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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6QIO

Ternary complex of FcRn ectodomain, FcRn binding optimised human serum albumin and the human growth hormone derivative somapacitan

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0005504molecular_functionfatty acid binding
A0005507molecular_functioncopper ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005788cellular_componentendoplasmic reticulum lumen
A0006783biological_processheme biosynthetic process
A0008289molecular_functionlipid binding
A0009267biological_processcellular response to starvation
A0015643molecular_functiontoxic substance binding
A0015723biological_processbilirubin transport
A0016209molecular_functionantioxidant activity
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0030170molecular_functionpyridoxal phosphate binding
A0031093cellular_componentplatelet alpha granule lumen
A0031667biological_processresponse to nutrient levels
A0032991cellular_componentprotein-containing complex
A0034599biological_processcellular response to oxidative stress
A0042167biological_processheme catabolic process
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051087molecular_functionprotein-folding chaperone binding
A0051902biological_processnegative regulation of mitochondrial depolarization
A0070062cellular_componentextracellular exosome
A0072562cellular_componentblood microparticle
A0072732biological_processcellular response to calcium ion starvation
A0098869biological_processcellular oxidant detoxification
A0140104molecular_functionmolecular carrier activity
A0140272molecular_functionexogenous protein binding
A1903981molecular_functionenterobactin binding
C0000139cellular_componentGolgi membrane
C0002376biological_processimmune system process
C0002474biological_processantigen processing and presentation of peptide antigen via MHC class I
C0002477biological_processantigen processing and presentation of exogenous peptide antigen via MHC class Ib
C0002502biological_processpeptide antigen assembly with MHC class I protein complex
C0002503biological_processpeptide antigen assembly with MHC class II protein complex
C0002715biological_processregulation of natural killer cell mediated immunity
C0002726biological_processpositive regulation of T cell cytokine production
C0005198molecular_functionstructural molecule activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005765cellular_componentlysosomal membrane
C0005783cellular_componentendoplasmic reticulum
C0005788cellular_componentendoplasmic reticulum lumen
C0005794cellular_componentGolgi apparatus
C0005886cellular_componentplasma membrane
C0005925cellular_componentfocal adhesion
C0006879biological_processintracellular iron ion homeostasis
C0006955biological_processimmune response
C0007608biological_processsensory perception of smell
C0007611biological_processlearning or memory
C0009897cellular_componentexternal side of plasma membrane
C0009986cellular_componentcell surface
C0010038biological_processresponse to metal ion
C0012507cellular_componentER to Golgi transport vesicle membrane
C0016020cellular_componentmembrane
C0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
C0019886biological_processantigen processing and presentation of exogenous peptide antigen via MHC class II
C0023026molecular_functionMHC class II protein complex binding
C0030670cellular_componentphagocytic vesicle membrane
C0031901cellular_componentearly endosome membrane
C0031902cellular_componentlate endosome membrane
C0031905cellular_componentearly endosome lumen
C0033572biological_processtransferrin transport
C0034756biological_processregulation of iron ion transport
C0034757biological_processnegative regulation of iron ion transport
C0035580cellular_componentspecific granule lumen
C0042605molecular_functionpeptide antigen binding
C0042612cellular_componentMHC class I protein complex
C0042613cellular_componentMHC class II protein complex
C0042802molecular_functionidentical protein binding
C0042803molecular_functionprotein homodimerization activity
C0042824cellular_componentMHC class I peptide loading complex
C0048260biological_processpositive regulation of receptor-mediated endocytosis
C0048261biological_processnegative regulation of receptor-mediated endocytosis
C0050680biological_processnegative regulation of epithelial cell proliferation
C0050768biological_processnegative regulation of neurogenesis
C0050778biological_processpositive regulation of immune response
C0050870biological_processpositive regulation of T cell activation
C0051289biological_processprotein homotetramerization
C0055038cellular_componentrecycling endosome membrane
C0070062cellular_componentextracellular exosome
C0071281biological_processcellular response to iron ion
C0071316biological_processcellular response to nicotine
C1904724cellular_componenttertiary granule lumen
C1990000biological_processamyloid fibril formation
C1990712cellular_componentHFE-transferrin receptor complex
C2000774biological_processpositive regulation of cellular senescence
C2000978biological_processnegative regulation of forebrain neuron differentiation
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue MES A 601
ChainResidue
ALEU387
AILE388
AASN391
ATYR411
AVAL433
AARG485
ASER489
site_idAC2
Number of Residues6
Detailsbinding site for residue CYS B 301
ChainResidue
BCYS48
CSER52
CASP53
CHOH211
BGLN34
BSER37
site_idAC3
Number of Residues15
Detailsbinding site for residue JG5 A 603
ChainResidue
APHE228
ASER232
AVAL325
ALEU347
AALA350
ALYS351
ASER480
ALEU481
BGLY222
BGLN223
BLEU240
BTHR241
BHOH449
AHOH727
AHOH814
Functional Information from PROSITE/UniProt
site_idPS00212
Number of Residues25
DetailsALBUMIN_1 Albumin domain signature. YkaafteCCqaAdkaaCLlpkldeL
ChainResidueDetails
ATYR161-LEU185
ATYR353-PHE377
APHE551-LEU575
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACRVNH
ChainResidueDetails
CTYR78-HIS84
BTYR250-HIS256
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues192
DetailsDomain: {"description":"Albumin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00769","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues197
DetailsDomain: {"description":"Albumin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00769","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P02770","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P02769","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28567254","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IJF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"656055","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues37
DetailsSite: {"description":"Not glycated","evidences":[{"source":"PubMed","id":"15047055","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsSite: {"description":"Aspirin-acetylated lysine"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
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_FI11
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_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P07724","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07724","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"3759977","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues13
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"15047055","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
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_FI22
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_FI23
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; in variant Redhill","featureId":"CAR_000226"}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; in variant Casebrook","featureId":"CAR_000069"}
ChainResidueDetails
site_idSWS_FT_FI25
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_FI26
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; alternate","evidences":[{"source":"PubMed","id":"3759977","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues87
DetailsDomain: {"description":"Ig-like C1-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues89
DetailsRegion: {"description":"Alpha-2","evidences":[{"source":"PubMed","id":"10933786","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EXU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues89
DetailsRegion: {"description":"Alpha-3","evidences":[{"source":"PubMed","id":"10933786","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EXU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues88
DetailsDomain: {"description":"Ig-like C1-type"}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues1
DetailsModified residue: {"description":"Pyrrolidone carboxylic acid; in form pI 5.3","evidences":[{"source":"PubMed","id":"7554280","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis","evidences":[{"source":"PubMed","id":"7918443","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"7918443","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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