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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

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
D0002376biological_processimmune system process
D0002474biological_processantigen processing and presentation of peptide antigen via MHC class I
D0002477biological_processantigen processing and presentation of exogenous peptide antigen via MHC class Ib
D0002502biological_processpeptide antigen assembly with MHC class I protein complex
D0002503biological_processpeptide antigen assembly with MHC class II protein complex
D0002715biological_processregulation of natural killer cell mediated immunity
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
D0005886cellular_componentplasma membrane
D0005925cellular_componentfocal adhesion
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
D0010038biological_processresponse to metal ion
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
D0032398cellular_componentMHC class Ib protein complex
D0033572biological_processtransferrin transport
D0034756biological_processregulation of iron ion transport
D0034757biological_processnegative regulation of iron ion transport
D0035580cellular_componentspecific granule lumen
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
D0048260biological_processpositive regulation of receptor-mediated endocytosis
D0048261biological_processnegative 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
D0070062cellular_componentextracellular exosome
D0071281biological_processcellular response to iron ion
D0071316biological_processcellular response to nicotine
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
DTYR78-HIS84
CTYR257-HIS263
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19119025","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues142
DetailsDomain: {"description":"Thioredoxin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"11825568","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16193070","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19119025","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"19119025","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35948544","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3F8U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7QPD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Contributes to redox potential value","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Lowers pKa of C-terminal Cys of first active site","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Lowers pKa of C-terminal Cys of second active site","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P27773","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P27773","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues176
DetailsDomain: {"description":"Ig-like C1-type"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues91
DetailsRegion: {"description":"Alpha-2"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues91
DetailsRegion: {"description":"Alpha-3"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"3980466","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7118212","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"3980466","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
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_FI19
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_FI20
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"7918443","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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