Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2BS3

GLU C180 -> GLN VARIANT 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	0016020	cellular_component	membrane
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	0005886	cellular_component	plasma membrane
B	0006099	biological_process	tricarboxylic acid cycle
B	0009055	molecular_function	electron transfer activity
B	0009060	biological_process	aerobic respiration
B	0016020	cellular_component	membrane
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	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	0016020	cellular_component	membrane
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	0050660	molecular_function	flavin adenine dinucleotide binding
E	0005886	cellular_component	plasma membrane
E	0006099	biological_process	tricarboxylic acid cycle
E	0009055	molecular_function	electron transfer activity
E	0009060	biological_process	aerobic respiration
E	0016020	cellular_component	membrane
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	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A1658

Chain	Residue
A	SER371
A	MET372
A	GLY373
A	GLU393
A	ALA395
A	HOH2156

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA D1658

Chain	Residue
D	GLU393
D	ALA395
D	HOH2162
D	SER371
D	MET372
D	GLY373

site_id	AC3
Number of Residues	37
Details	BINDING SITE FOR RESIDUE FAD A1656

Chain	Residue
A	GLY12
A	GLY13
A	GLY14
A	LEU15
A	ALA16
A	SER35
A	LEU36
A	ILE37
A	SER42
A	HIS43
A	SER44
A	ALA47
A	GLY49
A	GLY50
A	LYS179
A	ALA181
A	ALA215
A	THR216
A	GLY217
A	THR227
A	ASN228
A	THR235
A	HIS369
A	TYR370
A	GLY392
A	GLU393
A	ARG404
A	GLY407
A	ASN408
A	SER409
A	VAL410
A	CIT1657
A	HOH2269
A	HOH2270
A	HOH2271
A	HOH2272
A	HOH2273

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CIT A1657

Chain	Residue
A	ALA46
A	GLN48
A	GLY49
A	PHE141
A	GLN255
A	HIS257
A	LEU267
A	THR269
A	GLU270
A	ARG301
A	HIS369
A	ARG404
A	GLY406
A	FAD1656
A	HOH2274

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES B1240

Chain	Residue
B	VAL56
B	CYS57
B	ARG58
B	GLY60
B	ILE61
B	CYS62
B	GLY63
B	CYS65
B	CYS77

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE F3S B1241

Chain	Residue
B	CYS161
B	THR163
B	CYS208
B	MET209
B	THR210
B	LEU211
B	LEU212
B	ALA213
B	CYS214

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 B1242

Chain	Residue
B	CYS151
B	ILE152
B	GLU153
B	CYS154
B	GLY155
B	CYS157
B	CYS218
B	PRO219
B	LYS220

site_id	AC8
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM C1255

Chain	Residue
C	ALA97
C	LYS100
C	PHE101
C	TRP126
C	GLY133
C	MET136
C	PHE137
C	HIS182
C	GLY186
C	LEU190
C	LYS193
C	HEM1256
C	HOH2046
C	HOH2047
B	HOH2142
C	GLN30
C	SER31
C	GLY34
C	LEU37
C	PHE90
C	HIS93
C	ALA94

site_id	AC9
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM C1256

Chain	Residue
C	PHE40
C	MET41
C	HIS44
C	LEU82
C	ALA83
C	HIS143
C	MET147
C	ILE154
C	SER159
C	ARG162
C	TYR172
C	LEU176
C	GLY224
C	PHE228
C	HEM1255

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE LMT C1257

Chain	Residue
C	PHE101
C	PRO102
C	ASN104
C	TYR108
C	MET131
F	PHE95
F	MET98
F	ARG99

site_id	BC2
Number of Residues	38
Details	BINDING SITE FOR RESIDUE FAD D1656

Chain	Residue
D	GLY12
D	GLY13
D	GLY14
D	LEU15
D	ALA16
D	SER35
D	LEU36
D	ILE37
D	SER42
D	HIS43
D	SER44
D	ALA47
D	GLY49
D	GLY50
D	LYS179
D	GLU180
D	ALA181
D	ALA215
D	THR216
D	GLY217
D	THR227
D	ASN228
D	THR235
D	HIS369
D	TYR370
D	GLY392
D	GLU393
D	ARG404
D	GLY407
D	ASN408
D	SER409
D	VAL410
D	CIT1657
D	HOH2128
D	HOH2285
D	HOH2286
D	HOH2287
D	HOH2288

site_id	BC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CIT D1657

Chain	Residue
D	ALA46
D	GLN48
D	GLY49
D	PHE141
D	GLN255
D	HIS257
D	LEU267
D	THR269
D	GLU270
D	ARG301
D	HIS369
D	ARG404
D	FAD1656
D	HOH2289
D	HOH2291

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES E1240

Chain	Residue
E	VAL56
E	CYS57
E	ARG58
E	GLY60
E	ILE61
E	CYS62
E	GLY63
E	CYS65
E	CYS77

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE F3S E1241

Chain	Residue
E	CYS161
E	THR163
E	CYS208
E	MET209
E	THR210
E	LEU211
E	LEU212
E	ALA213
E	CYS214

site_id	BC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 E1242

Chain	Residue
E	CYS151
E	ILE152
E	GLU153
E	CYS154
E	GLY155
E	CYS157
E	CYS218
E	PRO219
E	LYS220

site_id	BC7
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM F1255

Chain	Residue
F	GLN30
F	SER31
F	GLY34
F	LEU37
F	PHE90
F	HIS93
F	ALA94
F	ALA97
F	LYS100
F	PHE101
F	TRP126
F	GLY133
F	MET136
F	PHE137
F	VAL179
F	HIS182
F	GLY186
F	LEU190
F	LYS193
F	HEM1256
F	HOH2057
F	HOH2058
F	HOH2059

site_id	BC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM F1256

Chain	Residue
F	PHE40
F	MET41
F	HIS44
F	LEU82
F	ALA83
F	HIS143
F	MET147
F	ILE154
F	SER159
F	ARG162
F	TYR172
F	LEU176
F	GLY224
F	PHE228
F	HEM1255

site_id	BC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE LMT F1257

Chain	Residue
C	LEU26
C	PHE95
C	MET98
C	ARG99
F	PHE101
F	PRO102
F	ASN104
F	TYR108
F	MET131

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	4
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"P00363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	38
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	2
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	2
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	180
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	58
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	58
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"10586875","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	222
Details	Transmembrane: {"description":"Helical"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	76
Details	Topological domain: {"description":"Periplasmic"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	84
Details	Topological domain: {"description":"Cytoplasmic"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	8
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

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