8AE2
Cryo-EM structure of full-length human immunoglobulin M - F(ab')2 conformation 5
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. YACEVTH |
Chain | Residue | Details |
L | TYR193-HIS199 | |
B | TYR318-HIS324 | |
C | PHE318-HIS324 | |
C | PHE424-HIS430 | |
C | TYR534-HIS540 |
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 |
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 |
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 |
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 |
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 |