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7K0C

Structure of Secretory IgM Core

Functional Information from GO Data
ChainGOidnamespacecontents
D0002250biological_processadaptive immune response
D0003094biological_processglomerular filtration
D0003697molecular_functionsingle-stranded DNA binding
D0003823molecular_functionantigen binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0006955biological_processimmune response
D0006959biological_processhumoral immune response
D0019731biological_processantibacterial humoral response
D0019862molecular_functionIgA binding
D0030674molecular_functionprotein-macromolecule adaptor activity
D0031210molecular_functionphosphatidylcholine binding
D0034987molecular_functionimmunoglobulin receptor binding
D0042803molecular_functionprotein homodimerization activity
D0042834molecular_functionpeptidoglycan binding
D0045087biological_processinnate immune response
D0060267biological_processpositive regulation of respiratory burst
D0065003biological_processprotein-containing complex assembly
D0070062cellular_componentextracellular exosome
D0071748cellular_componentmonomeric IgA immunoglobulin complex
D0071750cellular_componentdimeric IgA immunoglobulin complex
D0071751cellular_componentsecretory IgA immunoglobulin complex
D0071752cellular_componentsecretory dimeric IgA immunoglobulin complex
D0071756cellular_componentpentameric IgM immunoglobulin complex
D0071757cellular_componenthexameric IgM immunoglobulin complex
D0072562cellular_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
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:25946035, ECO:0000269|PubMed:407930
ChainResidueDetails
DGLN1
FASN332
BASN332
KASN332
LASN332
IASN332
JASN332
EASN332
HASN332
GASN332

site_idSWS_FT_FI2
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
ChainResidueDetails
DASN49
FASN395
BASN395
KASN395
LASN395
IASN395
JASN395
EASN395
HASN395
GASN395

site_idSWS_FT_FI3
Number of Residues10
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:35981043, ECO:0000269|PubMed:4742735, ECO:0007744|PDB:7XQ8
ChainResidueDetails
AASN402
FASN402
BASN402
KASN402
LASN402
IASN402
JASN402
EASN402
HASN402
GASN402

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
CASN168
CASN481

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
CASN403

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
CASN451

226707

PDB entries from 2024-10-30

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