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8SKV

Structure of human SIgA1 in complex with Streptococcus pyogenes protein M4 (Arp4)

Functional Information from GO Data
ChainGOidnamespacecontents
a0005515molecular_functionprotein binding
a0005576cellular_componentextracellular region
b0005515molecular_functionprotein binding
b0005576cellular_componentextracellular region
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. FSCMVGH
ChainResidueDetails
APHE430-HIS436

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Pentaglycyl murein peptidoglycan amidated threonine => ECO:0000255|PROSITE-ProRule:PRU00477
ChainResidueDetails
aTHR315
DSER224
DSER238
DSER240
bTHR315
ASER240
BSER224
BSER238
BSER240
CSER224
CSER238
CSER240

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
JASN49
DTHR225
DTHR228
DTHR236
ATHR228
ATHR236
BTHR225
BTHR228
BTHR236
CTHR225
CTHR228
CTHR236

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:6526384
ChainResidueDetails
EASN117
ASER232
BSER230
BSER232
CSER230
CSER232
DSER230
DSER232

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
EASN168
EASN481
CTHR233
DTHR233

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
EASN403
BASN263
CASN263
DASN263

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
EASN451

222036

PDB entries from 2024-07-03

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