8AE0

Cryo-EM structure of full-length human immunoglobulin M - F(ab')2 conformation 3

Functional Information from GO Data

Chain	GOid	namespace	contents
J	0002250	biological_process	adaptive immune response
J	0003094	biological_process	glomerular filtration
J	0003697	molecular_function	single-stranded DNA binding
J	0003823	molecular_function	antigen binding
J	0005576	cellular_component	extracellular region
J	0005615	cellular_component	extracellular space
J	0006955	biological_process	immune response
J	0006959	biological_process	humoral immune response
J	0019731	biological_process	antibacterial humoral response
J	0019862	molecular_function	IgA binding
J	0030674	molecular_function	protein-macromolecule adaptor activity
J	0031210	molecular_function	phosphatidylcholine binding
J	0034987	molecular_function	immunoglobulin receptor binding
J	0042803	molecular_function	protein homodimerization activity
J	0042834	molecular_function	peptidoglycan binding
J	0045087	biological_process	innate immune response
J	0060267	biological_process	positive regulation of respiratory burst
J	0065003	biological_process	protein-containing complex assembly
J	0070062	cellular_component	extracellular exosome
J	0071748	cellular_component	monomeric IgA immunoglobulin complex
J	0071750	cellular_component	dimeric IgA immunoglobulin complex
J	0071751	cellular_component	secretory IgA immunoglobulin complex
J	0071752	cellular_component	secretory dimeric IgA immunoglobulin complex
J	0071756	cellular_component	pentameric IgM immunoglobulin complex
J	0071757	cellular_component	hexameric IgM immunoglobulin complex
J	0072562	cellular_component	blood microparticle

Functional Information from PROSITE/UniProt

site_id	PS00290
Number of Residues	7
Details	IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCRVDH

Chain	Residue	Details
I	TYR318-HIS324
N	PHE318-HIS324
N	PHE424-HIS430
N	TYR534-HIS540
L	TYR193-HIS199

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	900
Details	Domain: {"description":"Ig-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1010
Details	Domain: {"description":"Ig-like 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	10
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	10
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

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