Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3EAO

Crystal structure of recombinant rat selenoprotein thioredoxin reductase 1 with oxidized C-terminal tail

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001707	biological_process	mesoderm formation
A	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
A	0005634	cellular_component	nucleus
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	0070995	biological_process	NADPH oxidation
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	0001707	biological_process	mesoderm formation
B	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
B	0005634	cellular_component	nucleus
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	0070995	biological_process	NADPH oxidation
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
C	0001707	biological_process	mesoderm formation
C	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005829	cellular_component	cytosol
C	0006979	biological_process	response to oxidative stress
C	0007369	biological_process	gastrulation
C	0008283	biological_process	cell population proliferation
C	0009410	biological_process	response to xenobiotic stimulus
C	0010269	biological_process	response to selenium ion
C	0016174	molecular_function	NAD(P)H oxidase H2O2-forming activity
C	0016259	biological_process	selenocysteine metabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
C	0033797	molecular_function	selenate reductase activity
C	0042537	biological_process	benzene-containing compound metabolic process
C	0042744	biological_process	hydrogen peroxide catabolic process
C	0042802	molecular_function	identical protein binding
C	0043025	cellular_component	neuronal cell body
C	0043065	biological_process	positive regulation of apoptotic process
C	0045340	molecular_function	mercury ion binding
C	0045454	biological_process	cell redox homeostasis
C	0048678	biological_process	response to axon injury
C	0050137	molecular_function	NADPH peroxidase activity
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	0055093	biological_process	response to hyperoxia
C	0070276	biological_process	halogen metabolic process
C	0070995	biological_process	NADPH oxidation
C	0071280	biological_process	cellular response to copper ion
C	0071455	biological_process	cellular response to hyperoxia
C	0071949	molecular_function	FAD binding
C	0098869	biological_process	cellular oxidant detoxification
D	0001707	biological_process	mesoderm formation
D	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005829	cellular_component	cytosol
D	0006979	biological_process	response to oxidative stress
D	0007369	biological_process	gastrulation
D	0008283	biological_process	cell population proliferation
D	0009410	biological_process	response to xenobiotic stimulus
D	0010269	biological_process	response to selenium ion
D	0016174	molecular_function	NAD(P)H oxidase H2O2-forming activity
D	0016259	biological_process	selenocysteine metabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
D	0033797	molecular_function	selenate reductase activity
D	0042537	biological_process	benzene-containing compound metabolic process
D	0042744	biological_process	hydrogen peroxide catabolic process
D	0042802	molecular_function	identical protein binding
D	0043025	cellular_component	neuronal cell body
D	0043065	biological_process	positive regulation of apoptotic process
D	0045340	molecular_function	mercury ion binding
D	0045454	biological_process	cell redox homeostasis
D	0048678	biological_process	response to axon injury
D	0050137	molecular_function	NADPH peroxidase activity
D	0050660	molecular_function	flavin adenine dinucleotide binding
D	0055093	biological_process	response to hyperoxia
D	0070276	biological_process	halogen metabolic process
D	0070995	biological_process	NADPH oxidation
D	0071280	biological_process	cellular response to copper ion
D	0071455	biological_process	cellular response to hyperoxia
D	0071949	molecular_function	FAD binding
D	0098869	biological_process	cellular oxidant detoxification
E	0001707	biological_process	mesoderm formation
E	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
E	0005634	cellular_component	nucleus
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	0070995	biological_process	NADPH oxidation
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	0001707	biological_process	mesoderm formation
F	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
F	0005634	cellular_component	nucleus
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	0070995	biological_process	NADPH oxidation
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	31
Details	BINDING SITE FOR RESIDUE FAD A 600

Chain	Residue
A	GLY19
A	THR58
A	CYS59
A	VAL62
A	GLY63
A	CYS64
A	LYS67
A	ALA130
A	TYR131
A	GLY132
A	ALA160
A	GLY20
A	THR161
A	GLY162
A	ARG293
A	ILE300
A	GLY333
A	ASP334
A	GLU341
A	LEU342
A	THR343
A	PRO344
A	GLY21
A	PHE375
B	HIS472
A	SER22
A	GLY23
A	LEU41
A	ASP42
A	PHE43
A	GLY57

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE NAP A 601

Chain	Residue
A	LEU168
A	ALA198
A	SER199
A	TYR200
A	VAL201
A	ARG221
A	SER222
A	ARG226
A	VAL252
A	ALA290
A	VAL291
A	GLY292
A	ARG293

site_id	AC3
Number of Residues	33
Details	BINDING SITE FOR RESIDUE FAD B 600

Chain	Residue
A	HIS472
B	ILE18
B	GLY19
B	GLY20
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	ALA130
B	TYR131
B	GLY132
B	ALA160
B	THR161
B	GLY162
B	SER180
B	ARG293
B	ILE300
B	GLY333
B	ASP334
B	GLU341
B	LEU342
B	THR343
B	PRO344
B	PHE375

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE NAP B 601

Chain	Residue
B	LEU168
B	ALA198
B	SER199
B	TYR200
B	VAL201
B	ARG221
B	SER222
B	ARG226
B	VAL252
B	VAL291
B	GLY292
B	ARG293

site_id	AC5
Number of Residues	32
Details	BINDING SITE FOR RESIDUE FAD C 600

Chain	Residue
C	THR58
C	CYS59
C	VAL62
C	GLY63
C	CYS64
C	LYS67
C	ALA130
C	TYR131
C	GLY132
C	ALA160
C	THR161
C	GLY162
C	ARG293
C	ILE300
C	GLY333
C	ASP334
C	GLU341
C	LEU342
C	THR343
C	PRO344
C	PHE375
D	HIS472
C	ILE18
C	GLY19
C	GLY20
C	GLY21
C	SER22
C	GLY23
C	LEU41
C	ASP42
C	PHE43
C	GLY57

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE NAP C 601

Chain	Residue
C	LEU168
C	ALA198
C	SER199
C	TYR200
C	VAL201
C	ARG221
C	SER222
C	ARG226
C	VAL252
C	ALA290
C	VAL291
C	GLY292
C	ARG293

site_id	AC7
Number of Residues	30
Details	BINDING SITE FOR RESIDUE FAD D 600

Chain	Residue
C	HIS472
D	GLY19
D	GLY20
D	GLY21
D	SER22
D	GLY23
D	LEU41
D	ASP42
D	PHE43
D	GLY57
D	THR58
D	CYS59
D	VAL62
D	GLY63
D	CYS64
D	LYS67
D	ALA130
D	TYR131
D	GLY132
D	ALA160
D	THR161
D	GLY162
D	ARG293
D	ILE300
D	GLY333
D	ASP334
D	GLU341
D	LEU342
D	THR343
D	PRO344

site_id	AC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE NAP D 601

Chain	Residue
D	LEU168
D	ALA198
D	SER199
D	TYR200
D	VAL201
D	ARG221
D	SER222
D	ARG226
D	VAL252
D	ALA290
D	VAL291
D	GLY292
D	ARG293

site_id	AC9
Number of Residues	31
Details	BINDING SITE FOR RESIDUE FAD E 600

Chain	Residue
E	GLY19
E	GLY20
E	GLY21
E	SER22
E	GLY23
E	LEU41
E	ASP42
E	PHE43
E	GLY57
E	THR58
E	CYS59
E	VAL62
E	GLY63
E	CYS64
E	LYS67
E	ALA130
E	TYR131
E	GLY132
E	ALA160
E	THR161
E	GLY162
E	ARG293
E	ILE300
E	GLY333
E	ASP334
E	GLU341
E	LEU342
E	THR343
E	PRO344
E	PHE375
F	HIS472

site_id	BC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE NAP E 601

Chain	Residue
E	LEU168
E	ALA198
E	SER199
E	TYR200
E	VAL201
E	ARG221
E	SER222
E	ARG226
E	VAL252
E	ALA290
E	VAL291
E	GLY292
E	ARG293

site_id	BC2
Number of Residues	34
Details	BINDING SITE FOR RESIDUE FAD F 600

Chain	Residue
E	HIS472
F	ILE18
F	GLY19
F	GLY20
F	GLY21
F	SER22
F	GLY23
F	GLY24
F	LEU41
F	ASP42
F	PHE43
F	GLY57
F	THR58
F	CYS59
F	VAL62
F	GLY63
F	CYS64
F	LYS67
F	ALA130
F	TYR131
F	GLY132
F	ALA160
F	THR161
F	GLY162
F	VAL201
F	ARG293
F	ILE300
F	GLY333
F	ASP334
F	GLU341
F	LEU342
F	THR343
F	PRO344
F	PHE375

site_id	BC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE NAP F 601

Chain	Residue
F	LEU168
F	ALA198
F	SER199
F	TYR200
F	VAL201
F	ARG221
F	SER222
F	ARG226
F	VAL252
F	ALA290
F	VAL291
F	GLY292
F	ARG293

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	6
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	HIS472
B	HIS472
C	HIS472
D	HIS472
E	HIS472
F	HIS472

site_id	SWS_FT_FI2
Number of Residues	78
Details	BINDING: BINDING => ECO:0007744\|PDB:1H6V

Chain	Residue	Details
A	ILE18
A	VAL291
A	ASP334
A	GLU341
A	HIS472
B	ILE18
B	ASP42
B	GLY63
B	TYR131
B	THR161
B	ARG166
A	ASP42
B	ALA198
B	ARG221
B	ARG226
B	VAL291
B	ASP334
B	GLU341
B	HIS472
C	ILE18
C	ASP42
C	GLY63
A	GLY63
C	TYR131
C	THR161
C	ARG166
C	ALA198
C	ARG221
C	ARG226
C	VAL291
C	ASP334
C	GLU341
C	HIS472
A	TYR131
D	ILE18
D	ASP42
D	GLY63
D	TYR131
D	THR161
D	ARG166
D	ALA198
D	ARG221
D	ARG226
D	VAL291
A	THR161
D	ASP334
D	GLU341
D	HIS472
E	ILE18
E	ASP42
E	GLY63
E	TYR131
E	THR161
E	ARG166
E	ALA198
A	ARG166
E	ARG221
E	ARG226
E	VAL291
E	ASP334
E	GLU341
E	HIS472
F	ILE18
F	ASP42
F	GLY63
F	TYR131
A	ALA198
F	THR161
F	ARG166
F	ALA198
F	ARG221
F	ARG226
F	VAL291
F	ASP334
F	GLU341
F	HIS472
A	ARG221
A	ARG226

site_id	SWS_FT_FI3
Number of Residues	18
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q16881

Chain	Residue	Details
A	THR58
D	THR58
D	TYR200
D	LYS315
E	THR58
E	TYR200
E	LYS315
F	THR58
F	TYR200
F	LYS315
A	TYR200
A	LYS315
B	THR58
B	TYR200
B	LYS315
C	THR58
C	TYR200
C	LYS315

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:Q9JMH6

Chain	Residue	Details
A	LYS68
B	LYS68
C	LYS68
D	LYS68
E	LYS68
F	LYS68

site_id	SWS_FT_FI5
Number of Residues	6
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:Q16881

Chain	Residue	Details
A	TYR131
B	TYR131
C	TYR131
D	TYR131
E	TYR131
F	TYR131

site_id	SWS_FT_FI6
Number of Residues	12
Details	CROSSLNK: Cysteinyl-selenocysteine (Cys-Sec)

Chain	Residue	Details
A	CYS497
E	SEC498
F	CYS497
F	SEC498
A	SEC498
B	CYS497
B	SEC498
C	CYS497
C	SEC498
D	CYS497
D	SEC498
E	CYS497

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
A	CYS64
A	CYS59

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
D	HIS472
D	GLU477

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
E	HIS472
E	GLU477

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
F	HIS472
F	GLU477

site_id	CSA13
Number of Residues	3
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
A	ASP181
A	CYS177
A	SER180

site_id	CSA14
Number of Residues	3
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
B	ASP181
B	CYS177
B	SER180

site_id	CSA15
Number of Residues	3
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
C	ASP181
C	CYS177
C	SER180

site_id	CSA16
Number of Residues	3
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
D	ASP181
D	CYS177
D	SER180

site_id	CSA17
Number of Residues	3
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
E	ASP181
E	CYS177
E	SER180

site_id	CSA18
Number of Residues	3
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
F	ASP181
F	CYS177
F	SER180

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
B	CYS64
B	CYS59

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
C	CYS64
C	CYS59

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

Chain	Residue	Details
D	CYS64
D	CYS59

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

Chain	Residue	Details
E	CYS64
E	CYS59

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

Chain	Residue	Details
F	CYS64
F	CYS59

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

Chain	Residue	Details
A	HIS472
A	GLU477

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

Chain	Residue	Details
B	HIS472
B	GLU477

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
C	HIS472
C	GLU477

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