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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2ESG

Solution structure of the complex between immunoglobulin IgA1 and human serum albumin

Functional Information from GO Data
ChainGOidnamespacecontents
C0003677molecular_functionDNA binding
C0005504molecular_functionfatty acid binding
C0005507molecular_functioncopper ion binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005788cellular_componentendoplasmic reticulum lumen
C0006783biological_processheme biosynthetic process
C0008289molecular_functionlipid binding
C0009267biological_processcellular response to starvation
C0015643molecular_functiontoxic substance binding
C0015723biological_processbilirubin transport
C0016209molecular_functionantioxidant activity
C0019825molecular_functionoxygen binding
C0020037molecular_functionheme binding
C0030170molecular_functionpyridoxal phosphate binding
C0031093cellular_componentplatelet alpha granule lumen
C0031667biological_processresponse to nutrient levels
C0032991cellular_componentprotein-containing complex
C0034599biological_processcellular response to oxidative stress
C0042167biological_processheme catabolic process
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0051087molecular_functionprotein-folding chaperone binding
C0051902biological_processnegative regulation of mitochondrial depolarization
C0070062cellular_componentextracellular exosome
C0072562cellular_componentblood microparticle
C0072732biological_processcellular response to calcium ion starvation
C0098869biological_processcellular oxidant detoxification
C0140104molecular_functionmolecular carrier activity
C0140272molecular_functionexogenous protein binding
C1903981molecular_functionenterobactin binding
Functional Information from PROSITE/UniProt
site_idPS00212
Number of Residues25
DetailsALBUMIN_1 Albumin domain signature. YkaafteCCqaAdkaaCLlpkldeL
ChainResidueDetails
CTYR161-LEU185
CTYR353-PHE377
CPHE551-LEU575
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
ChainResidueDetails
LTYR192-HIS198
APHE433-HIS439
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues184
DetailsDomain: {"description":"Ig-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues190
DetailsDomain: {"description":"Ig-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues204
DetailsDomain: {"description":"Ig-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues52
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues36
DetailsCompositional bias: {"description":"Pro residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues6
DetailsGlycosylation: {"description":"O-linked (GalNAc...) serine","evidences":[{"source":"PubMed","id":"4373463","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues6
DetailsGlycosylation: {"description":"O-linked (GalNAc...) threonine","evidences":[{"source":"PubMed","id":"20823119","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31959827","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsGlycosylation: {"description":"O-linked (GalNAc...) serine","evidences":[{"source":"PubMed","id":"20823119","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31959827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4373463","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GalNAc...) threonine","evidences":[{"source":"PubMed","id":"31959827","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22171320","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues192
DetailsDomain: {"description":"Albumin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00769","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues197
DetailsDomain: {"description":"Albumin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00769","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P02769","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28567254","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IJF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"656055","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues36
DetailsSite: {"description":"Not glycated","evidences":[{"source":"PubMed","id":"15047055","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsSite: {"description":"Aspirin-acetylated lysine"}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18318008","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P07724","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07724","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"3759977","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues13
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"15047055","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"3759977","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6853480","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"15047055","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3759977","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; in variant Redhill","featureId":"CAR_000226"}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; in variant Casebrook","featureId":"CAR_000069"}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"15047055","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3759977","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6706980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6853480","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; alternate","evidences":[{"source":"PubMed","id":"3759977","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-12-24

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