Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2J3N

X-ray structure of human thioredoxin reductase 1

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	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
C	0016491	molecular_function	oxidoreductase activity
C	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
C	0045454	biological_process	cell redox homeostasis
C	0050660	molecular_function	flavin adenine dinucleotide binding
D	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
D	0016491	molecular_function	oxidoreductase activity
D	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
D	0045454	biological_process	cell redox homeostasis
D	0050660	molecular_function	flavin adenine dinucleotide binding
E	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
E	0016491	molecular_function	oxidoreductase activity
E	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
E	0045454	biological_process	cell redox homeostasis
E	0050660	molecular_function	flavin adenine dinucleotide binding
F	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
F	0016491	molecular_function	oxidoreductase activity
F	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
F	0045454	biological_process	cell redox homeostasis
F	0050660	molecular_function	flavin adenine dinucleotide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	30
Details	BINDING SITE FOR RESIDUE FAD A 600

Chain	Residue
A	ILE18
A	GLY57
A	THR58
A	CYS59
A	CYS64
A	LYS67
A	TYR131
A	GLY132
A	ALA160
A	THR161
A	GLY162
A	GLY19
A	TYR200
A	VAL201
A	ARG293
A	ASP334
A	GLU341
A	LEU342
A	THR343
A	PRO344
A	HOH2007
B	HIS472
A	GLY20
B	HOH2008
A	GLY21
A	SER22
A	GLY23
A	LEU41
A	ASP42
A	PHE43

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

Chain	Residue
A	ARG166
A	LEU168
A	GLY197
A	ALA198
A	SER199
A	ARG221
A	SER222
A	ARG226
A	ILE291
A	GLY292
A	ARG293
A	LYS315
A	GLU341

site_id	AC3
Number of Residues	30
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	GLY63
B	CYS64
B	LYS67
B	ALA130
B	TYR131
B	GLY132
B	ALA160
B	THR161
B	GLY162
B	TYR200
B	VAL201
B	ARG293
B	ASP334
B	GLU341
B	LEU342
B	THR343
B	PRO344
B	ALA346

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE NAP B 601

Chain	Residue
B	ARG166
B	LEU168
B	GLY197
B	ALA198
B	SER199
B	ARG221
B	SER222
B	ILE223
B	ARG226
B	VAL252
B	ILE291
B	GLY292
B	ARG293
B	LYS315
B	GLU341

site_id	AC5
Number of Residues	31
Details	BINDING SITE FOR RESIDUE FAD C 600

Chain	Residue
C	CYS59
C	VAL62
C	GLY63
C	CYS64
C	LYS67
C	TYR131
C	GLY132
C	ALA160
C	THR161
C	GLY162
C	SER180
C	TYR200
C	ASP334
C	GLU341
C	LEU342
C	THR343
C	PRO344
C	ALA346
C	HOH2001
D	HIS472
C	GLY19
C	GLY20
C	GLY21
C	SER22
C	GLY23
C	LEU41
C	ASP42
C	PHE43
C	VAL44
C	GLY57
C	THR58

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

Chain	Residue
C	ARG166
C	LEU168
C	GLY197
C	ALA198
C	SER199
C	ARG221
C	SER222
C	ARG226
C	ILE291
C	GLY292
C	ARG293
C	GLU341
C	HOH2007

site_id	AC7
Number of Residues	34
Details	BINDING SITE FOR RESIDUE FAD D 600

Chain	Residue
C	HIS472
C	PRO473
C	HOH2006
D	ILE18
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	TYR131
D	GLY132
D	ALA160
D	THR161
D	GLY162
D	TYR200
D	VAL201
D	ARG293
D	ASP334
D	GLU341
D	LEU342
D	THR343
D	PRO344
D	ALA346
D	HOH2006

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE NAP D 601

Chain	Residue
D	LEU168
D	ALA198
D	SER199
D	ARG221
D	SER222
D	ARG226
D	VAL252
D	ILE291
D	GLY292
D	GLU341

site_id	AC9
Number of Residues	29
Details	BINDING SITE FOR RESIDUE FAD E 600

Chain	Residue
E	GLY19
E	GLY20
E	GLY21
E	SER22
E	GLY23
E	ASP42
E	PHE43
E	VAL44
E	GLY57
E	THR58
E	CYS59
E	VAL62
E	GLY63
E	CYS64
E	LYS67
E	TYR131
E	GLY132
E	ALA160
E	THR161
E	GLY162
E	TYR200
E	ARG293
E	ASP334
E	GLU341
E	LEU342
E	THR343
E	PRO344
F	HIS472
F	PRO473

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

Chain	Residue
E	ARG166
E	ALA198
E	SER199
E	ARG221
E	SER222
E	ARG226
E	GLY227
E	PHE228
E	ILE291
E	GLY292
E	ARG293
E	LYS315
E	GLU341

site_id	BC2
Number of Residues	29
Details	BINDING SITE FOR RESIDUE FAD F 600

Chain	Residue
E	HIS472
F	GLY19
F	GLY21
F	SER22
F	GLY23
F	ASP42
F	PHE43
F	GLY57
F	THR58
F	CYS59
F	VAL62
F	GLY63
F	CYS64
F	LYS67
F	TYR131
F	GLY132
F	THR161
F	GLY162
F	SER180
F	TYR200
F	VAL201
F	ARG293
F	ASP334
F	GLU341
F	LEU342
F	THR343
F	PRO344
F	ALA346
F	HOH2004

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE NAP F 601

Chain	Residue
F	ARG166
F	LEU168
F	ALA198
F	SER199
F	ARG221
F	SER222
F	ARG226
F	ILE291
F	GLY292
F	ARG293
F	GLU341

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MPD A 701

Chain	Residue
A	SER404
A	VAL478
A	THR481
A	SER483

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD B 700

Chain	Residue
A	LEU75
A	LEU76
B	GLN72
B	LEU76
B	ALA79

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MPD B 701

Chain	Residue
B	SER415
B	ARG416
B	ASN418
C	GLU122

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MPD D 700

Chain	Residue
C	GLN72
C	LEU76
C	ALA79

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MPD F 700

Chain	Residue
E	LEU76
E	ALA79
F	GLN72
F	LEU75
F	LEU76
F	ALA79
F	HOH2007

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 => ECO:0000250

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

site_id	SWS_FT_FI2
Number of Residues	72
Details	BINDING: BINDING => ECO:0000269\|PubMed:17512005, ECO:0007744\|PDB:2J3N

Chain	Residue	Details
A	GLY172
A	LEU465
A	VAL484
A	HIS472
B	GLY172
B	LYS192
B	PHE208
B	GLY213
B	GLU281
B	ILE316
B	GLN348
A	LYS192
B	PRO371
B	GLY442
B	LEU465
B	VAL484
B	HIS472
C	GLY172
C	LYS192
C	PHE208
C	GLY213
C	GLU281
A	PHE208
C	ILE316
C	GLN348
C	PRO371
C	GLY442
C	LEU465
C	VAL484
C	HIS472
D	GLY172
D	LYS192
D	PHE208
A	GLY213
D	GLY213
D	GLU281
D	ILE316
D	GLN348
D	PRO371
D	GLY442
D	LEU465
D	VAL484
D	HIS472
E	GLY172
A	GLU281
E	LYS192
E	PHE208
E	GLY213
E	GLU281
E	ILE316
E	GLN348
E	PRO371
E	GLY442
E	LEU465
E	VAL484
A	ILE316
E	HIS472
F	GLY172
F	LYS192
F	PHE208
F	GLY213
F	GLU281
F	ILE316
F	GLN348
F	PRO371
F	GLY442
A	GLN348
F	LEU465
F	VAL484
F	HIS472
A	PRO371
A	GLY442

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0007744\|PDB:2J3N

Chain	Residue	Details
A	GLU311
E	SER491
F	GLU311
F	SER491
A	SER491
B	GLU311
B	SER491
C	GLU311
C	SER491
D	GLU311
D	SER491
E	GLU311

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0007744\|PDB:2ZZ0, ECO:0007744\|PDB:2ZZB, ECO:0007744\|PDB:3QFA

Chain	Residue	Details
A	GLY350
B	GLY350
C	GLY350
D	GLY350
E	GLY350
F	GLY350

site_id	SWS_FT_FI5
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:O89049

Chain	Residue	Details
A	THR376
B	THR376
C	THR376
D	THR376
E	THR376
F	THR376

site_id	SWS_FT_FI6
Number of Residues	6
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:Q9JMH6

Chain	Residue	Details
A	VAL218
B	VAL218
C	VAL218
D	VAL218
E	VAL218
F	VAL218

site_id	SWS_FT_FI7
Number of Residues	6
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:15592455

Chain	Residue	Details
A	GLU281
B	GLU281
C	GLU281
D	GLU281
E	GLU281
F	GLU281

site_id	SWS_FT_FI8
Number of Residues	12
Details	CROSSLNK: Cysteinyl-selenocysteine (Cys-Sec) => ECO:0000250

Chain	Residue	Details
A	CYS497
E	CYS498
F	CYS497
F	CYS498
A	CYS498
B	CYS497
B	CYS498
C	CYS497
C	CYS498
D	CYS497
D	CYS498
E	CYS497

Catalytic Information from CSA

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

Chain	Residue	Details
A	HIS472
A	GLU477
B	CYS64
B	CYS59

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

Chain	Residue	Details
A	CYS64
A	CYS59
B	HIS472
B	GLU477

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

Chain	Residue	Details
D	CYS64
D	CYS59
C	HIS472
C	GLU477

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
D	HIS472
D	GLU477
C	CYS64
C	CYS59

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
F	CYS64
F	CYS59
E	HIS472
E	GLU477

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
F	HIS472
F	GLU477
E	CYS64
E	CYS59

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
A	ASP181
A	CYS177
A	SER180

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
B	ASP181
B	CYS177
B	SER180

site_id	CSA9
Number of Residues	3
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
C	ASP181
C	CYS177
C	SER180

site_id	CSA10
Number of Residues	3
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
D	ASP181
D	CYS177
D	SER180

site_id	CSA11
Number of Residues	3
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
E	ASP181
E	CYS177
E	SER180

site_id	CSA12
Number of Residues	3
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
F	ASP181
F	CYS177
F	SER180

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