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6KXS

Cryo-EM structure of human IgM-Fc in complex with the J chain and the ectodomain of pIgR

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. FTCRVDH
ChainResidueDetails
APHE318-HIS324
APHE424-HIS430
ATYR534-HIS540

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:6526384
ChainResidueDetails
PASN65
LASN332
BASN332
CASN332
DASN332
EASN332
FASN332
GASN332
HASN332
KASN332

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:6526384
ChainResidueDetails
PASN72
LASN395
BASN395
CASN395
DASN395
EASN395
FASN395
GASN395
HASN395
KASN395

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:6526384
ChainResidueDetails
PASN117
LASN402
BASN402
CASN402
DASN402
EASN402
FASN402
GASN402
HASN402
KASN402

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:6526384
ChainResidueDetails
PASN168
PASN481

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6526384
ChainResidueDetails
PASN403

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6526384
ChainResidueDetails
PASN451

222926

PDB entries from 2024-07-24

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