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4N0U

Ternary complex between Neonatal Fc receptor, serum albumin and Fc

Functional Information from GO Data
ChainGOidnamespacecontents
B0000139cellular_componentGolgi membrane
B0001913biological_processT cell mediated cytotoxicity
B0001916biological_processpositive regulation of T cell mediated cytotoxicity
B0002237biological_processresponse to molecule of bacterial origin
B0002474biological_processantigen processing and presentation of peptide antigen via MHC class I
B0002481biological_processantigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent
B0002502biological_processpeptide antigen assembly with MHC class I protein complex
B0002503biological_processpeptide antigen assembly with MHC class II protein complex
B0002726biological_processpositive regulation of T cell cytokine production
B0005198molecular_functionstructural molecule activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005765cellular_componentlysosomal membrane
B0005783cellular_componentendoplasmic reticulum
B0005788cellular_componentendoplasmic reticulum lumen
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005925cellular_componentfocal adhesion
B0006826biological_processiron ion transport
B0006879biological_processintracellular iron ion homeostasis
B0006955biological_processimmune response
B0007608biological_processsensory perception of smell
B0007611biological_processlearning or memory
B0009897cellular_componentexternal side of plasma membrane
B0009986cellular_componentcell surface
B0010977biological_processnegative regulation of neuron projection development
B0012507cellular_componentER to Golgi transport vesicle membrane
B0016020cellular_componentmembrane
B0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
B0019886biological_processantigen processing and presentation of exogenous peptide antigen via MHC class II
B0023026molecular_functionMHC class II protein complex binding
B0030670cellular_componentphagocytic vesicle membrane
B0031901cellular_componentearly endosome membrane
B0031902cellular_componentlate endosome membrane
B0031905cellular_componentearly endosome lumen
B0032092biological_processpositive regulation of protein binding
B0033077biological_processT cell differentiation in thymus
B0034756biological_processregulation of iron ion transport
B0035580cellular_componentspecific granule lumen
B0042026biological_processprotein refolding
B0042605molecular_functionpeptide antigen binding
B0042612cellular_componentMHC class I protein complex
B0042613cellular_componentMHC class II protein complex
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0042824cellular_componentMHC class I peptide loading complex
B0045646biological_processregulation of erythrocyte differentiation
B0048260biological_processpositive regulation of receptor-mediated endocytosis
B0050680biological_processnegative regulation of epithelial cell proliferation
B0050768biological_processnegative regulation of neurogenesis
B0050778biological_processpositive regulation of immune response
B0050870biological_processpositive regulation of T cell activation
B0051289biological_processprotein homotetramerization
B0055038cellular_componentrecycling endosome membrane
B0060586biological_processmulticellular organismal-level iron ion homeostasis
B0070062cellular_componentextracellular exosome
B0071281biological_processcellular response to iron ion
B0071283biological_processcellular response to iron(III) ion
B0071316biological_processcellular response to nicotine
B1900121biological_processnegative regulation of receptor binding
B1900122biological_processpositive regulation of receptor binding
B1904434biological_processpositive regulation of ferrous iron binding
B1904437biological_processpositive regulation of transferrin receptor binding
B1904724cellular_componenttertiary granule lumen
B1990000biological_processamyloid fibril formation
B1990712cellular_componentHFE-transferrin receptor complex
B2000774biological_processpositive regulation of cellular senescence
B2000978biological_processnegative regulation of forebrain neuron differentiation
D0003677molecular_functionDNA binding
D0005504molecular_functionfatty acid binding
D0005507molecular_functioncopper ion binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005783cellular_componentendoplasmic reticulum
D0005788cellular_componentendoplasmic reticulum lumen
D0005794cellular_componentGolgi apparatus
D0008289molecular_functionlipid binding
D0009267biological_processcellular response to starvation
D0015643molecular_functiontoxic substance binding
D0016209molecular_functionantioxidant activity
D0019825molecular_functionoxygen binding
D0030170molecular_functionpyridoxal phosphate binding
D0031093cellular_componentplatelet alpha granule lumen
D0032991cellular_componentprotein-containing complex
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D0051087molecular_functionprotein-folding chaperone binding
D0051902biological_processnegative regulation of mitochondrial depolarization
D0070062cellular_componentextracellular exosome
D0072562cellular_componentblood microparticle
D0072732biological_processcellular response to calcium ion starvation
D0098869biological_processcellular oxidant detoxification
D0140272molecular_functionexogenous protein binding
D1903981molecular_functionenterobactin binding
Functional Information from PROSITE/UniProt
site_idPS00212
Number of Residues25
DetailsALBUMIN_1 Albumin domain signature. YkaafteCCqaAdkaaCLlpkldeL
ChainResidueDetails
DTYR161-LEU185
DTYR353-PHE377
DPHE551-LEU575

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YCCIVQH
ChainResidueDetails
ATYR250-HIS256
EPHE423-HIS429
BTYR78-HIS84

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:11406581, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19358553, ECO:0000269|PubMed:20357243
ChainResidueDetails
EASN297

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P02769
ChainResidueDetails
DGLU6
DASP13
DGLU244
DGLU252
DASP255
DASP259

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:28567254, ECO:0007744|PDB:5IJF
ChainResidueDetails
DHIS67
DHIS247
DASP249
BLYS58
BLYS91
BLYS94

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:656055
ChainResidueDetails
DLYS240

site_idSWS_FT_FI5
Number of Residues37
DetailsSITE: Not glycated => ECO:0000269|PubMed:15047055
ChainResidueDetails
DLYS4
DLYS174
DLYS181
DLYS190
DLYS195
DLYS205
DLYS212
DLYS240
DLYS262
DLYS274
DLYS286
DLYS20
DLYS359
DLYS372
DLYS389
DLYS402
DLYS414
DLYS432
DLYS436
DLYS466
DLYS475
DLYS500
DLYS41
DLYS519
DLYS524
DLYS538
DLYS541
DLYS557
DLYS560
DLYS564
DLYS574
DLYS64
DLYS73
DLYS93
DLYS106
DLYS136
DLYS159

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Aspirin-acetylated lysine
ChainResidueDetails
DLYS199

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
DSER5

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:24275569
ChainResidueDetails
DSER58

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:24275569
ChainResidueDetails
DSER65

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
DTHR83

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P07724
ChainResidueDetails
DLYS205
DLYS436
DLYS519
DLYS564

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07724
ChainResidueDetails
DSER273

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
DSER419

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
DTHR420
DTHR422

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
DSER489

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
ChainResidueDetails
DLYS534

site_idSWS_FT_FI17
Number of Residues4
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977
ChainResidueDetails
DLYS12
DLYS281
DLYS317
DLYS439

site_idSWS_FT_FI18
Number of Residues13
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
ChainResidueDetails
DLYS51
DLYS444
DLYS536
DLYS545
DLYS573
DLYS137
DLYS162
DLYS225
DLYS276
DLYS313
DLYS323
DLYS378
DLYS413

site_idSWS_FT_FI19
Number of Residues1
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:3759977, ECO:0000269|PubMed:6853480
ChainResidueDetails
DLYS199

site_idSWS_FT_FI20
Number of Residues2
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977
ChainResidueDetails
DLYS233
DLYS351

site_idSWS_FT_FI21
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; in variant Redhill
ChainResidueDetails
DASN318

site_idSWS_FT_FI22
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; in variant Casebrook
ChainResidueDetails
DASP494

site_idSWS_FT_FI23
Number of Residues1
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977, ECO:0000269|PubMed:6706980, ECO:0000269|PubMed:6853480
ChainResidueDetails
DLYS525

site_idSWS_FT_FI24
Number of Residues1
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:3759977
ChainResidueDetails
DLYS534

227111

PDB entries from 2024-11-06

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