Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3F8U

Tapasin/ERp57 heterodimer

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002250	biological_process	adaptive immune response
A	0002502	biological_process	peptide antigen assembly with MHC class I protein complex
A	0003723	molecular_function	RNA binding
A	0003756	molecular_function	protein disulfide isomerase activity
A	0004197	molecular_function	cysteine-type endopeptidase activity
A	0004629	molecular_function	phospholipase C activity
A	0005515	molecular_function	protein binding
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005783	cellular_component	endoplasmic reticulum
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0005925	cellular_component	focal adhesion
A	0006457	biological_process	protein folding
A	0009986	cellular_component	cell surface
A	0015035	molecular_function	protein-disulfide reductase activity
A	0015036	molecular_function	disulfide oxidoreductase activity
A	0016853	molecular_function	isomerase activity
A	0034975	biological_process	protein folding in endoplasmic reticulum
A	0034976	biological_process	response to endoplasmic reticulum stress
A	0042470	cellular_component	melanosome
A	0042802	molecular_function	identical protein binding
A	0042824	cellular_component	MHC class I peptide loading complex
A	0045335	cellular_component	phagocytic vesicle
A	0055038	cellular_component	recycling endosome membrane
A	0061779	cellular_component	Tapasin-ERp57 complex
A	0070062	cellular_component	extracellular exosome
A	0070527	biological_process	platelet aggregation
A	0097191	biological_process	extrinsic apoptotic signaling pathway
A	0098761	biological_process	cellular response to interleukin-7
A	2001238	biological_process	positive regulation of extrinsic apoptotic signaling pathway
B	0016020	cellular_component	membrane
B	0019885	biological_process	antigen processing and presentation of endogenous peptide antigen via MHC class I
C	0002250	biological_process	adaptive immune response
C	0002502	biological_process	peptide antigen assembly with MHC class I protein complex
C	0003723	molecular_function	RNA binding
C	0003756	molecular_function	protein disulfide isomerase activity
C	0004197	molecular_function	cysteine-type endopeptidase activity
C	0004629	molecular_function	phospholipase C activity
C	0005515	molecular_function	protein binding
C	0005615	cellular_component	extracellular space
C	0005634	cellular_component	nucleus
C	0005783	cellular_component	endoplasmic reticulum
C	0005788	cellular_component	endoplasmic reticulum lumen
C	0005925	cellular_component	focal adhesion
C	0006457	biological_process	protein folding
C	0009986	cellular_component	cell surface
C	0015035	molecular_function	protein-disulfide reductase activity
C	0015036	molecular_function	disulfide oxidoreductase activity
C	0016853	molecular_function	isomerase activity
C	0034975	biological_process	protein folding in endoplasmic reticulum
C	0034976	biological_process	response to endoplasmic reticulum stress
C	0042470	cellular_component	melanosome
C	0042802	molecular_function	identical protein binding
C	0042824	cellular_component	MHC class I peptide loading complex
C	0045335	cellular_component	phagocytic vesicle
C	0055038	cellular_component	recycling endosome membrane
C	0061779	cellular_component	Tapasin-ERp57 complex
C	0070062	cellular_component	extracellular exosome
C	0070527	biological_process	platelet aggregation
C	0097191	biological_process	extrinsic apoptotic signaling pathway
C	0098761	biological_process	cellular response to interleukin-7
C	2001238	biological_process	positive regulation of extrinsic apoptotic signaling pathway
D	0016020	cellular_component	membrane
D	0019885	biological_process	antigen processing and presentation of endogenous peptide antigen via MHC class I

Functional Information from PROSITE/UniProt

site_id	PS00194
Number of Residues	19
Details	THIOREDOXIN_1 Thioredoxin family active site. LIeFYapWCGHCKnLepkY

Chain	Residue	Details
A	LEU398-TYR416

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:19119025, ECO:0000269\|PubMed:19159218

Chain	Residue	Details
B	ASN233
D	ASN233
C	CYS57
C	ALA60

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Nucleophile => ECO:0000269\|PubMed:19119025, ECO:0000269\|PubMed:35948544, ECO:0007744\|PDB:3F8U, ECO:0007744\|PDB:7QPD

Chain	Residue	Details
A	CYS406
A	CYS409
C	CYS406
C	CYS409

site_id	SWS_FT_FI3
Number of Residues	8
Details	SITE: Contributes to redox potential value => ECO:0000250

Chain	Residue	Details
A	GLY58
A	HIS59
A	GLY407
A	HIS408
C	GLY58
C	HIS59
C	GLY407
C	HIS408

site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Lowers pKa of C-terminal Cys of first active site => ECO:0000250

Chain	Residue	Details
A	ARG119
C	ARG119

site_id	SWS_FT_FI5
Number of Residues	2
Details	SITE: Lowers pKa of C-terminal Cys of second active site => ECO:0000250

Chain	Residue	Details
A	ARG471
C	ARG471

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N6-methyllysine => ECO:0007744\|PubMed:24129315

Chain	Residue	Details
A	LYS61
C	LYS61

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:P27773

Chain	Residue	Details
A	LYS129
A	LYS218
C	LYS129
C	LYS218

site_id	SWS_FT_FI8
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P27773

Chain	Residue	Details
A	LYS152
A	LYS252
A	LYS362
A	LYS494
C	LYS152
C	LYS252
C	LYS362
C	LYS494

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	THR319
C	THR319

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1mek

Chain	Residue	Details
A	GLY58
A	ALA60
A	HIS59
A	CYS57

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1mek

Chain	Residue	Details
A	HIS408
A	CYS406
A	GLY407
A	CYS409

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1mek

Chain	Residue	Details
C	GLY58
C	ALA60
C	HIS59
C	CYS57

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1mek

Chain	Residue	Details
C	HIS408
C	CYS406
C	GLY407
C	CYS409

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1mek

Chain	Residue	Details
A	ALA60
A	CYS57

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1mek

Chain	Residue	Details
A	CYS406
A	CYS409

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1mek

Chain	Residue	Details
C	ALA60
C	CYS57

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1mek

Chain	Residue	Details
C	CYS406
C	CYS409

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)