Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6TGA

Cryo-EM Structure of as isolated form of NAD+-dependent Formate Dehydrogenase from Rhodobacter capsulatus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008863	molecular_function	formate dehydrogenase (NAD+) activity
A	0015942	biological_process	formate metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0043546	molecular_function	molybdopterin cofactor binding
A	0045333	biological_process	cellular respiration
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
A	1990204	cellular_component	oxidoreductase complex
B	0008137	molecular_function	NADH dehydrogenase (ubiquinone) activity
B	0010181	molecular_function	FMN binding
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	1902600	biological_process	proton transmembrane transport
C	0016491	molecular_function	oxidoreductase activity
C	0046872	molecular_function	metal ion binding
C	0051537	molecular_function	2 iron, 2 sulfur cluster binding
D	0016491	molecular_function	oxidoreductase activity
E	0008863	molecular_function	formate dehydrogenase (NAD+) activity
E	0015942	biological_process	formate metabolic process
E	0016491	molecular_function	oxidoreductase activity
E	0043546	molecular_function	molybdopterin cofactor binding
E	0045333	biological_process	cellular respiration
E	0046872	molecular_function	metal ion binding
E	0051536	molecular_function	iron-sulfur cluster binding
E	0051537	molecular_function	2 iron, 2 sulfur cluster binding
E	0051539	molecular_function	4 iron, 4 sulfur cluster binding
E	1990204	cellular_component	oxidoreductase complex
F	0008137	molecular_function	NADH dehydrogenase (ubiquinone) activity
F	0010181	molecular_function	FMN binding
F	0016491	molecular_function	oxidoreductase activity
F	0046872	molecular_function	metal ion binding
F	0051539	molecular_function	4 iron, 4 sulfur cluster binding
F	1902600	biological_process	proton transmembrane transport
G	0016491	molecular_function	oxidoreductase activity
G	0046872	molecular_function	metal ion binding
G	0051537	molecular_function	2 iron, 2 sulfur cluster binding
H	0016491	molecular_function	oxidoreductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	29
Details	binding site for residue MGD A 1001

Chain	Residue
A	ARG357
A	GLU656
A	ASP657
A	SER661
A	HIS681
A	ASN686
A	SER699
A	LYS704
A	ASP730
A	THR827
A	ARG829
A	CYS358
A	ASN835
A	VAL836
A	ALA838
A	GLN839
A	ASN908
A	TYR924
A	LYS925
A	MGD1002
A	6MO1003
A	H2S1009
A	CYS382
A	VAL385
A	CYS386
A	LEU551
A	GLU555
A	GLN589
A	GLY655

site_id	AC2
Number of Residues	32
Details	binding site for residue MGD A 1002

Chain	Residue
A	CYS261
A	LYS295
A	CYS386
A	ILE419
A	GLY420
A	ASN422
A	ASP425
A	GLY426
A	HIS427
A	VAL447
A	ASP448
A	PRO449
A	ARG450
A	PRO470
A	GLY471
A	ASN473
A	GLY550
A	LEU551
A	GLY552
A	HIS556
A	GLY588
A	GLN589
A	THR826
A	ARG829
A	ILE830
A	LEU831
A	GLN833
A	ASN835
A	HIS901
A	LYS925
A	MGD1001
A	6MO1003

site_id	AC3
Number of Residues	4
Details	binding site for residue 6MO A 1003

Chain	Residue
A	CYS386
A	MGD1001
A	MGD1002
A	H2S1009

site_id	AC4
Number of Residues	6
Details	binding site for residue FES A 1004

Chain	Residue
A	CYS57
A	VAL65
A	GLY66
A	CYS68
A	CYS71
A	CYS85

site_id	AC5
Number of Residues	7
Details	binding site for residue SF4 A 1005

Chain	Residue
A	HIS117
A	CYS121
A	CYS124
A	ALA126
A	CYS130
A	THR236
A	ALA237

site_id	AC6
Number of Residues	10
Details	binding site for residue SF4 A 1006

Chain	Residue
A	CYS182
A	ILE183
A	VAL184
A	CYS185
A	MET186
A	CYS188
A	ILE212
A	CYS234
A	THR236
A	THR238

site_id	AC7
Number of Residues	7
Details	binding site for residue SF4 A 1007

Chain	Residue
A	CYS192
A	THR198
A	CYS224
A	CYS227
A	GLY228
A	ALA229
A	CYS230

site_id	AC8
Number of Residues	8
Details	binding site for residue SF4 A 1008

Chain	Residue
A	CYS265
A	CYS293
A	LYS295
A	VAL429
A	CYS258
A	TYR260
A	CYS261
A	GLY264

site_id	AC9
Number of Residues	4
Details	binding site for residue H2S A 1009

Chain	Residue
A	CYS386
A	VAL592
A	MGD1001
A	6MO1003

site_id	AD1
Number of Residues	13
Details	binding site for residue FMN B 601

Chain	Residue
B	GLY146
B	ARG147
B	GLY148
B	ASN174
B	ASP176
B	GLU177
B	TYR254
B	GLY257
B	GLU258
B	GLU259
B	ASN293
B	ASN294
B	SER297

site_id	AD2
Number of Residues	8
Details	binding site for residue SF4 B 602

Chain	Residue
B	SER426
B	CYS427
B	GLY428
B	THR429
B	CYS430
B	CYS433
B	LEU470
B	CYS471

site_id	AD3
Number of Residues	6
Details	binding site for residue FES G 201

Chain	Residue
G	CYS77
G	ALA79
G	CYS82
G	CYS116
G	LEU119
G	CYS120

site_id	AD4
Number of Residues	29
Details	binding site for residue MGD E 1001

Chain	Residue
E	ARG357
E	CYS358
E	CYS382
E	VAL385
E	CYS386
E	LEU551
E	GLU555
E	GLN589
E	GLY655
E	GLU656
E	ASP657
E	SER661
E	HIS681
E	ASN686
E	SER699
E	LYS704
E	ASP730
E	THR827
E	ARG829
E	ASN835
E	VAL836
E	ALA838
E	GLN839
E	ASN908
E	TYR924
E	LYS925
E	MGD1002
E	6MO1003
E	H2S1009

site_id	AD5
Number of Residues	32
Details	binding site for residue MGD E 1002

Chain	Residue
E	CYS261
E	LYS295
E	CYS386
E	ILE419
E	GLY420
E	ASN422
E	ASP425
E	GLY426
E	HIS427
E	VAL447
E	ASP448
E	PRO449
E	ARG450
E	PRO470
E	GLY471
E	ASN473
E	GLY550
E	LEU551
E	GLY552
E	HIS556
E	GLY588
E	GLN589
E	THR826
E	ARG829
E	ILE830
E	LEU831
E	GLN833
E	ASN835
E	HIS901
E	LYS925
E	MGD1001
E	6MO1003

site_id	AD6
Number of Residues	4
Details	binding site for residue 6MO E 1003

Chain	Residue
E	CYS386
E	MGD1001
E	MGD1002
E	H2S1009

site_id	AD7
Number of Residues	6
Details	binding site for residue FES E 1004

Chain	Residue
E	CYS57
E	VAL65
E	GLY66
E	CYS68
E	CYS71
E	CYS85

site_id	AD8
Number of Residues	7
Details	binding site for residue SF4 E 1005

Chain	Residue
E	HIS117
E	CYS121
E	CYS124
E	ALA126
E	CYS130
E	THR236
E	ALA237

site_id	AD9
Number of Residues	10
Details	binding site for residue SF4 E 1006

Chain	Residue
E	CYS182
E	ILE183
E	VAL184
E	CYS185
E	MET186
E	CYS188
E	ILE212
E	CYS234
E	THR236
E	THR238

site_id	AE1
Number of Residues	7
Details	binding site for residue SF4 E 1007

Chain	Residue
E	CYS192
E	THR198
E	CYS224
E	CYS227
E	GLY228
E	ALA229
E	CYS230

site_id	AE2
Number of Residues	8
Details	binding site for residue SF4 E 1008

Chain	Residue
E	CYS258
E	TYR260
E	CYS261
E	GLY264
E	CYS265
E	CYS293
E	LYS295
E	VAL429

site_id	AE3
Number of Residues	4
Details	binding site for residue H2S E 1009

Chain	Residue
E	CYS386
E	VAL592
E	MGD1001
E	6MO1003

site_id	AE4
Number of Residues	13
Details	binding site for residue FMN F 601

Chain	Residue
F	GLY146
F	ARG147
F	GLY148
F	ASN174
F	ASP176
F	GLU177
F	TYR254
F	GLY257
F	GLU258
F	GLU259
F	ASN293
F	ASN294
F	SER297

site_id	AE5
Number of Residues	8
Details	binding site for residue SF4 F 602

Chain	Residue
F	SER426
F	CYS427
F	GLY428
F	THR429
F	CYS430
F	CYS433
F	LEU470
F	CYS471

site_id	AE6
Number of Residues	6
Details	binding site for residue FES C 201

Chain	Residue
C	CYS77
C	ALA79
C	CYS82
C	CYS116
C	LEU119
C	CYS120

Functional Information from PROSITE/UniProt

site_id	PS00198
Number of Residues	12
Details	4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiVCMrCVrACE

Chain	Residue	Details
A	CYS182-GLU193
A	CYS224-PRO235

site_id	PS00551
Number of Residues	19
Details	MOLYBDOPTERIN_PROK_1 Prokaryotic molybdopterin oxidoreductases signature 1. TtCay.CGVgCsFeAhmlgD

Chain	Residue	Details
A	THR256-ASP274

site_id	PS00644
Number of Residues	16
Details	COMPLEX1_51K_1 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. GAGAYVCGEETSLLNS

Chain	Residue	Details
B	GLY250-SER265

site_id	PS00645
Number of Residues	12
Details	COMPLEX1_51K_2 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. ESCGtCtPCRiG

Chain	Residue	Details
B	GLU425-GLY436

site_id	PS00932
Number of Residues	28
Details	MOLYBDOPTERIN_PROK_3 Prokaryotic molybdopterin oxidoreductases signature 3. AetrGIrDgDwVrLaSraGettlrAtVT

Chain	Residue	Details
A	ALA861-THR888

site_id	PS01039
Number of Residues	14
Details	SBP_BACTERIAL_3 Bacterial extracellular solute-binding proteins, family 3 signature. GFEMEVRVgAGAYV

Chain	Residue	Details
B	GLY242-VAL255

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)