Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3QFA

Crystal structure of the human thioredoxin reductase-thioredoxin complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
A	0016491	molecular_function	oxidoreductase activity
A	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A	0045454	biological_process	cell redox homeostasis
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
B	0016491	molecular_function	oxidoreductase activity
B	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B	0045454	biological_process	cell redox homeostasis
B	0050660	molecular_function	flavin adenine dinucleotide binding
C	0003723	molecular_function	RNA binding
C	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006351	biological_process	DNA-templated transcription
C	0009314	biological_process	response to radiation
C	0015035	molecular_function	protein-disulfide reductase activity
C	0019725	biological_process	cellular homeostasis
C	0042803	molecular_function	protein homodimerization activity
C	0043388	biological_process	positive regulation of DNA binding
C	0045454	biological_process	cell redox homeostasis
C	0047134	molecular_function	protein-disulfide reductase [NAD(P)H] activity
C	0051897	biological_process	positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
C	0055114	biological_process	obsolete oxidation-reduction process
C	0061692	biological_process	cellular detoxification of hydrogen peroxide
C	0070062	cellular_component	extracellular exosome
C	0071731	biological_process	response to nitric oxide
D	0003723	molecular_function	RNA binding
D	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006351	biological_process	DNA-templated transcription
D	0009314	biological_process	response to radiation
D	0015035	molecular_function	protein-disulfide reductase activity
D	0019725	biological_process	cellular homeostasis
D	0042803	molecular_function	protein homodimerization activity
D	0043388	biological_process	positive regulation of DNA binding
D	0045454	biological_process	cell redox homeostasis
D	0047134	molecular_function	protein-disulfide reductase [NAD(P)H] activity
D	0051897	biological_process	positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
D	0055114	biological_process	obsolete oxidation-reduction process
D	0061692	biological_process	cellular detoxification of hydrogen peroxide
D	0070062	cellular_component	extracellular exosome
D	0071731	biological_process	response to nitric oxide

Functional Information from PDB Data

site_id	AC1
Number of Residues	38
Details	BINDING SITE FOR RESIDUE FAD A 600

Chain	Residue
A	ILE18
A	CYS59
A	VAL62
A	GLY63
A	CYS64
A	LYS67
A	ALA130
A	TYR131
A	GLY132
A	ALA160
A	THR161
A	GLY19
A	GLY162
A	SER180
A	TYR200
A	VAL201
A	ARG293
A	ILE300
A	GLY333
A	ASP334
A	GLU341
A	LEU342
A	GLY21
A	THR343
A	PRO344
A	HOH504
A	HOH524
A	HOH549
A	HOH572
A	HOH585
A	HOH591
B	HIS472
A	SER22
A	GLY23
A	LEU41
A	ASP42
A	PHE43
A	THR58

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 801

Chain	Residue
A	ASP231
A	LYS235
A	TYR405
A	TYR422

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 802

Chain	Residue
A	GLU368
A	ASN369
A	GLY384
A	LEU385
A	HOH545
A	HOH690

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 804

Chain	Residue
A	GLN258
A	ASN428
A	LYS430
A	ASP431
A	ARG434
A	HOH578
A	HOH598

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 803

Chain	Residue
A	GLU387
A	ILE399
A	LYS486
A	ARG487

site_id	AC6
Number of Residues	38
Details	BINDING SITE FOR RESIDUE FAD B 600

Chain	Residue
A	HIS472
B	ILE18
B	GLY19
B	GLY21
B	SER22
B	GLY23
B	LEU41
B	ASP42
B	PHE43
B	GLY57
B	THR58
B	CYS59
B	VAL62
B	GLY63
B	CYS64
B	LYS67
B	TYR131
B	GLY132
B	ALA160
B	THR161
B	GLY162
B	TYR200
B	VAL201
B	ARG293
B	ILE300
B	GLY333
B	ASP334
B	GLU341
B	LEU342
B	THR343
B	PRO344
B	HOH509
B	HOH520
B	HOH521
B	HOH536
B	HOH542
B	HOH591
B	HOH602

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 804

Chain	Residue
B	ASN432
B	ARG434
B	LYS430
B	ASP431

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL D 803

Chain	Residue
D	ASP26
D	SER28
D	ALA29
D	THR30
D	SER35
D	LYS36
D	LYS39
D	GLU56

Functional Information from PROSITE/UniProt

site_id	PS00076
Number of Residues	11
Details	PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCIP

Chain	Residue	Details
A	GLY56-PRO66

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17512005","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2J3N","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PDB","id":"2J3N","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PDB","id":"2ZZ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZZB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QFA","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"O89049","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Non-standard residue: {"description":"Selenocysteine","evidences":[{"source":"PubMed","id":"8650234","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9JMH6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Cross-link: {"description":"Cysteinyl-selenocysteine (Cys-Sec)","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	206
Details	Domain: {"description":"Thioredoxin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9108029","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Site: {"description":"Deprotonates C-terminal active site Cys","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Site: {"description":"Contributes to redox potential value","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P10639","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	4
Details	Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"17260951","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	2
Details	Modified residue: {"description":"S-nitrosocysteine; alternate","evidences":[{"source":"PubMed","id":"16408020","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17606900","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P10639","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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