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	0019725	biological_process	cellular homeostasis
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
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	0019725	biological_process	cellular homeostasis
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
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	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	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

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
B	VAL24-PHE42
A	VAL24-PHE42

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9108029","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	3
Details	Site: {"description":"Deprotonates C-terminal active site Cys","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Site: {"description":"Contributes to redox potential value","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	3
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P10639","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"17260951","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	3
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_FI8
Number of Residues	3
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P10639","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	103
Details	Domain: {"description":"Thioredoxin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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)