Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1KF6

E. coli Quinol-Fumarate Reductase with Bound Inhibitor HQNO

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000104	molecular_function	succinate dehydrogenase activity
A	0000166	molecular_function	nucleotide binding
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006113	biological_process	fermentation
A	0006974	biological_process	DNA damage response
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	0019645	biological_process	anaerobic electron transport chain
A	0022900	biological_process	electron transport chain
A	0044780	biological_process	bacterial-type flagellum assembly
A	0045283	cellular_component	fumarate reductase complex
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0071949	molecular_function	FAD binding
B	0005515	molecular_function	protein binding
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006099	biological_process	tricarboxylic acid cycle
B	0006113	biological_process	fermentation
B	0008177	molecular_function	succinate dehydrogenase (quinone) activity
B	0009055	molecular_function	electron transfer activity
B	0009061	biological_process	anaerobic respiration
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0019645	biological_process	anaerobic electron transport chain
B	0044780	biological_process	bacterial-type flagellum assembly
B	0045283	cellular_component	fumarate reductase complex
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	0000104	molecular_function	succinate dehydrogenase activity
C	0005886	cellular_component	plasma membrane
C	0006113	biological_process	fermentation
C	0009061	biological_process	anaerobic respiration
C	0016020	cellular_component	membrane
C	0019645	biological_process	anaerobic electron transport chain
C	0044780	biological_process	bacterial-type flagellum assembly
C	0045283	cellular_component	fumarate reductase complex
D	0000104	molecular_function	succinate dehydrogenase activity
D	0005886	cellular_component	plasma membrane
D	0006106	biological_process	fumarate metabolic process
D	0006113	biological_process	fermentation
D	0009061	biological_process	anaerobic respiration
D	0016020	cellular_component	membrane
D	0019645	biological_process	anaerobic electron transport chain
D	0044780	biological_process	bacterial-type flagellum assembly
D	0045283	cellular_component	fumarate reductase complex
M	0000104	molecular_function	succinate dehydrogenase activity
M	0000166	molecular_function	nucleotide binding
M	0005515	molecular_function	protein binding
M	0005829	cellular_component	cytosol
M	0005886	cellular_component	plasma membrane
M	0006113	biological_process	fermentation
M	0006974	biological_process	DNA damage response
M	0008177	molecular_function	succinate dehydrogenase (quinone) activity
M	0009055	molecular_function	electron transfer activity
M	0009061	biological_process	anaerobic respiration
M	0016020	cellular_component	membrane
M	0016491	molecular_function	oxidoreductase activity
M	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
M	0019645	biological_process	anaerobic electron transport chain
M	0022900	biological_process	electron transport chain
M	0044780	biological_process	bacterial-type flagellum assembly
M	0045283	cellular_component	fumarate reductase complex
M	0050660	molecular_function	flavin adenine dinucleotide binding
M	0071949	molecular_function	FAD binding
N	0005515	molecular_function	protein binding
N	0005829	cellular_component	cytosol
N	0005886	cellular_component	plasma membrane
N	0006099	biological_process	tricarboxylic acid cycle
N	0006113	biological_process	fermentation
N	0008177	molecular_function	succinate dehydrogenase (quinone) activity
N	0009055	molecular_function	electron transfer activity
N	0009061	biological_process	anaerobic respiration
N	0016020	cellular_component	membrane
N	0016491	molecular_function	oxidoreductase activity
N	0019645	biological_process	anaerobic electron transport chain
N	0044780	biological_process	bacterial-type flagellum assembly
N	0045283	cellular_component	fumarate reductase complex
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	0000104	molecular_function	succinate dehydrogenase activity
O	0005886	cellular_component	plasma membrane
O	0006113	biological_process	fermentation
O	0009061	biological_process	anaerobic respiration
O	0016020	cellular_component	membrane
O	0019645	biological_process	anaerobic electron transport chain
O	0044780	biological_process	bacterial-type flagellum assembly
O	0045283	cellular_component	fumarate reductase complex
P	0000104	molecular_function	succinate dehydrogenase activity
P	0005886	cellular_component	plasma membrane
P	0006106	biological_process	fumarate metabolic process
P	0006113	biological_process	fermentation
P	0009061	biological_process	anaerobic respiration
P	0016020	cellular_component	membrane
P	0019645	biological_process	anaerobic electron transport chain
P	0044780	biological_process	bacterial-type flagellum assembly
P	0045283	cellular_component	fumarate reductase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K A 720

Chain	Residue
A	THR357
A	MET358
A	GLY359
A	GLU379
A	SER381

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K M 820

Chain	Residue
M	SER381
M	THR357
M	MET358
M	GLY359
M	GLU379

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE OAA A 702

Chain	Residue
A	HIS232
A	LEU242
A	THR244
A	GLU245
A	HIS355
A	ARG390
A	GLY392
A	SER393
A	FAD721

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT A 703

Chain	Residue
A	ASP556
A	ARG562
A	GLU564

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT B 704

Chain	Residue
A	ARG452
B	GLY41
B	ASP45

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE OAA M 802

Chain	Residue
M	PHE116
M	HIS232
M	LEU242
M	THR244
M	GLU245
M	ARG287
M	HIS355
M	ARG390
M	SER393
M	FAD821

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT N 803

Chain	Residue
M	TRP448
M	ARG452
N	GLY41
N	ASP45
N	TYR53
N	TRP55

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES B 244

Chain	Residue
B	SER56
B	CYS57
B	ARG58
B	CYS62
B	GLY63
B	CYS65
B	CYS77

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE F3S B 245

Chain	Residue
B	CYS158
B	GLN160
B	CYS204
B	THR205
B	PHE206
B	VAL207
B	GLY208
B	TYR209
B	CYS210
B	ILE224

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SF4 B 246

Chain	Residue
B	CYS148
B	ILE149
B	CYS151
B	GLY152
B	CYS154
B	CYS214

site_id	BC2
Number of Residues	32
Details	BINDING SITE FOR RESIDUE FAD A 721

Chain	Residue
A	GLY11
A	ALA12
A	GLY14
A	ALA15
A	SER36
A	LYS37
A	VAL38
A	SER43
A	HIS44
A	THR45
A	ALA48
A	GLU49
A	GLY50
A	GLY51
A	HIS155
A	VAL157
A	ALA191
A	THR192
A	GLY193
A	THR203
A	ASN204
A	ASP211
A	HIS355
A	TYR356
A	GLU379
A	ARG390
A	SER393
A	ASN394
A	SER395
A	LEU396
A	LEU399
A	OAA702

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES N 244

Chain	Residue
N	CYS62
N	GLY63
N	CYS65
N	CYS77
N	SER56
N	CYS57
N	ARG58

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE F3S N 245

Chain	Residue
N	CYS158
N	GLN160
N	CYS204
N	THR205
N	PHE206
N	VAL207
N	GLY208
N	CYS210
N	ILE224

site_id	BC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 N 246

Chain	Residue
N	CYS148
N	ILE149
N	ASN150
N	CYS151
N	GLY152
N	CYS154
N	CYS214
N	VAL218

site_id	BC6
Number of Residues	36
Details	BINDING SITE FOR RESIDUE FAD M 821

Chain	Residue
M	GLY11
M	ALA12
M	GLY13
M	GLY14
M	ALA15
M	SER36
M	LYS37
M	VAL38
M	SER43
M	HIS44
M	THR45
M	ALA48
M	GLU49
M	GLY50
M	GLY51
M	HIS155
M	PHE156
M	VAL157
M	ALA191
M	THR192
M	GLY193
M	THR203
M	ASN204
M	ASP211
M	LEU242
M	HIS355
M	TYR356
M	GLY378
M	GLU379
M	ARG390
M	SER393
M	ASN394
M	SER395
M	LEU396
M	LEU399
M	OAA802

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE HQO C 700

Chain	Residue
B	THR205
B	PHE206
B	GLN225
B	LYS228
C	ARG28
C	GLU29
D	TRP14
D	PHE17
D	HIS80

site_id	BC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CE1 P 710

Chain	Residue
B	THR239
D	TRP76
P	ASP9
P	LYS97
P	TRP98
P	TYR101
P	GLY102
P	CE1810

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CE1 P 810

Chain	Residue
D	ASP9
D	TRP98
P	ASP9
P	PHE13
P	TRP76
P	CE1710

site_id	CC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CE1 O 811

Chain	Residue
C	TYR129
D	LEU43
D	PHE44
D	PRO45
D	GLY46
O	LEU73
O	CE1813

site_id	CC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CE1 O 812

Chain	Residue
C	VAL98
C	PRO107
C	SER111
C	ALA114
C	VAL118
O	LEU124
O	TYR129
P	PRO45

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CE1 O 813

Chain	Residue
C	TYR129
O	ARG23
O	PHE24
O	GLY30
O	CE1811

site_id	CC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 1PE A 705

Chain	Residue
A	GLY72
A	ARG287
A	ASP288
A	LYS289
A	GLN292
A	TYR466
A	GLN533

site_id	CC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE HQO N 800

Chain	Residue
N	THR205
N	PHE206
N	GLN225
N	LYS228
O	ARG28
O	GLU29
P	TRP14
P	PHE17
P	ARG81

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. CRMAICGSC

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. CiNCGlCYaACP

Chain	Residue	Details
B	CYS148-PRO159

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

Chain	Residue	Details
A	ARG42-GLY51

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"evidences":[{"source":"PubMed","id":"1856194","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"PDB","id":"1KF6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1L0V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PDB","id":"1KF6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PDB","id":"2B76","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CIR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Tele-8alpha-FAD histidine","evidences":[{"source":"PubMed","id":"10373108","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1L0V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	162
Details	Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
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_FI8
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10373108","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1L0V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10373108","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KF6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1L0V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	292
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"10373108","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	78
Details	Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"10373108","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	52
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"10373108","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	10
Details	Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"10373108","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PDB","id":"1L0V","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	ARG287
A	HIS355
A	ARG390
A	HIS232

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

Chain	Residue	Details
M	ARG287
M	HIS355
M	ARG390
M	HIS232

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