Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6AWF

Escherichia coli quinol:fumarate reductase crystallized without dicarboxylate

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	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	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	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	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
E	0000104	molecular_function	succinate dehydrogenase activity
E	0000166	molecular_function	nucleotide binding
E	0005515	molecular_function	protein binding
E	0005829	cellular_component	cytosol
E	0005886	cellular_component	plasma membrane
E	0006974	biological_process	DNA damage response
E	0008177	molecular_function	succinate dehydrogenase (quinone) activity
E	0009055	molecular_function	electron transfer activity
E	0009061	biological_process	anaerobic respiration
E	0016020	cellular_component	membrane
E	0016491	molecular_function	oxidoreductase activity
E	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
E	0019645	biological_process	anaerobic electron transport chain
E	0022900	biological_process	electron transport chain
E	0044780	biological_process	bacterial-type flagellum assembly
E	0045283	cellular_component	fumarate reductase complex
E	0050660	molecular_function	flavin adenine dinucleotide binding
E	0071949	molecular_function	FAD binding
F	0005515	molecular_function	protein binding
F	0005829	cellular_component	cytosol
F	0005886	cellular_component	plasma membrane
F	0006099	biological_process	tricarboxylic acid cycle
F	0008177	molecular_function	succinate dehydrogenase (quinone) activity
F	0009055	molecular_function	electron transfer activity
F	0009061	biological_process	anaerobic respiration
F	0016020	cellular_component	membrane
F	0016491	molecular_function	oxidoreductase activity
F	0019645	biological_process	anaerobic electron transport chain
F	0044780	biological_process	bacterial-type flagellum assembly
F	0045283	cellular_component	fumarate reductase complex
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	0000104	molecular_function	succinate dehydrogenase activity
G	0005886	cellular_component	plasma membrane
G	0009061	biological_process	anaerobic respiration
G	0016020	cellular_component	membrane
G	0019645	biological_process	anaerobic electron transport chain
G	0044780	biological_process	bacterial-type flagellum assembly
G	0045283	cellular_component	fumarate reductase complex
H	0000104	molecular_function	succinate dehydrogenase activity
H	0005886	cellular_component	plasma membrane
H	0006106	biological_process	fumarate metabolic process
H	0009061	biological_process	anaerobic respiration
H	0016020	cellular_component	membrane
H	0019645	biological_process	anaerobic electron transport chain
H	0044780	biological_process	bacterial-type flagellum assembly
H	0045283	cellular_component	fumarate reductase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	32
Details	binding site for residue FAD A 701

Chain	Residue
A	VAL10
A	SER43
A	HIS44
A	THR45
A	ALA47
A	ALA48
A	GLY50
A	GLY51
A	VAL157
A	ALA191
A	THR192
A	GLY11
A	GLY193
A	THR203
A	ASN204
A	ASP211
A	LEU242
A	HIS355
A	TYR356
A	GLU379
A	ARG390
A	SER393
A	ALA12
A	SER395
A	LEU396
A	LEU399
A	GLY13
A	GLY14
A	ALA15
A	SER36
A	LYS37
A	VAL38

site_id	AC2
Number of Residues	4
Details	binding site for residue PO4 A 702

Chain	Residue
A	GLN230
A	HIS232
A	PRO233
A	ARG390

site_id	AC3
Number of Residues	6
Details	binding site for residue FES B 301

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

site_id	AC4
Number of Residues	6
Details	binding site for residue F3S B 302

Chain	Residue
B	CYS158
B	CYS204
B	THR205
B	PHE206
B	CYS210
B	ALA221

site_id	AC5
Number of Residues	6
Details	binding site for residue SF4 B 303

Chain	Residue
B	CYS148
B	ILE149
B	CYS151
B	CYS154
B	ALA171
B	CYS214

site_id	AC6
Number of Residues	6
Details	binding site for residue PO4 E 702

Chain	Residue
E	PHE116
E	HIS232
E	HIS355
E	ARG390
E	GLY392
E	SER393

site_id	AC7
Number of Residues	7
Details	binding site for residue FES F 301

Chain	Residue
F	SER56
F	CYS57
F	ALA60
F	CYS62
F	GLY63
F	CYS65
F	CYS77

site_id	AC8
Number of Residues	8
Details	binding site for residue F3S F 302

Chain	Residue
F	CYS158
F	GLN160
F	PRO170
F	CYS204
F	THR205
F	PHE206
F	CYS210
F	ALA221

site_id	AC9
Number of Residues	6
Details	binding site for residue SF4 F 303

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

site_id	AD1
Number of Residues	34
Details	binding site for Di-peptide FAD E 701 and HIS E 44

Chain	Residue
E	PHE156
E	VAL157
E	ALA191
E	THR192
E	GLY193
E	ASN204
E	GLY205
E	ASP211
E	LEU242
E	TYR356
E	GLU379
E	ARG390
E	SER393
E	SER395
E	LEU396
E	LEU399
E	GLY11
E	ALA12
E	GLY13
E	GLY14
E	ALA15
E	SER36
E	LYS37
E	VAL38
E	ARG42
E	SER43
E	THR45
E	VAL46
E	ALA47
E	ALA48
E	GLU49
E	GLY50
E	GLY51
E	HIS155

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	3
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	30
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P0AC47","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	120
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00708","evidenceCode":"ECO:0000255"}]}

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	7
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	2
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_FI15
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PDB","id":"1L0V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	100
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00709","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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