Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1F6M

CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THIOREDOXIN REDUCTASE, THIOREDOXIN, AND THE NADP+ ANALOG, AADP+

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0016491	molecular_function	oxidoreductase activity
A	0019430	biological_process	removal of superoxide radicals
A	0032991	cellular_component	protein-containing complex
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	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0016491	molecular_function	oxidoreductase activity
B	0019430	biological_process	removal of superoxide radicals
B	0032991	cellular_component	protein-containing complex
B	0045454	biological_process	cell redox homeostasis
B	0050660	molecular_function	flavin adenine dinucleotide binding
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0015035	molecular_function	protein-disulfide reductase activity
C	0030337	molecular_function	DNA polymerase processivity factor activity
C	0045454	biological_process	cell redox homeostasis
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0015035	molecular_function	protein-disulfide reductase activity
D	0030337	molecular_function	DNA polymerase processivity factor activity
D	0045454	biological_process	cell redox homeostasis
E	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0016491	molecular_function	oxidoreductase activity
E	0019430	biological_process	removal of superoxide radicals
E	0032991	cellular_component	protein-containing complex
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	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0016491	molecular_function	oxidoreductase activity
F	0019430	biological_process	removal of superoxide radicals
F	0032991	cellular_component	protein-containing complex
F	0045454	biological_process	cell redox homeostasis
F	0050660	molecular_function	flavin adenine dinucleotide binding
G	0005515	molecular_function	protein binding
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0015035	molecular_function	protein-disulfide reductase activity
G	0030337	molecular_function	DNA polymerase processivity factor activity
G	0045454	biological_process	cell redox homeostasis
H	0005515	molecular_function	protein binding
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0015035	molecular_function	protein-disulfide reductase activity
H	0030337	molecular_function	DNA polymerase processivity factor activity
H	0045454	biological_process	cell redox homeostasis

Functional Information from PDB Data

site_id	AC1
Number of Residues	35
Details	BINDING SITE FOR RESIDUE FAD A 1500

Chain	Residue
A	GLY12
A	GLY41
A	GLN42
A	LEU43
A	THR46
A	VAL49
A	ASN51
A	HIS83
A	ILE84
A	ALA111
A	THR112
A	SER13
A	GLY113
A	ALA114
A	HIS245
A	ILE251
A	GLY285
A	ASP286
A	ARG293
A	GLN294
A	ALA295
A	SER298
A	GLY14
A	3AA1501
A	HOH1502
A	HOH1521
A	HOH1530
A	HOH1556
B	TYR23
A	PRO15
A	ALA16
A	THR35
A	GLY36
A	MET37
A	GLU38

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE 3AA A 1501

Chain	Residue
A	LEU119
A	GLY153
A	GLY154
A	ASN155
A	THR156
A	GLU159
A	HIS175
A	ARG176
A	ARG177
A	ARG181
A	ALA242
A	ILE243
A	GLY244
A	HIS245
A	TYR292
A	ARG293
A	GLN294
A	FAD1500

site_id	AC3
Number of Residues	36
Details	BINDING SITE FOR RESIDUE FAD B 2500

Chain	Residue
A	TYR23
B	GLY12
B	SER13
B	GLY14
B	PRO15
B	ALA16
B	THR35
B	GLY36
B	MET37
B	GLU38
B	GLY41
B	GLN42
B	LEU43
B	THR46
B	VAL49
B	ASN51
B	HIS83
B	ILE84
B	ALA111
B	THR112
B	GLY113
B	ALA114
B	HIS245
B	ASN248
B	ILE251
B	GLY285
B	ASP286
B	ARG293
B	GLN294
B	ALA295
B	SER298
B	3AA2501
B	HOH2503
B	HOH2504
B	HOH2507
B	HOH2541

site_id	AC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE 3AA B 2501

Chain	Residue
B	ILE243
B	GLY244
B	HIS245
B	TYR292
B	ARG293
B	GLN294
B	FAD2500
B	HOH2518
B	HOH2529
B	HOH2542
B	HOH2557
B	ARG117
B	GLY153
B	GLY154
B	ASN155
B	THR156
B	GLU159
B	HIS175
B	ARG176
B	ARG177
B	ARG181

site_id	AC5
Number of Residues	33
Details	BINDING SITE FOR RESIDUE FAD E 3500

Chain	Residue
E	GLY12
E	SER13
E	GLY14
E	PRO15
E	ALA16
E	THR35
E	GLY36
E	MET37
E	GLU38
E	GLY41
E	GLN42
E	LEU43
E	THR46
E	VAL49
E	ASN51
E	HIS83
E	ILE84
E	ALA111
E	THR112
E	GLY113
E	ALA114
E	HIS245
E	ILE251
E	GLY285
E	ASP286
E	ARG293
E	GLN294
E	ALA295
E	SER298
E	3AA3501
E	HOH3522
E	HOH3533
F	TYR23

site_id	AC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE 3AA E 3501

Chain	Residue
E	LEU119
E	GLY153
E	GLY154
E	ASN155
E	THR156
E	GLU159
E	HIS175
E	ARG176
E	ARG177
E	ARG181
E	ALA242
E	ILE243
E	GLY244
E	HIS245
E	TYR292
E	ARG293
E	GLN294
E	FAD3500
E	HOH3504

site_id	AC7
Number of Residues	37
Details	BINDING SITE FOR RESIDUE FAD F 4500

Chain	Residue
E	TYR23
F	GLY12
F	SER13
F	GLY14
F	PRO15
F	ALA16
F	THR35
F	GLY36
F	MET37
F	GLU38
F	GLY41
F	GLN42
F	LEU43
F	THR46
F	VAL49
F	ASN51
F	HIS83
F	ILE84
F	ALA111
F	THR112
F	GLY113
F	ALA114
F	HIS245
F	ASN248
F	ILE251
F	GLY285
F	ASP286
F	ARG293
F	GLN294
F	ALA295
F	SER298
F	3AA4501
F	HOH4502
F	HOH4503
F	HOH4504
F	HOH4508
F	HOH4514

site_id	AC8
Number of Residues	20
Details	BINDING SITE FOR RESIDUE 3AA F 4501

Chain	Residue
F	ARG117
F	GLY153
F	GLY154
F	ASN155
F	THR156
F	GLU159
F	HIS175
F	ARG176
F	ARG177
F	ARG181
F	ILE243
F	GLY244
F	HIS245
F	TYR292
F	ARG293
F	GLN294
F	FAD4500
F	HOH4543
F	HOH4544
F	HOH4563

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	64
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8114095","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	428
Details	Domain: {"description":"Thioredoxin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Active site: {"description":"Nucleophile"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Site: {"description":"Deprotonates C-terminal active site Cys"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Site: {"description":"Contributes to redox potential value"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1tde

Chain	Residue	Details
A	SER135
A	CYS138
A	ASP139

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1tde

Chain	Residue	Details
B	SER135
B	CYS138
B	ASP139

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1tde

Chain	Residue	Details
E	SER135
E	CYS138
E	ASP139

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1tde

Chain	Residue	Details
F	SER135
F	CYS138
F	ASP139

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

Chain	Residue	Details
C	SER35
C	CYS32

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

Chain	Residue	Details
D	SER35
D	CYS32

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

Chain	Residue	Details
G	SER35
G	CYS32

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

Chain	Residue	Details
H	SER35
H	CYS32

site_id	MCSA1
Number of Residues	3
Details	M-CSA 381

Chain	Residue	Details
A	SER135	covalent catalysis, proton shuttle (general acid/base)
A	CYS138	covalent catalysis, proton shuttle (general acid/base)
A	ASP139	proton shuttle (general acid/base)

site_id	MCSA2
Number of Residues	3
Details	M-CSA 381

Chain	Residue	Details
B	SER135	covalent catalysis, proton shuttle (general acid/base)
B	CYS138	covalent catalysis, proton shuttle (general acid/base)
B	ASP139	proton shuttle (general acid/base)

site_id	MCSA3
Number of Residues	3
Details	M-CSA 381

Chain	Residue	Details
E	SER135	covalent catalysis, proton shuttle (general acid/base)
E	CYS138	covalent catalysis, proton shuttle (general acid/base)
E	ASP139	proton shuttle (general acid/base)

site_id	MCSA4
Number of Residues	3
Details	M-CSA 381

Chain	Residue	Details
F	SER135	covalent catalysis, proton shuttle (general acid/base)
F	CYS138	covalent catalysis, proton shuttle (general acid/base)
F	ASP139	proton shuttle (general acid/base)

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