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7QNG

Structure of a MHC I-Tapasin-ERp57 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
B0003756molecular_functionprotein disulfide isomerase activity
D0000139cellular_componentGolgi membrane
D0001913biological_processT cell mediated cytotoxicity
D0001916biological_processpositive regulation of T cell mediated cytotoxicity
D0002237biological_processresponse to molecule of bacterial origin
D0002474biological_processantigen processing and presentation of peptide antigen via MHC class I
D0002481biological_processantigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent
D0002502biological_processpeptide antigen assembly with MHC class I protein complex
D0002503biological_processpeptide antigen assembly with MHC class II protein complex
D0002726biological_processpositive regulation of T cell cytokine production
D0005198molecular_functionstructural molecule activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005765cellular_componentlysosomal membrane
D0005783cellular_componentendoplasmic reticulum
D0005788cellular_componentendoplasmic reticulum lumen
D0005794cellular_componentGolgi apparatus
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0005925cellular_componentfocal adhesion
D0006826biological_processiron ion transport
D0006879biological_processintracellular iron ion homeostasis
D0006955biological_processimmune response
D0007608biological_processsensory perception of smell
D0007611biological_processlearning or memory
D0009897cellular_componentexternal side of plasma membrane
D0009986cellular_componentcell surface
D0010977biological_processnegative regulation of neuron projection development
D0012507cellular_componentER to Golgi transport vesicle membrane
D0016020cellular_componentmembrane
D0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
D0019886biological_processantigen processing and presentation of exogenous peptide antigen via MHC class II
D0023026molecular_functionMHC class II protein complex binding
D0030670cellular_componentphagocytic vesicle membrane
D0031901cellular_componentearly endosome membrane
D0031902cellular_componentlate endosome membrane
D0031905cellular_componentearly endosome lumen
D0032092biological_processpositive regulation of protein binding
D0033077biological_processT cell differentiation in thymus
D0034756biological_processregulation of iron ion transport
D0035580cellular_componentspecific granule lumen
D0042026biological_processprotein refolding
D0042605molecular_functionpeptide antigen binding
D0042612cellular_componentMHC class I protein complex
D0042613cellular_componentMHC class II protein complex
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
D0042824cellular_componentMHC class I peptide loading complex
D0045646biological_processregulation of erythrocyte differentiation
D0048260biological_processpositive regulation of receptor-mediated endocytosis
D0050680biological_processnegative regulation of epithelial cell proliferation
D0050768biological_processnegative regulation of neurogenesis
D0050778biological_processpositive regulation of immune response
D0050870biological_processpositive regulation of T cell activation
D0051289biological_processprotein homotetramerization
D0055038cellular_componentrecycling endosome membrane
D0060586biological_processmulticellular organismal-level iron ion homeostasis
D0070062cellular_componentextracellular exosome
D0071281biological_processcellular response to iron ion
D0071283biological_processcellular response to iron(III) ion
D0071316biological_processcellular response to nicotine
D1900121biological_processnegative regulation of receptor binding
D1900122biological_processpositive regulation of receptor binding
D1904434biological_processpositive regulation of ferrous iron binding
D1904437biological_processpositive regulation of transferrin receptor binding
D1904724cellular_componenttertiary granule lumen
D1990000biological_processamyloid fibril formation
D1990712cellular_componentHFE-transferrin receptor complex
D2000774biological_processpositive regulation of cellular senescence
D2000978biological_processnegative regulation of forebrain neuron differentiation
Functional Information from PROSITE/UniProt
site_idPS00194
Number of Residues19
DetailsTHIOREDOXIN_1 Thioredoxin family active site. LIeFYapWCGHCKnLepkY
ChainResidueDetails
BLEU374-TYR392

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACRVNH
ChainResidueDetails
CTYR257-HIS263
DTYR78-HIS84

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid; in form pI 5.3 => ECO:0000269|PubMed:7554280
ChainResidueDetails
DGLN2
BALA36

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis => ECO:0000269|PubMed:7918443
ChainResidueDetails
DILE1
BCYS385

site_idSWS_FT_FI3
Number of Residues6
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
ChainResidueDetails
DLYS19
DLYS41
DLYS48
DLYS58
DLYS91
DLYS94

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Lowers pKa of C-terminal Cys of first active site => ECO:0000250
ChainResidueDetails
BARG95

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Lowers pKa of C-terminal Cys of second active site => ECO:0000250
ChainResidueDetails
BARG447

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-methyllysine => ECO:0007744|PubMed:24129315
ChainResidueDetails
BLYS37

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P27773
ChainResidueDetails
BLYS105
BLYS194

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P27773
ChainResidueDetails
BLYS228
BLYS338
BLYS470
BLYS128

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BTHR295

219140

PDB entries from 2024-05-01

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