Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2CFY

Crystal 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	33
Details	BINDING SITE FOR RESIDUE FAD A 600

Chain	Residue
A	ILE18
A	VAL44
A	GLY57
A	THR58
A	CYS59
A	GLY63
A	CYS64
A	LYS67
A	ALA130
A	TYR131
A	GLY132
A	GLY19
A	ALA160
A	THR161
A	GLY162
A	TYR200
A	VAL201
A	ARG293
A	ILE300
A	GLY333
A	ASP334
A	GLU341
A	GLY20
A	LEU342
A	THR343
A	PRO344
B	HIS472
A	GLY21
A	SER22
A	GLY23
A	LEU41
A	ASP42
A	PHE43

site_id	AC2
Number of Residues	31
Details	BINDING SITE FOR RESIDUE FAD B 600

Chain	Residue
A	HIS472
B	ILE18
B	GLY19
B	GLY20
B	GLY21
B	GLY23
B	LEU41
B	ASP42
B	PHE43
B	VAL44
B	GLY57
B	THR58
B	CYS59
B	CYS64
B	LYS67
B	TYR131
B	GLY132
B	ALA160
B	THR161
B	GLY162
B	VAL201
B	ARG293
B	ILE300
B	GLY333
B	ASP334
B	GLU341
B	LEU342
B	THR343
B	PRO344
B	HOH2003
B	HOH2053

site_id	AC3
Number of Residues	31
Details	BINDING SITE FOR RESIDUE FAD C 600

Chain	Residue
C	ILE18
C	GLY19
C	GLY20
C	GLY21
C	SER22
C	GLY23
C	LEU41
C	ASP42
C	PHE43
C	VAL44
C	GLY57
C	THR58
C	CYS64
C	LYS67
C	ALA130
C	TYR131
C	GLY132
C	ALA160
C	THR161
C	GLY162
C	VAL201
C	ARG293
C	ILE300
C	GLY333
C	ASP334
C	GLU341
C	LEU342
C	THR343
C	PRO344
C	HOH2057
D	HIS472

site_id	AC4
Number of Residues	30
Details	BINDING SITE FOR RESIDUE FAD D 600

Chain	Residue
D	GLY23
D	LEU41
D	ASP42
D	PHE43
D	VAL44
D	GLY57
D	THR58
D	CYS59
D	GLY63
D	CYS64
D	LYS67
D	ALA130
D	TYR131
D	GLY132
D	ALA160
D	THR161
D	GLY162
D	VAL201
D	ARG293
D	ILE300
D	GLY333
D	ASP334
D	GLU341
D	LEU342
D	THR343
D	PRO344
C	HIS472
D	GLY19
D	GLY21
D	SER22

site_id	AC5
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FAD E 600

Chain	Residue
E	ILE18
E	GLY19
E	GLY21
E	SER22
E	GLY23
E	LEU41
E	ASP42
E	PHE43
E	VAL44
E	GLY57
E	THR58
E	CYS59
E	CYS64
E	TYR131
E	GLY132
E	THR161
E	GLY162
E	ILE300
E	GLY333
E	ASP334
E	GLU341
E	LEU342
E	THR343

site_id	AC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE FAD F 600

Chain	Residue
F	GLY19
F	GLY20
F	GLY21
F	GLY23
F	LEU41
F	ASP42
F	PHE43
F	VAL44
F	GLY57
F	THR58
F	ALA130
F	TYR131
F	GLY132
F	THR161
F	GLY162
F	ILE300
F	GLY333
F	ASP334
F	ALA346

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	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	144
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17512005","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2J3N","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PDB","id":"2J3N","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PDB","id":"2ZZ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZZB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QFA","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"O89049","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9JMH6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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	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

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

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