Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2IFQ

Crystal structure of S-nitroso thioredoxin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0003723	molecular_function	RNA binding
A	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0009314	biological_process	response to radiation
A	0015035	molecular_function	protein-disulfide reductase activity
A	0042803	molecular_function	protein homodimerization activity
A	0043388	biological_process	positive regulation of DNA binding
A	0045454	biological_process	cell redox homeostasis
A	0046826	biological_process	negative regulation of protein export from nucleus
A	0047134	molecular_function	protein-disulfide reductase (NAD(P)H) activity
A	0051897	biological_process	positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
A	0055114	biological_process	obsolete oxidation-reduction process
A	0061692	biological_process	cellular detoxification of hydrogen peroxide
A	0070062	cellular_component	extracellular exosome
A	0071731	biological_process	response to nitric oxide
A	2000170	biological_process	positive regulation of peptidyl-cysteine S-nitrosylation
B	0000122	biological_process	negative regulation of transcription by RNA polymerase II
B	0003723	molecular_function	RNA binding
B	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0009314	biological_process	response to radiation
B	0015035	molecular_function	protein-disulfide reductase activity
B	0042803	molecular_function	protein homodimerization activity
B	0043388	biological_process	positive regulation of DNA binding
B	0045454	biological_process	cell redox homeostasis
B	0046826	biological_process	negative regulation of protein export from nucleus
B	0047134	molecular_function	protein-disulfide reductase (NAD(P)H) activity
B	0051897	biological_process	positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
B	0055114	biological_process	obsolete oxidation-reduction process
B	0061692	biological_process	cellular detoxification of hydrogen peroxide
B	0070062	cellular_component	extracellular exosome
B	0071731	biological_process	response to nitric oxide
B	2000170	biological_process	positive regulation of peptidyl-cysteine S-nitrosylation
C	0000122	biological_process	negative regulation of transcription by RNA polymerase II
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	0009314	biological_process	response to radiation
C	0015035	molecular_function	protein-disulfide reductase activity
C	0042803	molecular_function	protein homodimerization activity
C	0043388	biological_process	positive regulation of DNA binding
C	0045454	biological_process	cell redox homeostasis
C	0046826	biological_process	negative regulation of protein export from nucleus
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
C	2000170	biological_process	positive regulation of peptidyl-cysteine S-nitrosylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EOH C 106

Chain	Residue
C	GLN4
C	GLU6
C	ALA10
C	VAL86
C	GLY87
C	GLU103

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EOH C 107

Chain	Residue
C	GLY83
C	HOH110
C	HOH131
C	LEU15
C	PHE80
C	LYS82

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EOH C 108

Chain	Residue
B	PHE41
B	LYS94
C	GLU47
C	LYS48
C	LYS82

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EOH B 106

Chain	Residue
B	GLY33
C	THR9
C	GLN84
C	LYS85

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL24-PHE42
B	VAL24-PHE42

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000269\|PubMed:9108029

Chain	Residue	Details
B	GLY33
B	LYS36
C	GLY33
C	LYS36

site_id	SWS_FT_FI2
Number of Residues	1
Details	SITE: Deprotonates C-terminal active site Cys => ECO:0000305

Chain	Residue	Details
B	PHE27
C	PHE27

site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Contributes to redox potential value => ECO:0000305

Chain	Residue	Details
B	PRO34
B	CYS35
C	PRO34
C	CYS35

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
B	GLN4
B	PRO40
C	GLN4
C	PRO40

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:P10639

Chain	Residue	Details
B	THR9
C	THR9

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: S-nitrosocysteine => ECO:0000269\|PubMed:17260951

Chain	Residue	Details
B	GLN63
B	GLU70
C	GLN63
C	GLU70

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: S-nitrosocysteine; alternate => ECO:0000269\|PubMed:16408020, ECO:0000269\|PubMed:17606900

Chain	Residue	Details
B	MET74
C	MET74

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P10639

Chain	Residue	Details
B	GLU95
C	GLU95

Catalytic Information from CSA

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

Chain	Residue	Details
A	PRO34
A	CYS35
A	CYS32
A	GLY33

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

Chain	Residue	Details
C	PRO34
C	CYS35
C	CYS32
C	GLY33

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

Chain	Residue	Details
B	PRO34
B	CYS35
B	CYS32
B	GLY33

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1mek

Chain	Residue	Details
A	CYS35
A	CYS32

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

Chain	Residue	Details
C	CYS35
C	CYS32

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

Chain	Residue	Details
B	CYS35
B	CYS32

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