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6WU6

succinate-coenzyme Q reductase

Functional Information from GO Data
ChainGOidnamespacecontents
A0006099biological_processtricarboxylic acid cycle
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0022900biological_processelectron transport chain
A0050660molecular_functionflavin adenine dinucleotide binding
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0006099biological_processtricarboxylic acid cycle
B0008177molecular_functionsuccinate dehydrogenase (quinone) activity
B0009055molecular_functionelectron transfer activity
B0009060biological_processaerobic respiration
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0019646biological_processaerobic electron transport chain
B0022904biological_processrespiratory electron transport chain
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
B0051538molecular_function3 iron, 4 sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
C0005886cellular_componentplasma membrane
C0006099biological_processtricarboxylic acid cycle
C0008177molecular_functionsuccinate dehydrogenase (quinone) activity
C0009055molecular_functionelectron transfer activity
C0009060biological_processaerobic respiration
C0016020cellular_componentmembrane
C0017004biological_processcytochrome complex assembly
C0019646biological_processaerobic electron transport chain
C0020037molecular_functionheme binding
C0046872molecular_functionmetal ion binding
C0048039molecular_functionubiquinone binding
D0006099biological_processtricarboxylic acid cycle
D0016020cellular_componentmembrane
D0020037molecular_functionheme binding
E0006099biological_processtricarboxylic acid cycle
E0016491molecular_functionoxidoreductase activity
E0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
E0022900biological_processelectron transport chain
E0050660molecular_functionflavin adenine dinucleotide binding
F0005515molecular_functionprotein binding
F0005886cellular_componentplasma membrane
F0006099biological_processtricarboxylic acid cycle
F0008177molecular_functionsuccinate dehydrogenase (quinone) activity
F0009055molecular_functionelectron transfer activity
F0009060biological_processaerobic respiration
F0016020cellular_componentmembrane
F0016491molecular_functionoxidoreductase activity
F0019646biological_processaerobic electron transport chain
F0022904biological_processrespiratory electron transport chain
F0046872molecular_functionmetal ion binding
F0051536molecular_functioniron-sulfur cluster binding
F0051537molecular_function2 iron, 2 sulfur cluster binding
F0051538molecular_function3 iron, 4 sulfur cluster binding
F0051539molecular_function4 iron, 4 sulfur cluster binding
G0005886cellular_componentplasma membrane
G0006099biological_processtricarboxylic acid cycle
G0008177molecular_functionsuccinate dehydrogenase (quinone) activity
G0009055molecular_functionelectron transfer activity
G0009060biological_processaerobic respiration
G0016020cellular_componentmembrane
G0017004biological_processcytochrome complex assembly
G0019646biological_processaerobic electron transport chain
G0020037molecular_functionheme binding
G0046872molecular_functionmetal ion binding
G0048039molecular_functionubiquinone binding
H0006099biological_processtricarboxylic acid cycle
H0016020cellular_componentmembrane
H0020037molecular_functionheme binding
I0006099biological_processtricarboxylic acid cycle
I0016491molecular_functionoxidoreductase activity
I0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
I0022900biological_processelectron transport chain
I0050660molecular_functionflavin adenine dinucleotide binding
J0005515molecular_functionprotein binding
J0005886cellular_componentplasma membrane
J0006099biological_processtricarboxylic acid cycle
J0008177molecular_functionsuccinate dehydrogenase (quinone) activity
J0009055molecular_functionelectron transfer activity
J0009060biological_processaerobic respiration
J0016020cellular_componentmembrane
J0016491molecular_functionoxidoreductase activity
J0019646biological_processaerobic electron transport chain
J0022904biological_processrespiratory electron transport chain
J0046872molecular_functionmetal ion binding
J0051536molecular_functioniron-sulfur cluster binding
J0051537molecular_function2 iron, 2 sulfur cluster binding
J0051538molecular_function3 iron, 4 sulfur cluster binding
J0051539molecular_function4 iron, 4 sulfur cluster binding
K0005886cellular_componentplasma membrane
K0006099biological_processtricarboxylic acid cycle
K0008177molecular_functionsuccinate dehydrogenase (quinone) activity
K0009055molecular_functionelectron transfer activity
K0009060biological_processaerobic respiration
K0016020cellular_componentmembrane
K0017004biological_processcytochrome complex assembly
K0019646biological_processaerobic electron transport chain
K0020037molecular_functionheme binding
K0046872molecular_functionmetal ion binding
K0048039molecular_functionubiquinone binding
L0006099biological_processtricarboxylic acid cycle
L0016020cellular_componentmembrane
L0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue FES B 301
ChainResidue
BSER54
BCYS75
BCYS55
BARG56
BGLY58
BVAL59
BCYS60
BGLY61
BSER62
BASP63

site_idAC2
Number of Residues8
Detailsbinding site for residue SF4 B 302
ChainResidue
BCYS149
BILE150
BCYS152
BALA153
BCYS155
BCYS216
BPRO217
BLEU220

site_idAC3
Number of Residues9
Detailsbinding site for residue F3S B 303
ChainResidue
BCYS159
BSER161
BPHE169
BCYS206
BSER208
BILE209
BMET210
BASN211
BCYS212

site_idAC4
Number of Residues9
Detailsbinding site for residue HEM C 201
ChainResidue
CHIS30
CGLY34
CHIS84
CVAL85
DALA23
DTHR27
DILE30
DHIS71
DGLY75

site_idAC5
Number of Residues10
Detailsbinding site for residue FES F 301
ChainResidue
FSER54
FCYS55
FARG56
FGLY58
FVAL59
FCYS60
FGLY61
FSER62
FASP63
FCYS75

site_idAC6
Number of Residues8
Detailsbinding site for residue SF4 F 302
ChainResidue
FCYS149
FILE150
FCYS152
FALA153
FCYS155
FCYS216
FPRO217
FLEU220

site_idAC7
Number of Residues9
Detailsbinding site for residue F3S F 303
ChainResidue
FCYS159
FSER161
FPHE169
FCYS206
FSER208
FILE209
FMET210
FASN211
FCYS212

site_idAC8
Number of Residues9
Detailsbinding site for residue HEM G 201
ChainResidue
GHIS30
GGLY34
GHIS84
GVAL85
HALA23
HTHR27
HILE30
HHIS71
HGLY75

site_idAC9
Number of Residues10
Detailsbinding site for residue FES J 301
ChainResidue
JSER54
JCYS55
JARG56
JGLY58
JVAL59
JCYS60
JGLY61
JSER62
JASP63
JCYS75

site_idAD1
Number of Residues8
Detailsbinding site for residue SF4 J 302
ChainResidue
JCYS149
JILE150
JCYS152
JALA153
JCYS155
JCYS216
JPRO217
JLEU220

site_idAD2
Number of Residues9
Detailsbinding site for residue F3S J 303
ChainResidue
JCYS159
JSER161
JPHE169
JCYS206
JSER208
JILE209
JMET210
JASN211
JCYS212

site_idAD3
Number of Residues9
Detailsbinding site for residue HEM K 201
ChainResidue
KHIS30
KGLY34
KHIS84
KVAL85
LALA23
LTHR27
LILE30
LHIS71
LGLY75

site_idAD4
Number of Residues25
Detailsbinding site for residue FAD A 601
ChainResidue
AILE13
AGLY14
AALA15
AGLY16
AGLY17
AALA18
AVAL39
ASER44
ATHR46
ASER48
AALA49
AGLN50
ATYR165
ATHR202
AILE217
ATHR219
AASP221
AHIS354
AGLU388
AARG399
AGLY402
AASN403
ASER404
ALEU405
ALEU408

site_idAD5
Number of Residues3
Detailsbinding site for residue NA A 602
ChainResidue
AMET356
AGLY358
AGLY359

site_idAD6
Number of Residues25
Detailsbinding site for residue FAD E 601
ChainResidue
EILE13
EGLY14
EALA15
EGLY16
EGLY17
EALA18
EVAL39
ESER44
ETHR46
ESER48
EALA49
EGLN50
ETYR165
ETHR202
EILE217
ETHR219
EASP221
EHIS354
EGLU388
EARG399
EGLY402
EASN403
ESER404
ELEU405
ELEU408

site_idAD7
Number of Residues3
Detailsbinding site for residue NA E 602
ChainResidue
EMET356
EGLY358
EGLY359

site_idAD8
Number of Residues25
Detailsbinding site for residue FAD I 601
ChainResidue
IILE13
IGLY14
IALA15
IGLY16
IGLY17
IALA18
IVAL39
ISER44
ITHR46
ISER48
IALA49
IGLN50
ITYR165
ITHR202
IILE217
ITHR219
IASP221
IHIS354
IGLU388
IARG399
IGLY402
IASN403
ISER404
ILEU405
ILEU408

site_idAD9
Number of Residues3
Detailsbinding site for residue NA I 602
ChainResidue
IMET356
IGLY358
IGLY359

Functional Information from PROSITE/UniProt
site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiLCAcCStSCP
ChainResidueDetails
BCYS149-PRO160

site_idPS00504
Number of Residues10
DetailsFRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTvsAqGG
ChainResidueDetails
AARG43-GLY52

site_idPS01000
Number of Residues25
DetailsSDH_CYT_1 Succinate dehydrogenase cytochrome b subunit signature 1. RPVnldLqtirfpItaiaSilHRvS
ChainResidueDetails
CARG9-SER33

site_idPS01001
Number of Residues14
DetailsSDH_CYT_2 Succinate dehydrogenase cytochrome b subunit signature 2. HvvvGIRHMmMDfG
ChainResidueDetails
CHIS84-GLY97

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues267
DetailsDomain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues90
DetailsDomain: {"description":"4Fe-4S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues30
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12560550","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues195
DetailsTransmembrane: {"description":"Helical"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues45
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues54
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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