR193-HIS199
BTYR318-HIS324
CPHE318-HIS324
CPHE424-HIS430
CTYR534-HIS540

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues900
DetailsDomain: {"description":"Ig-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1010
DetailsDomain: {"description":"Ig-like 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"35981043","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4742735","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7XQ8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35981043","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4742735","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7XQ8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000167","evidences":[{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18780401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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