Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1E7P

QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000104	molecular_function	succinate dehydrogenase activity
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	0022904	biological_process	respiratory electron transport chain
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0005886	cellular_component	plasma membrane
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	0005886	cellular_component	plasma membrane
C	0006099	biological_process	tricarboxylic acid cycle
C	0016020	cellular_component	membrane
C	0022904	biological_process	respiratory electron transport chain
C	0046872	molecular_function	metal ion binding
D	0000104	molecular_function	succinate dehydrogenase activity
D	0005886	cellular_component	plasma membrane
D	0008177	molecular_function	succinate dehydrogenase (quinone) activity
D	0009055	molecular_function	electron transfer activity
D	0009061	biological_process	anaerobic respiration
D	0016491	molecular_function	oxidoreductase activity
D	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
D	0022900	biological_process	electron transport chain
D	0022904	biological_process	respiratory electron transport chain
D	0050660	molecular_function	flavin adenine dinucleotide binding
E	0005886	cellular_component	plasma membrane
E	0006099	biological_process	tricarboxylic acid cycle
E	0008177	molecular_function	succinate dehydrogenase (quinone) activity
E	0009055	molecular_function	electron transfer activity
E	0009060	biological_process	aerobic respiration
E	0016491	molecular_function	oxidoreductase activity
E	0022904	biological_process	respiratory electron transport chain
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	0051538	molecular_function	3 iron, 4 sulfur cluster binding
E	0051539	molecular_function	4 iron, 4 sulfur cluster binding
F	0005886	cellular_component	plasma membrane
F	0006099	biological_process	tricarboxylic acid cycle
F	0016020	cellular_component	membrane
F	0022904	biological_process	respiratory electron transport chain
F	0046872	molecular_function	metal ion binding
G	0000104	molecular_function	succinate dehydrogenase activity
G	0005886	cellular_component	plasma membrane
G	0008177	molecular_function	succinate dehydrogenase (quinone) activity
G	0009055	molecular_function	electron transfer activity
G	0009061	biological_process	anaerobic respiration
G	0016491	molecular_function	oxidoreductase activity
G	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
G	0022900	biological_process	electron transport chain
G	0022904	biological_process	respiratory electron transport chain
G	0050660	molecular_function	flavin adenine dinucleotide binding
H	0005886	cellular_component	plasma membrane
H	0006099	biological_process	tricarboxylic acid cycle
H	0008177	molecular_function	succinate dehydrogenase (quinone) activity
H	0009055	molecular_function	electron transfer activity
H	0009060	biological_process	aerobic respiration
H	0016491	molecular_function	oxidoreductase activity
H	0022904	biological_process	respiratory electron transport chain
H	0046872	molecular_function	metal ion binding
H	0051536	molecular_function	iron-sulfur cluster binding
H	0051537	molecular_function	2 iron, 2 sulfur cluster binding
H	0051538	molecular_function	3 iron, 4 sulfur cluster binding
H	0051539	molecular_function	4 iron, 4 sulfur cluster binding
I	0005886	cellular_component	plasma membrane
I	0006099	biological_process	tricarboxylic acid cycle
I	0016020	cellular_component	membrane
I	0022904	biological_process	respiratory electron transport chain
I	0046872	molecular_function	metal ion binding
J	0000104	molecular_function	succinate dehydrogenase activity
J	0005886	cellular_component	plasma membrane
J	0008177	molecular_function	succinate dehydrogenase (quinone) activity
J	0009055	molecular_function	electron transfer activity
J	0009061	biological_process	anaerobic respiration
J	0016491	molecular_function	oxidoreductase activity
J	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
J	0022900	biological_process	electron transport chain
J	0022904	biological_process	respiratory electron transport chain
J	0050660	molecular_function	flavin adenine dinucleotide binding
K	0005886	cellular_component	plasma membrane
K	0006099	biological_process	tricarboxylic acid cycle
K	0008177	molecular_function	succinate dehydrogenase (quinone) activity
K	0009055	molecular_function	electron transfer activity
K	0009060	biological_process	aerobic respiration
K	0016491	molecular_function	oxidoreductase activity
K	0022904	biological_process	respiratory electron transport chain
K	0046872	molecular_function	metal ion binding
K	0051536	molecular_function	iron-sulfur cluster binding
K	0051537	molecular_function	2 iron, 2 sulfur cluster binding
K	0051538	molecular_function	3 iron, 4 sulfur cluster binding
K	0051539	molecular_function	4 iron, 4 sulfur cluster binding
L	0005886	cellular_component	plasma membrane
L	0006099	biological_process	tricarboxylic acid cycle
L	0016020	cellular_component	membrane
L	0022904	biological_process	respiratory electron transport chain
L	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	GLY12
A	SER44
A	ALA46
A	ALA47
A	GLN48
A	GLY49
A	GLY50
A	ALA181
A	ALA215
A	THR216
A	GLY217
A	GLY13
A	THR227
A	ASN228
A	THR235
A	LEU267
A	HIS369
A	TYR370
A	GLU393
A	ARG404
A	GLY407
A	SER409
A	GLY14
A	VAL410
A	MLA702
A	LEU15
A	ALA16
A	SER35
A	LEU36
A	SER42
A	HIS43

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MLA A 702

Chain	Residue
A	PHE141
A	HIS257
A	LEU267
A	THR269
A	GLU270
A	HIS369
A	ARG404
A	GLY407
A	FAD701

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA A 703

Chain	Residue
A	TYR370
A	SER371
A	MET372
A	GLU393
A	ALA395

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES B 301

Chain	Residue
B	CYS57
B	ARG58
B	GLY60
B	ILE61
B	CYS62
B	GLY63
B	CYS65
B	CYS77

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE F3S B 302

Chain	Residue
B	CYS161
B	THR163
B	CYS208
B	THR210
B	LEU211
B	LEU212
B	ALA213
B	CYS214

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 B 303

Chain	Residue
B	CYS151
B	ILE152
B	GLU153
B	CYS154
B	GLY155
B	CYS157
B	ALA174
B	CYS218

site_id	AC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM C 301

Chain	Residue
C	GLN30
C	SER31
C	GLY34
C	LEU37
C	PHE90
C	HIS93
C	ALA94
C	ALA97
C	LYS100
C	TRP126
C	GLN129
C	GLY133
C	MET136
C	PHE137
C	HIS182
C	GLY183
C	GLY186
C	LEU190
C	LYS193

site_id	AC8
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM C 302

Chain	Residue
C	TYR172
C	LEU175
C	LEU176
C	VAL179
C	GLY224
C	PHE228
C	PHE40
C	MET41
C	HIS44
C	VAL48
C	LEU82
C	ALA83
C	HIS143
C	MET147
C	ILE154
C	SER159
C	ARG162

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE LMT C 303

Chain	Residue
C	MET22
C	PHE95
C	MET98
F	PHE101
F	PRO102
F	TYR105
F	TYR108
F	ALA130
F	MET131

site_id	BC1
Number of Residues	31
Details	BINDING SITE FOR RESIDUE FAD D 701

Chain	Residue
D	GLY12
D	GLY13
D	GLY14
D	LEU15
D	ALA16
D	SER35
D	LEU36
D	SER42
D	HIS43
D	SER44
D	ALA46
D	ALA47
D	GLN48
D	GLY49
D	GLY50
D	ALA181
D	ALA215
D	THR216
D	GLY217
D	THR227
D	ASN228
D	THR235
D	LEU267
D	HIS369
D	TYR370
D	GLU393
D	ARG404
D	GLY407
D	SER409
D	VAL410
D	MLA702

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MLA D 702

Chain	Residue
D	PHE141
D	HIS257
D	LEU267
D	THR269
D	GLU270
D	HIS369
D	ARG404
D	GLY407
D	FAD701

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA D 703

Chain	Residue
D	TYR370
D	SER371
D	MET372
D	GLU393
D	ALA395

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES E 301

Chain	Residue
E	CYS57
E	ARG58
E	GLY60
E	ILE61
E	CYS62
E	GLY63
E	CYS65
E	CYS77

site_id	BC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE F3S E 302

Chain	Residue
E	CYS161
E	THR163
E	CYS208
E	THR210
E	LEU211
E	LEU212
E	ALA213
E	CYS214

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 E 303

Chain	Residue
E	CYS151
E	ILE152
E	GLU153
E	CYS154
E	GLY155
E	CYS157
E	ALA174
E	CYS218

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE LMT F 301

Chain	Residue
C	PHE101
C	PRO102
C	TYR105
C	TYR108
C	ALA130
C	MET131
F	MET22
F	PHE95
F	MET98

site_id	BC8
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM F 302

Chain	Residue
F	GLN30
F	SER31
F	GLY34
F	LEU37
F	PHE90
F	HIS93
F	ALA94
F	ALA97
F	LYS100
F	TRP126
F	GLN129
F	GLY133
F	MET136
F	PHE137
F	HIS182
F	GLY183
F	GLY186
F	LEU190
F	LYS193

site_id	BC9
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM F 303

Chain	Residue
F	PHE40
F	MET41
F	HIS44
F	VAL48
F	LEU82
F	ALA83
F	HIS143
F	MET147
F	ILE154
F	SER159
F	ARG162
F	TYR172
F	LEU175
F	LEU176
F	VAL179
F	GLY224
F	PHE228

site_id	CC1
Number of Residues	31
Details	BINDING SITE FOR RESIDUE FAD G 701

Chain	Residue
G	GLY12
G	GLY13
G	GLY14
G	LEU15
G	ALA16
G	SER35
G	LEU36
G	SER42
G	HIS43
G	SER44
G	ALA46
G	ALA47
G	GLN48
G	GLY49
G	GLY50
G	ALA181
G	ALA215
G	THR216
G	GLY217
G	THR227
G	ASN228
G	THR235
G	LEU267
G	HIS369
G	TYR370
G	GLU393
G	ARG404
G	GLY407
G	SER409
G	VAL410
G	MLA702

site_id	CC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MLA G 702

Chain	Residue
G	PHE141
G	HIS257
G	LEU267
G	THR269
G	GLU270
G	HIS369
G	ARG404
G	GLY407
G	FAD701

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA G 703

Chain	Residue
G	TYR370
G	SER371
G	MET372
G	GLU393
G	ALA395

site_id	CC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES H 301

Chain	Residue
H	CYS57
H	ARG58
H	GLY60
H	ILE61
H	CYS62
H	GLY63
H	CYS65
H	CYS77

site_id	CC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE F3S H 302

Chain	Residue
H	CYS161
H	THR163
H	CYS208
H	THR210
H	LEU211
H	LEU212
H	ALA213
H	CYS214

site_id	CC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 H 303

Chain	Residue
H	CYS151
H	ILE152
H	GLU153
H	CYS154
H	GLY155
H	CYS157
H	ALA174
H	CYS218

site_id	CC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM I 301

Chain	Residue
I	GLN30
I	SER31
I	GLY34
I	LEU37
I	PHE90
I	HIS93
I	ALA94
I	ALA97
I	LYS100
I	TRP126
I	GLN129
I	GLY133
I	MET136
I	PHE137
I	HIS182
I	GLY183
I	GLY186
I	LEU190
I	LYS193

site_id	CC8
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM I 302

Chain	Residue
I	PHE40
I	MET41
I	HIS44
I	VAL48
I	LEU82
I	ALA83
I	HIS143
I	MET147
I	ILE154
I	SER159
I	ARG162
I	TYR172
I	LEU175
I	LEU176
I	VAL179
I	GLY224
I	PHE228

site_id	CC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE LMT I 303

Chain	Residue
I	MET22
I	PHE95
I	MET98
L	PHE101
L	PRO102
L	TYR105
L	TYR108
L	ALA130
L	MET131

site_id	DC1
Number of Residues	31
Details	BINDING SITE FOR RESIDUE FAD J 701

Chain	Residue
J	GLY12
J	GLY13
J	GLY14
J	LEU15
J	ALA16
J	SER35
J	LEU36
J	SER42
J	HIS43
J	SER44
J	ALA46
J	ALA47
J	GLN48
J	GLY49
J	GLY50
J	ALA181
J	ALA215
J	THR216
J	GLY217
J	THR227
J	ASN228
J	THR235
J	LEU267
J	HIS369
J	TYR370
J	GLU393
J	ARG404
J	GLY407
J	SER409
J	VAL410
J	MLA702

site_id	DC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MLA J 702

Chain	Residue
J	PHE141
J	HIS257
J	LEU267
J	THR269
J	GLU270
J	HIS369
J	ARG404
J	GLY407
J	FAD701

site_id	DC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA J 703

Chain	Residue
J	TYR370
J	SER371
J	MET372
J	GLU393
J	ALA395

site_id	DC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES K 301

Chain	Residue
K	CYS57
K	ARG58
K	GLY60
K	ILE61
K	CYS62
K	GLY63
K	CYS65
K	CYS77

site_id	DC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE F3S K 302

Chain	Residue
K	CYS161
K	THR163
K	CYS208
K	THR210
K	LEU211
K	LEU212
K	ALA213
K	CYS214

site_id	DC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 K 303

Chain	Residue
K	CYS151
K	ILE152
K	GLU153
K	CYS154
K	GLY155
K	CYS157
K	ALA174
K	CYS218

site_id	DC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE LMT L 301

Chain	Residue
I	PHE101
I	PRO102
I	TYR105
I	TYR108
I	ALA130
I	MET131
L	MET22
L	PHE95
L	MET98

site_id	DC8
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM L 302

Chain	Residue
L	GLN30
L	SER31
L	GLY34
L	LEU37
L	PHE90
L	HIS93
L	ALA94
L	ALA97
L	LYS100
L	TRP126
L	GLN129
L	GLY133
L	MET136
L	PHE137
L	HIS182
L	GLY183
L	GLY186
L	LEU190
L	LYS193

site_id	DC9
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM L 303

Chain	Residue
L	PHE40
L	MET41
L	HIS44
L	VAL48
L	LEU82
L	ALA83
L	HIS143
L	MET147
L	ILE154
L	SER159
L	ARG162
L	TYR172
L	LEU175
L	LEU176
L	VAL179
L	GLY224
L	PHE228

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. CiECGcCIaACG

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. RSHSaaAqGG

Chain	Residue	Details
A	ARG41-GLY50

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"P00363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	76
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10586875","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11248702","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QLB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10586875","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QLB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Tele-8alpha-FAD histidine","evidences":[{"source":"PubMed","id":"10586875","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11248702","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QLB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	360
Details	Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	116
Details	Domain: {"description":"4Fe-4S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	116
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"10586875","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	444
Details	Transmembrane: {"description":"Helical"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	152
Details	Topological domain: {"description":"Periplasmic"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	168
Details	Topological domain: {"description":"Cytoplasmic"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	16
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10586875","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11248702","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QLB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1d4c

Chain	Residue	Details
A	HIS257
A	ARG404
A	HIS369
A	ARG301

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1d4c

Chain	Residue	Details
D	HIS257
D	ARG404
D	HIS369
D	ARG301

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1d4c

Chain	Residue	Details
G	HIS257
G	ARG404
G	HIS369
G	ARG301

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1d4c

Chain	Residue	Details
J	HIS257
J	ARG404
J	HIS369
J	ARG301

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