Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4KPR

Tetrameric form of rat selenoprotein thioredoxin reductase 1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001650	cellular_component	fibrillar center
A	0001707	biological_process	mesoderm formation
A	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0006979	biological_process	response to oxidative stress
A	0007369	biological_process	gastrulation
A	0008283	biological_process	cell population proliferation
A	0009410	biological_process	response to xenobiotic stimulus
A	0010269	biological_process	response to selenium ion
A	0016174	molecular_function	NAD(P)H oxidase H2O2-forming activity
A	0016259	biological_process	selenocysteine metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A	0033797	molecular_function	selenate reductase activity
A	0042537	biological_process	benzene-containing compound metabolic process
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0042802	molecular_function	identical protein binding
A	0043025	cellular_component	neuronal cell body
A	0043065	biological_process	positive regulation of apoptotic process
A	0045340	molecular_function	mercury ion binding
A	0045454	biological_process	cell redox homeostasis
A	0048678	biological_process	response to axon injury
A	0050137	molecular_function	NADPH peroxidase activity
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0055093	biological_process	response to hyperoxia
A	0070276	biological_process	halogen metabolic process
A	0071280	biological_process	cellular response to copper ion
A	0071455	biological_process	cellular response to hyperoxia
A	0071949	molecular_function	FAD binding
A	0098869	biological_process	cellular oxidant detoxification
B	0001650	cellular_component	fibrillar center
B	0001707	biological_process	mesoderm formation
B	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005829	cellular_component	cytosol
B	0006979	biological_process	response to oxidative stress
B	0007369	biological_process	gastrulation
B	0008283	biological_process	cell population proliferation
B	0009410	biological_process	response to xenobiotic stimulus
B	0010269	biological_process	response to selenium ion
B	0016174	molecular_function	NAD(P)H oxidase H2O2-forming activity
B	0016259	biological_process	selenocysteine metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B	0033797	molecular_function	selenate reductase activity
B	0042537	biological_process	benzene-containing compound metabolic process
B	0042744	biological_process	hydrogen peroxide catabolic process
B	0042802	molecular_function	identical protein binding
B	0043025	cellular_component	neuronal cell body
B	0043065	biological_process	positive regulation of apoptotic process
B	0045340	molecular_function	mercury ion binding
B	0045454	biological_process	cell redox homeostasis
B	0048678	biological_process	response to axon injury
B	0050137	molecular_function	NADPH peroxidase activity
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0055093	biological_process	response to hyperoxia
B	0070276	biological_process	halogen metabolic process
B	0071280	biological_process	cellular response to copper ion
B	0071455	biological_process	cellular response to hyperoxia
B	0071949	molecular_function	FAD binding
B	0098869	biological_process	cellular oxidant detoxification
E	0001650	cellular_component	fibrillar center
E	0001707	biological_process	mesoderm formation
E	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
E	0005634	cellular_component	nucleus
E	0005654	cellular_component	nucleoplasm
E	0005737	cellular_component	cytoplasm
E	0005739	cellular_component	mitochondrion
E	0005829	cellular_component	cytosol
E	0006979	biological_process	response to oxidative stress
E	0007369	biological_process	gastrulation
E	0008283	biological_process	cell population proliferation
E	0009410	biological_process	response to xenobiotic stimulus
E	0010269	biological_process	response to selenium ion
E	0016174	molecular_function	NAD(P)H oxidase H2O2-forming activity
E	0016259	biological_process	selenocysteine metabolic process
E	0016491	molecular_function	oxidoreductase activity
E	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
E	0033797	molecular_function	selenate reductase activity
E	0042537	biological_process	benzene-containing compound metabolic process
E	0042744	biological_process	hydrogen peroxide catabolic process
E	0042802	molecular_function	identical protein binding
E	0043025	cellular_component	neuronal cell body
E	0043065	biological_process	positive regulation of apoptotic process
E	0045340	molecular_function	mercury ion binding
E	0045454	biological_process	cell redox homeostasis
E	0048678	biological_process	response to axon injury
E	0050137	molecular_function	NADPH peroxidase activity
E	0050660	molecular_function	flavin adenine dinucleotide binding
E	0055093	biological_process	response to hyperoxia
E	0070276	biological_process	halogen metabolic process
E	0071280	biological_process	cellular response to copper ion
E	0071455	biological_process	cellular response to hyperoxia
E	0071949	molecular_function	FAD binding
E	0098869	biological_process	cellular oxidant detoxification
F	0001650	cellular_component	fibrillar center
F	0001707	biological_process	mesoderm formation
F	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
F	0005634	cellular_component	nucleus
F	0005654	cellular_component	nucleoplasm
F	0005737	cellular_component	cytoplasm
F	0005739	cellular_component	mitochondrion
F	0005829	cellular_component	cytosol
F	0006979	biological_process	response to oxidative stress
F	0007369	biological_process	gastrulation
F	0008283	biological_process	cell population proliferation
F	0009410	biological_process	response to xenobiotic stimulus
F	0010269	biological_process	response to selenium ion
F	0016174	molecular_function	NAD(P)H oxidase H2O2-forming activity
F	0016259	biological_process	selenocysteine metabolic process
F	0016491	molecular_function	oxidoreductase activity
F	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
F	0033797	molecular_function	selenate reductase activity
F	0042537	biological_process	benzene-containing compound metabolic process
F	0042744	biological_process	hydrogen peroxide catabolic process
F	0042802	molecular_function	identical protein binding
F	0043025	cellular_component	neuronal cell body
F	0043065	biological_process	positive regulation of apoptotic process
F	0045340	molecular_function	mercury ion binding
F	0045454	biological_process	cell redox homeostasis
F	0048678	biological_process	response to axon injury
F	0050137	molecular_function	NADPH peroxidase activity
F	0050660	molecular_function	flavin adenine dinucleotide binding
F	0055093	biological_process	response to hyperoxia
F	0070276	biological_process	halogen metabolic process
F	0071280	biological_process	cellular response to copper ion
F	0071455	biological_process	cellular response to hyperoxia
F	0071949	molecular_function	FAD binding
F	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO3 E 501

Chain	Residue
E	THR304
E	VAL305

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MPD E 502

Chain	Residue
E	LEU75
E	HOH740
E	HOH755
E	HOH768
E	HOH770
F	GLN72
F	LEU76

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MPD E 503

Chain	Residue
E	GLY237
E	ARG249

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD E 504

Chain	Residue
B	PRO317
E	PRO317
E	VAL318
E	THR319
E	ASN325

site_id	AC5
Number of Residues	38
Details	BINDING SITE FOR RESIDUE FAD E 505

Chain	Residue
E	ILE18
E	GLY19
E	GLY21
E	SER22
E	GLY23
E	LEU41
E	ASP42
E	PHE43
E	GLY57
E	THR58
E	CYS59
E	GLY63
E	CYS64
E	LYS67
E	ALA130
E	TYR131
E	GLY132
E	ALA160
E	THR161
E	GLY162
E	TYR200
E	ARG293
E	ILE300
E	GLY333
E	ASP334
E	GLU341
E	LEU342
E	THR343
E	PRO344
E	HOH617
E	HOH621
E	HOH622
E	HOH623
E	HOH647
E	HOH672
E	HOH696
E	HOH733
F	HIS472

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO3 F 501

Chain	Residue
F	PRO317

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO3 F 502

Chain	Residue
F	LYS192
F	GLU283
F	ASN285

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MPD F 503

Chain	Residue
F	ARG249

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MPD F 504

Chain	Residue
F	LEU49
F	THR51
F	PRO187
F	TYR188

site_id	BC1
Number of Residues	36
Details	BINDING SITE FOR RESIDUE FAD F 505

Chain	Residue
E	HIS472
F	ILE18
F	GLY19
F	GLY21
F	SER22
F	GLY23
F	LEU41
F	ASP42
F	PHE43
F	GLY57
F	THR58
F	CYS59
F	GLY63
F	CYS64
F	LYS67
F	ALA130
F	TYR131
F	GLY132
F	ALA160
F	THR161
F	GLY162
F	TYR200
F	ARG293
F	ILE300
F	GLY333
F	ASP334
F	GLU341
F	LEU342
F	THR343
F	PRO344
F	HOH602
F	HOH606
F	HOH607
F	HOH620
F	HOH644
F	HOH739

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MPD A 501

Chain	Residue
A	LEU76
B	GLN72
B	LEU76

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MPD A 502

Chain	Residue
A	GLY237
A	ARG249

site_id	BC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MPD A 503

Chain	Residue
A	PRO187

site_id	BC5
Number of Residues	32
Details	BINDING SITE FOR RESIDUE FAD A 504

Chain	Residue
A	ILE18
A	GLY19
A	GLY21
A	SER22
A	GLY23
A	LEU41
A	ASP42
A	PHE43
A	GLY57
A	THR58
A	CYS59
A	GLY63
A	CYS64
A	LYS67
A	ALA130
A	TYR131
A	GLY132
A	ALA160
A	THR161
A	GLY162
A	TYR200
A	VAL201
A	ARG293
A	ILE300
A	GLY333
A	ASP334
A	GLU341
A	LEU342
A	THR343
A	PRO344
A	HOH634
B	HIS472

site_id	BC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MPD B 501

Chain	Residue
B	GLY237
B	ARG249

site_id	BC7
Number of Residues	37
Details	BINDING SITE FOR RESIDUE FAD B 502

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	GLY63
B	CYS64
B	LYS67
B	ALA130
B	TYR131
B	GLY132
B	ALA160
B	THR161
B	GLY162
B	TYR200
B	ARG293
B	ILE300
B	GLY333
B	ASP334
B	GLU341
B	LEU342
B	THR343
B	PRO344
B	HOH603
B	HOH604
B	HOH606
B	HOH617
B	HOH636
B	HOH667
B	HOH677

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
E	GLY56-PRO66

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	112
Details	Binding site: {"evidences":[{"source":"PDB","id":"1H6V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q16881","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9JMH6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q16881","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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