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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6QIP

Ternary complex of FcRn ectodomain, FcRn binding optimised human serum albumin and the albumin-biniding side chain of 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
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0005794cellular_componentGolgi apparatus
A0008289molecular_functionlipid binding
A0009267biological_processcellular response to starvation
A0015643molecular_functiontoxic substance binding
A0016209molecular_functionantioxidant activity
A0019825molecular_functionoxygen binding
A0030170molecular_functionpyridoxal phosphate binding
A0031093cellular_componentplatelet alpha granule lumen
A0031667biological_processresponse to nutrient levels
A0032991cellular_componentprotein-containing complex
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
A0140272molecular_functionexogenous protein binding
A1903981molecular_functionenterobactin binding
C0000139cellular_componentGolgi membrane
C0001913biological_processT cell mediated cytotoxicity
C0001916biological_processpositive regulation of T cell mediated cytotoxicity
C0002237biological_processresponse to molecule of bacterial origin
C0002376biological_processimmune system process
C0002474biological_processantigen processing and presentation of peptide antigen via MHC class I
C0002481biological_processantigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent
C0002502biological_processpeptide antigen assembly with MHC class I protein complex
C0002503biological_processpeptide antigen assembly with MHC class II protein complex
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
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0005925cellular_componentfocal adhesion
C0006826biological_processiron ion transport
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
C0010977biological_processnegative regulation of neuron projection development
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
C0033077biological_processT cell differentiation in thymus
C0033572biological_processtransferrin transport
C0034756biological_processregulation of iron ion transport
C0034757biological_processnegative regulation of iron ion transport
C0035580cellular_componentspecific granule lumen
C0042026biological_processprotein refolding
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
C0045646biological_processregulation of erythrocyte differentiation
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
C0060586biological_processmulticellular organismal-level iron ion homeostasis
C0070062cellular_componentextracellular exosome
C0071281biological_processcellular response to iron ion
C0071283biological_processcellular response to iron(III) 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 Residues6
Detailsbinding site for residue MES A 601
ChainResidue
AASN391
ALEU407
AARG410
ATYR411
ALEU453
ASER489
site_idAC3
Number of Residues4
Detailsbinding site for residue CYS B 301
ChainResidue
CASP53
BGLN34
BSER37
BCYS48
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 Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P02769","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28567254","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IJF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"656055","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues37
DetailsSite: {"description":"Not glycated","evidences":[{"source":"PubMed","id":"15047055","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Aspirin-acetylated lysine"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
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_FI10
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_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P07724","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07724","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"3759977","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues13
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"15047055","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
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_FI21
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_FI22
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; in variant Redhill","featureId":"CAR_000226"}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; in variant Casebrook","featureId":"CAR_000069"}
ChainResidueDetails
site_idSWS_FT_FI24
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_FI25
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; alternate","evidences":[{"source":"PubMed","id":"3759977","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues87
DetailsDomain: {"description":"Ig-like C1-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI27
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_FI28
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_FI29
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues88
DetailsDomain: {"description":"Ig-like C1-type"}
ChainResidueDetails
site_idSWS_FT_FI31
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_FI32
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_FI33
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"7918443","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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