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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3F8U

Tapasin/ERp57 heterodimer

Functional Information from GO Data
ChainGOidnamespacecontents
A0002250biological_processadaptive immune response
A0002376biological_processimmune system process
A0002502biological_processpeptide antigen assembly with MHC class I protein complex
A0003723molecular_functionRNA binding
A0003756molecular_functionprotein disulfide isomerase activity
A0004197molecular_functioncysteine-type endopeptidase activity
A0004629molecular_functionphospholipase C activity
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0005925cellular_componentfocal adhesion
A0006457biological_processprotein folding
A0009986cellular_componentcell surface
A0015035molecular_functionprotein-disulfide reductase activity
A0015036molecular_functiondisulfide oxidoreductase activity
A0016853molecular_functionisomerase activity
A0034975biological_processprotein folding in endoplasmic reticulum
A0034976biological_processresponse to endoplasmic reticulum stress
A0042470cellular_componentmelanosome
A0042802molecular_functionidentical protein binding
A0042824cellular_componentMHC class I peptide loading complex
A0044183molecular_functionprotein folding chaperone
A0045335cellular_componentphagocytic vesicle
A0055038cellular_componentrecycling endosome membrane
A0061779cellular_componentTapasin-ERp57 complex
A0070062cellular_componentextracellular exosome
A0106222molecular_functionlncRNA binding
B0016020cellular_componentmembrane
B0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
C0002250biological_processadaptive immune response
C0002376biological_processimmune system process
C0002502biological_processpeptide antigen assembly with MHC class I protein complex
C0003723molecular_functionRNA binding
C0003756molecular_functionprotein disulfide isomerase activity
C0004197molecular_functioncysteine-type endopeptidase activity
C0004629molecular_functionphospholipase C activity
C0005515molecular_functionprotein binding
C0005615cellular_componentextracellular space
C0005634cellular_componentnucleus
C0005783cellular_componentendoplasmic reticulum
C0005788cellular_componentendoplasmic reticulum lumen
C0005925cellular_componentfocal adhesion
C0006457biological_processprotein folding
C0009986cellular_componentcell surface
C0015035molecular_functionprotein-disulfide reductase activity
C0015036molecular_functiondisulfide oxidoreductase activity
C0016853molecular_functionisomerase activity
C0034975biological_processprotein folding in endoplasmic reticulum
C0034976biological_processresponse to endoplasmic reticulum stress
C0042470cellular_componentmelanosome
C0042802molecular_functionidentical protein binding
C0042824cellular_componentMHC class I peptide loading complex
C0044183molecular_functionprotein folding chaperone
C0045335cellular_componentphagocytic vesicle
C0055038cellular_componentrecycling endosome membrane
C0061779cellular_componentTapasin-ERp57 complex
C0070062cellular_componentextracellular exosome
C0106222molecular_functionlncRNA binding
D0016020cellular_componentmembrane
D0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
Functional Information from PROSITE/UniProt
site_idPS00194
Number of Residues19
DetailsTHIOREDOXIN_1 Thioredoxin family active site. LIeFYapWCGHCKnLepkY
ChainResidueDetails
ALEU398-TYR416
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues108
DetailsDomain: {"description":"Thioredoxin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues284
DetailsDomain: {"description":"Thioredoxin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
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 Residues4
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 Residues8
DetailsSite: {"description":"Contributes to redox potential value","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Lowers pKa of C-terminal Cys of first active site","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Lowers pKa of C-terminal Cys of second active site","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P27773","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P27773","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues107
DetailsDomain: {"description":"Ig-like C1-type"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19119025","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
AGLY58
AALA60
AHIS59
ACYS57
site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
AHIS408
ACYS406
AGLY407
ACYS409
site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
CGLY58
CALA60
CHIS59
CCYS57
site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
CHIS408
CCYS406
CGLY407
CCYS409
site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
AALA60
ACYS57
site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
ACYS406
ACYS409
site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
CALA60
CCYS57
site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
CCYS406
CCYS409

246031

PDB entries from 2025-12-10

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