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4K71

Crystal structure of a high affinity Human Serum Albumin variant bound to the Neonatal Fc Receptor

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
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
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
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
C0032092biological_processpositive regulation of protein binding
C0033077biological_processT cell differentiation in thymus
C0034756biological_processregulation 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
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
C1900121biological_processnegative regulation of receptor binding
C1900122biological_processpositive regulation of receptor binding
C1904434biological_processpositive regulation of ferrous iron binding
C1904437biological_processpositive regulation of transferrin receptor binding
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
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
F0000139cellular_componentGolgi membrane
F0001913biological_processT cell mediated cytotoxicity
F0001916biological_processpositive regulation of T cell mediated cytotoxicity
F0002237biological_processresponse to molecule of bacterial origin
F0002474biological_processantigen processing and presentation of peptide antigen via MHC class I
F0002481biological_processantigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent
F0002502biological_processpeptide antigen assembly with MHC class I protein complex
F0002503biological_processpeptide antigen assembly with MHC class II protein complex
F0002726biological_processpositive regulation of T cell cytokine production
F0005198molecular_functionstructural molecule activity
F0005515molecular_functionprotein binding
F0005576cellular_componentextracellular region
F0005615cellular_componentextracellular space
F0005765cellular_componentlysosomal membrane
F0005783cellular_componentendoplasmic reticulum
F0005788cellular_componentendoplasmic reticulum lumen
F0005794cellular_componentGolgi apparatus
F0005829cellular_componentcytosol
F0005886cellular_componentplasma membrane
F0005925cellular_componentfocal adhesion
F0006826biological_processiron ion transport
F0006879biological_processintracellular iron ion homeostasis
F0006955biological_processimmune response
F0007608biological_processsensory perception of smell
F0007611biological_processlearning or memory
F0009897cellular_componentexternal side of plasma membrane
F0009986cellular_componentcell surface
F0010977biological_processnegative regulation of neuron projection development
F0012507cellular_componentER to Golgi transport vesicle membrane
F0016020cellular_componentmembrane
F0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
F0019886biological_processantigen processing and presentation of exogenous peptide antigen via MHC class II
F0023026molecular_functionMHC class II protein complex binding
F0030670cellular_componentphagocytic vesicle membrane
F0031901cellular_componentearly endosome membrane
F0031902cellular_componentlate endosome membrane
F0031905cellular_componentearly endosome lumen
F0032092biological_processpositive regulation of protein binding
F0033077biological_processT cell differentiation in thymus
F0034756biological_processregulation of iron ion transport
F0035580cellular_componentspecific granule lumen
F0042026biological_processprotein refolding
F0042605molecular_functionpeptide antigen binding
F0042612cellular_componentMHC class I protein complex
F0042613cellular_componentMHC class II protein complex
F0042802molecular_functionidentical protein binding
F0042803molecular_functionprotein homodimerization activity
F0042824cellular_componentMHC class I peptide loading complex
F0045646biological_processregulation of erythrocyte differentiation
F0048260biological_processpositive regulation of receptor-mediated endocytosis
F0050680biological_processnegative regulation of epithelial cell proliferation
F0050768biological_processnegative regulation of neurogenesis
F0050778biological_processpositive regulation of immune response
F0050870biological_processpositive regulation of T cell activation
F0051289biological_processprotein homotetramerization
F0055038cellular_componentrecycling endosome membrane
F0060586biological_processmulticellular organismal-level iron ion homeostasis
F0070062cellular_componentextracellular exosome
F0071281biological_processcellular response to iron ion
F0071283biological_processcellular response to iron(III) ion
F0071316biological_processcellular response to nicotine
F1900121biological_processnegative regulation of receptor binding
F1900122biological_processpositive regulation of receptor binding
F1904434biological_processpositive regulation of ferrous iron binding
F1904437biological_processpositive regulation of transferrin receptor binding
F1904724cellular_componenttertiary granule lumen
F1990000biological_processamyloid fibril formation
F1990712cellular_componentHFE-transferrin receptor complex
F2000774biological_processpositive regulation of cellular senescence
F2000978biological_processnegative regulation of forebrain neuron differentiation
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 601
ChainResidue
APRO282
ALEU283

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 602
ChainResidue
AHIS9
ALYS12
AGLU57

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 603
ChainResidue
AALA59
AGLU60
EARG214

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 604
ChainResidue
AHIS9
AARG10
AHIS3

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 605
ChainResidue
ATYR150
ALEU238
AHIS242
AARG257
AALA291
AHOH708

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 606
ChainResidue
APHE206
ALYS351
ASER480
ALEU481
AVAL482

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 607
ChainResidue
AHIS146
ASER193
AALA194
AGLN459
AHOH705

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 301
ChainResidue
BASN39
BARG42

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 302
ChainResidue
BSER181
BARG183

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 C 101
ChainResidue
CARG3
CTHR4

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 C 102
ChainResidue
CSER57
CLYS58

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 D 601
ChainResidue
BARG264
DASN44

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 602
ChainResidue
DPHE156
DLYS159
DARG160
DLYS281
DGLU285

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 603
ChainResidue
BARG214
DALA59
DGLU60

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 604
ChainResidue
DTYR150
DLEU238
DHIS242
DARG257
DALA291

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 605
ChainResidue
DPHE206
DLYS351
DSER480
DLEU481
DVAL482

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 606
ChainResidue
DLYS195
DLYS199
DTRP214
DARG218
DARG222

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 E 301
ChainResidue
ESER181
EARG183

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 F 101
ChainResidue
FLYS41
FPHE70
FTHR71
FTYR78

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. YCCIVQH
ChainResidueDetails
BTYR250-HIS256
CTYR78-HIS84

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280
ChainResidueDetails
CGLN2
FGLN2

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis => ECO:0000269|PubMed:7918443
ChainResidueDetails
CILE1
DGLU252
DASP255
DASP259
FILE1
AGLU244
AGLU252
AASP255
AASP259
DGLU6
DASP13
DGLU244

site_idSWS_FT_FI3
Number of Residues12
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
ChainResidueDetails
CLYS19
FLYS58
FLYS91
FLYS94
CLYS41
CLYS48
CLYS58
CLYS91
CLYS94
FLYS19
FLYS41
FLYS48

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:656055
ChainResidueDetails
ALYS240
DLYS240

site_idSWS_FT_FI5
Number of Residues74
DetailsSITE: Not glycated => ECO:0000269|PubMed:15047055
ChainResidueDetails
ALYS4
ALYS174
ALYS181
ALYS190
ALYS195
ALYS205
ALYS212
ALYS240
ALYS262
ALYS274
ALYS286
ALYS20
ALYS359
ALYS372
ALYS389
ALYS402
ALYS414
ALYS432
ALYS436
ALYS466
ALYS475
ALYS500
ALYS41
ALYS519
ALYS524
ALYS538
ALYS541
ALYS557
ALYS560
ALYS564
ALYS574
DLYS4
DLYS20
ALYS64
DLYS41
DLYS64
DLYS73
DLYS93
DLYS106
DLYS136
DLYS159
DLYS174
DLYS181
DLYS190
ALYS73
DLYS195
DLYS205
DLYS212
DLYS240
DLYS262
DLYS274
DLYS286
DLYS359
DLYS372
DLYS389
ALYS93
DLYS402
DLYS414
DLYS432
DLYS436
DLYS466
DLYS475
DLYS500
DLYS519
DLYS524
DLYS538
ALYS106
DLYS541
DLYS557
DLYS560
DLYS564
DLYS574
ALYS136
ALYS159

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Aspirin-acetylated lysine
ChainResidueDetails
ALYS199
DLYS199

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
ASER5
DSER5

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER58
DSER58

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER65
DSER65

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
ATHR83
DTHR83

site_idSWS_FT_FI11
Number of Residues8
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P07724
ChainResidueDetails
ALYS205
ALYS436
ALYS519
ALYS564
DLYS205
DLYS436
DLYS519
DLYS564

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07724
ChainResidueDetails
ASER273
DSER273

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ASER419
DSER419

site_idSWS_FT_FI14
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
AALA420
ATHR422
DALA420
DTHR422

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER489
DSER489

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
ChainResidueDetails
ALYS534
DLYS534

site_idSWS_FT_FI17
Number of Residues8
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977
ChainResidueDetails
ALYS12
ALYS281
ALYS317
ALYS439
DLYS12
DLYS281
DLYS317
DLYS439

site_idSWS_FT_FI18
Number of Residues26
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
ChainResidueDetails
ALYS51
ALYS444
ALYS536
ALYS545
ALYS573
DLYS51
DLYS137
DLYS162
DLYS225
DLYS276
DLYS313
ALYS137
DLYS323
DLYS378
DLYS413
DLYS444
DLYS536
DLYS545
DLYS573
ALYS162
ALYS225
ALYS276
ALYS313
ALYS323
ALYS378
ALYS413

site_idSWS_FT_FI19
Number of Residues2
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:3759977, ECO:0000269|PubMed:6853480
ChainResidueDetails
ALYS199
DLYS199

site_idSWS_FT_FI20
Number of Residues4
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977
ChainResidueDetails
ALYS233
ALYS351
DLYS233
DLYS351

site_idSWS_FT_FI21
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; in variant Redhill
ChainResidueDetails
AASN318
DASN318

site_idSWS_FT_FI22
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; in variant Casebrook
ChainResidueDetails
AASP494
DASP494

site_idSWS_FT_FI23
Number of Residues2
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977, ECO:0000269|PubMed:6706980, ECO:0000269|PubMed:6853480
ChainResidueDetails
ALYS525
DLYS525

site_idSWS_FT_FI24
Number of Residues2
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:3759977
ChainResidueDetails
ALYS534
DLYS534

225158

PDB entries from 2024-09-18

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