Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5XMJ

Crystal structure of quinol:fumarate reductase from Desulfovibrio gigas

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000104	molecular_function	succinate dehydrogenase activity
A	0000166	molecular_function	nucleotide binding
A	0005886	cellular_component	plasma membrane
A	0008177	molecular_function	succinate dehydrogenase (quinone) activity
A	0009055	molecular_function	electron transfer activity
A	0009061	biological_process	anaerobic respiration
A	0016491	molecular_function	oxidoreductase activity
A	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
A	0022900	biological_process	electron transport chain
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0006099	biological_process	tricarboxylic acid cycle
B	0008177	molecular_function	succinate dehydrogenase (quinone) activity
B	0009055	molecular_function	electron transfer activity
B	0009060	biological_process	aerobic respiration
B	0016491	molecular_function	oxidoreductase activity
B	0022904	biological_process	respiratory electron transport chain
B	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0051538	molecular_function	3 iron, 4 sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0006099	biological_process	tricarboxylic acid cycle
C	0016020	cellular_component	membrane
C	0046872	molecular_function	metal ion binding
E	0000104	molecular_function	succinate dehydrogenase activity
E	0000166	molecular_function	nucleotide binding
E	0005886	cellular_component	plasma membrane
E	0008177	molecular_function	succinate dehydrogenase (quinone) activity
E	0009055	molecular_function	electron transfer activity
E	0009061	biological_process	anaerobic respiration
E	0016491	molecular_function	oxidoreductase activity
E	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
E	0022900	biological_process	electron transport chain
E	0050660	molecular_function	flavin adenine dinucleotide binding
F	0006099	biological_process	tricarboxylic acid cycle
F	0008177	molecular_function	succinate dehydrogenase (quinone) activity
F	0009055	molecular_function	electron transfer activity
F	0009060	biological_process	aerobic respiration
F	0016491	molecular_function	oxidoreductase activity
F	0022904	biological_process	respiratory electron transport chain
F	0046872	molecular_function	metal ion binding
F	0051536	molecular_function	iron-sulfur cluster binding
F	0051537	molecular_function	2 iron, 2 sulfur cluster binding
F	0051538	molecular_function	3 iron, 4 sulfur cluster binding
F	0051539	molecular_function	4 iron, 4 sulfur cluster binding
G	0006099	biological_process	tricarboxylic acid cycle
G	0016020	cellular_component	membrane
G	0046872	molecular_function	metal ion binding
I	0000104	molecular_function	succinate dehydrogenase activity
I	0000166	molecular_function	nucleotide binding
I	0005886	cellular_component	plasma membrane
I	0008177	molecular_function	succinate dehydrogenase (quinone) activity
I	0009055	molecular_function	electron transfer activity
I	0009061	biological_process	anaerobic respiration
I	0016491	molecular_function	oxidoreductase activity
I	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
I	0022900	biological_process	electron transport chain
I	0050660	molecular_function	flavin adenine dinucleotide binding
J	0006099	biological_process	tricarboxylic acid cycle
J	0008177	molecular_function	succinate dehydrogenase (quinone) activity
J	0009055	molecular_function	electron transfer activity
J	0009060	biological_process	aerobic respiration
J	0016491	molecular_function	oxidoreductase activity
J	0022904	biological_process	respiratory electron transport chain
J	0046872	molecular_function	metal ion binding
J	0051536	molecular_function	iron-sulfur cluster binding
J	0051537	molecular_function	2 iron, 2 sulfur cluster binding
J	0051538	molecular_function	3 iron, 4 sulfur cluster binding
J	0051539	molecular_function	4 iron, 4 sulfur cluster binding
K	0006099	biological_process	tricarboxylic acid cycle
K	0016020	cellular_component	membrane
K	0046872	molecular_function	metal ion binding
M	0000104	molecular_function	succinate dehydrogenase activity
M	0000166	molecular_function	nucleotide binding
M	0005886	cellular_component	plasma membrane
M	0008177	molecular_function	succinate dehydrogenase (quinone) activity
M	0009055	molecular_function	electron transfer activity
M	0009061	biological_process	anaerobic respiration
M	0016491	molecular_function	oxidoreductase activity
M	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
M	0022900	biological_process	electron transport chain
M	0050660	molecular_function	flavin adenine dinucleotide binding
N	0006099	biological_process	tricarboxylic acid cycle
N	0008177	molecular_function	succinate dehydrogenase (quinone) activity
N	0009055	molecular_function	electron transfer activity
N	0009060	biological_process	aerobic respiration
N	0016491	molecular_function	oxidoreductase activity
N	0022904	biological_process	respiratory electron transport chain
N	0046872	molecular_function	metal ion binding
N	0051536	molecular_function	iron-sulfur cluster binding
N	0051537	molecular_function	2 iron, 2 sulfur cluster binding
N	0051538	molecular_function	3 iron, 4 sulfur cluster binding
N	0051539	molecular_function	4 iron, 4 sulfur cluster binding
O	0006099	biological_process	tricarboxylic acid cycle
O	0016020	cellular_component	membrane
O	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	31
Details	binding site for residue FAD A 701

Chain	Residue
A	ILE11
A	HIS43
A	SER44
A	ALA46
A	ALA47
A	GLY49
A	GLY50
A	GLN180
A	ALA181
A	ALA215
A	THR216
A	GLY12
A	THR227
A	ASN228
A	GLY235
A	HIS369
A	GLY393
A	GLU394
A	ARG405
A	GLY408
A	SER410
A	LEU411
A	GLY13
A	ARG524
A	FUM702
A	ALA14
A	LEU15
A	ALA16
A	SER35
A	LEU36
A	SER42

site_id	AC2
Number of Residues	14
Details	binding site for residue FUM A 702

Chain	Residue
A	GLY49
A	PHE141
A	HIS257
A	LEU267
A	VAL268
A	THR269
A	GLU270
A	GLY271
A	ARG301
A	HIS369
A	ARG405
A	GLY407
A	GLY408
A	FAD701

site_id	AC3
Number of Residues	10
Details	binding site for residue F3S B 301

Chain	Residue
B	CYS161
B	THR163
B	CYS208
B	MET209
B	GLY210
B	LEU211
B	LEU212
B	ALA213
B	CYS214
B	LEU228

site_id	AC4
Number of Residues	9
Details	binding site for residue SF4 B 302

Chain	Residue
B	CYS151
B	GLU153
B	CYS154
B	CYS157
B	VAL174
B	CYS218
B	PRO219
B	ILE222
B	LEU224

site_id	AC5
Number of Residues	7
Details	binding site for residue FES B 303

Chain	Residue
B	CYS57
B	GLY60
B	ILE61
B	CYS62
B	GLY63
B	CYS65
B	CYS77

site_id	AC6
Number of Residues	16
Details	binding site for residue HEM C 301

Chain	Residue
C	PHE34
C	HIS38
C	MET39
C	VAL42
C	VAL72
C	HIS129
C	MET130
C	VAL133
C	LEU134
C	ILE139
C	LYS143
C	ARG147
C	TYR156
C	LEU159
C	LEU160
C	GLY204

site_id	AC7
Number of Residues	18
Details	binding site for residue HEM C 302

Chain	Residue
C	TRP112
C	ALA119
C	LEU123
C	HIS166
C	VAL167
C	LYS177
C	GLN24
C	MET25
C	GLY28
C	LEU31
C	ILE32
C	LEU35
C	MET76
C	HIS79
C	PHE80
C	ALA83
C	LYS86
C	MET87

site_id	AC8
Number of Residues	10
Details	binding site for residue LMT C 303

Chain	Residue
C	MET87
C	PRO88
C	PHE89
C	TRP94
C	LYS95
C	VAL116
C	ALA119
O	HIS9
O	ILE16
O	ILE81

site_id	AC9
Number of Residues	6
Details	binding site for residue MQ7 C 304

Chain	Residue
C	TRP36
C	ALA37
C	MET40
C	LEU41
C	ILE55
C	TYR63

site_id	AD1
Number of Residues	11
Details	binding site for residue FUM E 702

Chain	Residue
E	PHE141
E	HIS257
E	LEU267
E	VAL268
E	THR269
E	GLU270
E	ARG301
E	HIS369
E	ARG405
E	GLY407
E	GLY408

site_id	AD2
Number of Residues	9
Details	binding site for residue F3S F 301

Chain	Residue
F	CYS161
F	THR163
F	CYS208
F	MET209
F	GLY210
F	LEU211
F	LEU212
F	ALA213
F	CYS214

site_id	AD3
Number of Residues	6
Details	binding site for residue SF4 F 302

Chain	Residue
F	CYS151
F	CYS154
F	CYS157
F	VAL174
F	CYS218
F	ILE222

site_id	AD4
Number of Residues	16
Details	binding site for residue HEM G 301

Chain	Residue
G	PHE34
G	HIS38
G	MET39
G	VAL42
G	HIS129
G	ILE139
G	LYS143
G	SER144
G	ARG147
G	TYR156
G	LEU159
G	LEU160
G	GLY204
G	THR207
G	LEU208
G	PHE211

site_id	AD5
Number of Residues	19
Details	binding site for residue HEM G 302

Chain	Residue
F	MET209
G	GLN24
G	GLY28
G	LEU31
G	ILE32
G	HIS79
G	PHE80
G	ALA83
G	LYS86
G	MET87
G	TRP112
G	VAL116
G	ALA119
G	ILE122
G	LEU123
G	HIS166
G	VAL167
G	GLY170
G	LYS177

site_id	AD6
Number of Residues	30
Details	binding site for residue FAD I 701

Chain	Residue
I	GLY12
I	GLY13
I	ALA14
I	LEU15
I	ALA16
I	LEU36
I	SER42
I	HIS43
I	SER44
I	GLY49
I	GLY50
I	MET179
I	ALA181
I	ALA215
I	THR216
I	GLY217
I	THR227
I	ASN228
I	ILE231
I	GLY235
I	HIS369
I	GLY393
I	GLU394
I	ARG405
I	GLY408
I	SER410
I	LEU411
I	THR414
I	ARG524
I	FUM702

site_id	AD7
Number of Residues	8
Details	binding site for residue FUM I 702

Chain	Residue
I	PHE141
I	HIS257
I	THR269
I	GLU270
I	ARG301
I	HIS369
I	ARG405
I	FAD701

site_id	AD8
Number of Residues	6
Details	binding site for residue SF4 J 302

Chain	Residue
J	CYS151
J	CYS154
J	CYS157
J	VAL174
J	CYS218
J	ILE222

site_id	AD9
Number of Residues	11
Details	binding site for residue HEM K 301

Chain	Residue
K	PHE34
K	HIS38
K	VAL42
K	TYR63
K	HIS129
K	VAL133
K	SER144
K	ARG147
K	TYR156
K	LEU159
K	LEU208

site_id	AE1
Number of Residues	16
Details	binding site for residue HEM K 302

Chain	Residue
K	GLN24
K	MET25
K	GLY28
K	LEU31
K	ILE32
K	HIS79
K	ALA83
K	LYS86
K	TRP112
K	ALA119
K	LEU123
K	HIS166
K	VAL167
K	GLY170
K	ILE174
K	LYS177

site_id	AE2
Number of Residues	33
Details	binding site for residue FAD M 701

Chain	Residue
M	ILE11
M	GLY12
M	GLY13
M	ALA14
M	LEU15
M	ALA16
M	SER35
M	LEU36
M	SER42
M	HIS43
M	SER44
M	ALA47
M	GLN48
M	GLY49
M	GLY50
M	MET179
M	GLN180
M	ALA181
M	ALA215
M	THR216
M	GLY217
M	THR227
M	ASN228
M	GLY235
M	HIS369
M	TYR370
M	GLU394
M	GLY408
M	SER410
M	LEU411
M	THR414
M	ARG524
M	FUM702

site_id	AE3
Number of Residues	9
Details	binding site for residue FUM M 702

Chain	Residue
M	HIS257
M	LEU267
M	VAL268
M	THR269
M	GLU270
M	ARG301
M	HIS369
M	ARG405
M	FAD701

site_id	AE4
Number of Residues	10
Details	binding site for residue F3S N 301

Chain	Residue
N	CYS161
N	THR163
N	CYS208
N	MET209
N	GLY210
N	LEU211
N	LEU212
N	ALA213
N	CYS214
N	LEU228

site_id	AE5
Number of Residues	5
Details	binding site for residue SF4 N 302

Chain	Residue
N	CYS151
N	CYS154
N	CYS157
N	VAL174
N	CYS218

site_id	AE6
Number of Residues	10
Details	binding site for residue LMT O 301

Chain	Residue
C	HIS9
C	ILE16
C	ILE81
O	MET87
O	PRO88
O	PHE89
O	TRP94
O	LYS95
O	ARG98
O	VAL116

site_id	AE7
Number of Residues	14
Details	binding site for residue HEM O 302

Chain	Residue
O	PHE34
O	HIS38
O	MET39
O	HIS129
O	VAL133
O	ILE139
O	SER144
O	LEU148
O	TYR156
O	LEU159
O	LEU160
O	GLY204
O	THR207
O	PHE211

site_id	AE8
Number of Residues	19
Details	binding site for residue HEM O 303

Chain	Residue
O	GLN24
O	MET25
O	GLY28
O	LEU31
O	ILE32
O	HIS79
O	PHE80
O	ALA83
O	LYS86
O	MET87
O	TRP112
O	ALA119
O	ILE122
O	LEU123
O	HIS166
O	VAL167
O	GLY170
O	LYS177
O	TYR178

site_id	AE9
Number of Residues	32
Details	binding site for Di-peptide FAD E 701 and HIS E 43

Chain	Residue
E	ILE11
E	GLY12
E	GLY13
E	ALA14
E	LEU15
E	ALA16
E	SER35
E	LEU36
E	VAL37
E	SER42
E	SER44
E	SER45
E	ALA46
E	ALA47
E	GLY49
E	GLY50
E	MET179
E	ALA181
E	ALA215
E	THR216
E	GLY217
E	THR227
E	ASN228
E	ALA229
E	ILE231
E	GLU394
E	GLY408
E	ASN409
E	SER410
E	LEU411
E	THR414
E	ARG524

site_id	AF1
Number of Residues	13
Details	binding site for Di-peptide FES F 303 and CYS F 65

Chain	Residue
F	PHE55
F	CYS56
F	CYS57
F	ARG58
F	ILE61
F	CYS62
F	GLY63
F	SER64
F	ALA66
F	MET67
F	LEU75
F	ALA76
F	CYS77

site_id	AF2
Number of Residues	8
Details	binding site for Di-peptide PRO I 608 and PHE I 612

Chain	Residue
I	ASN605
I	GLU606
I	LEU607
I	PRO609
I	GLU610
I	LYS611
I	VAL613
I	ILE614

site_id	AF3
Number of Residues	8
Details	binding site for Di-peptide PRO I 608 and PHE I 612

Chain	Residue
I	ASN605
I	GLU606
I	LEU607
I	PRO609
I	GLU610
I	LYS611
I	VAL613
I	ILE614

site_id	AF4
Number of Residues	8
Details	binding site for Di-peptide PRO I 608 and PHE I 612

Chain	Residue
I	ASN605
I	GLU606
I	LEU607
I	PRO609
I	GLU610
I	LYS611
I	VAL613
I	ILE614

site_id	AF5
Number of Residues	8
Details	binding site for Di-peptide PRO I 608 and PHE I 612

Chain	Residue
I	ASN605
I	GLU606
I	LEU607
I	PRO609
I	GLU610
I	LYS611
I	VAL613
I	ILE614

site_id	AF6
Number of Residues	13
Details	binding site for Di-peptide F3S J 301 and CYS J 214

Chain	Residue
J	CYS161
J	THR163
J	CYS208
J	MET209
J	GLY210
J	LEU211
J	LEU212
J	ALA213
J	GLU215
J	ASP216
J	VAL217
J	CYS218
J	LEU224

site_id	AF7
Number of Residues	14
Details	binding site for Di-peptide FES J 303 and CYS J 65

Chain	Residue
J	ASP54
J	PHE55
J	CYS57
J	ARG58
J	GLY60
J	ILE61
J	CYS62
J	GLY63
J	SER64
J	ALA66
J	MET67
J	LEU75
J	ALA76
J	CYS77

site_id	AF8
Number of Residues	12
Details	binding site for Di-peptide FES N 303 and CYS N 65

Chain	Residue
N	PHE55
N	CYS57
N	ARG58
N	ILE61
N	CYS62
N	GLY63
N	SER64
N	ALA66
N	MET67
N	LEU75
N	ALA76
N	CYS77

Functional Information from PROSITE/UniProt

site_id	PS00197
Number of Residues	9
Details	2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CRAGICGSC

Chain	Residue	Details
B	CYS57-CYS65

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

Chain	Residue	Details
B	CYS151-GLY162

site_id	PS00504
Number of Residues	10
Details	FRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHSsaAqGG

Chain	Residue	Details
A	ARG41-GLY50

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