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1KFY

QUINOL-FUMARATE REDUCTASE WITH QUINOL INHIBITOR 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL

Functional Information from GO Data
ChainGOidnamespacecontents
A0000104molecular_functionsuccinate dehydrogenase activity
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006113biological_processfermentation
A0006974biological_processDNA damage response
A0008177molecular_functionsuccinate dehydrogenase (quinone) activity
A0009055molecular_functionelectron transfer activity
A0009061biological_processanaerobic respiration
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0019645biological_processanaerobic electron transport chain
A0022900biological_processelectron transport chain
A0044780biological_processbacterial-type flagellum assembly
A0045284cellular_componentobsolete plasma membrane fumarate reductase complex
A0050660molecular_functionflavin adenine dinucleotide binding
A0071949molecular_functionFAD binding
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006099biological_processtricarboxylic acid cycle
B0006113biological_processfermentation
B0008177molecular_functionsuccinate dehydrogenase (quinone) activity
B0009055molecular_functionelectron transfer activity
B0009061biological_processanaerobic respiration
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0019645biological_processanaerobic electron transport chain
B0044780biological_processbacterial-type flagellum assembly
B0045284cellular_componentobsolete plasma membrane fumarate reductase complex
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
C0000104molecular_functionsuccinate dehydrogenase activity
C0005886cellular_componentplasma membrane
C0006113biological_processfermentation
C0009061biological_processanaerobic respiration
C0016020cellular_componentmembrane
C0019645biological_processanaerobic electron transport chain
C0044780biological_processbacterial-type flagellum assembly
C0045284cellular_componentobsolete plasma membrane fumarate reductase complex
D0000104molecular_functionsuccinate dehydrogenase activity
D0005886cellular_componentplasma membrane
D0006106biological_processfumarate metabolic process
D0006113biological_processfermentation
D0009061biological_processanaerobic respiration
D0016020cellular_componentmembrane
D0019645biological_processanaerobic electron transport chain
D0044780biological_processbacterial-type flagellum assembly
D0045284cellular_componentobsolete plasma membrane fumarate reductase complex
M0000104molecular_functionsuccinate dehydrogenase activity
M0000166molecular_functionnucleotide binding
M0005515molecular_functionprotein binding
M0005829cellular_componentcytosol
M0005886cellular_componentplasma membrane
M0006113biological_processfermentation
M0006974biological_processDNA damage response
M0008177molecular_functionsuccinate dehydrogenase (quinone) activity
M0009055molecular_functionelectron transfer activity
M0009061biological_processanaerobic respiration
M0016020cellular_componentmembrane
M0016491molecular_functionoxidoreductase activity
M0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
M0019645biological_processanaerobic electron transport chain
M0022900biological_processelectron transport chain
M0044780biological_processbacterial-type flagellum assembly
M0045284cellular_componentobsolete plasma membrane fumarate reductase complex
M0050660molecular_functionflavin adenine dinucleotide binding
M0071949molecular_functionFAD binding
N0005515molecular_functionprotein binding
N0005829cellular_componentcytosol
N0005886cellular_componentplasma membrane
N0006099biological_processtricarboxylic acid cycle
N0006113biological_processfermentation
N0008177molecular_functionsuccinate dehydrogenase (quinone) activity
N0009055molecular_functionelectron transfer activity
N0009061biological_processanaerobic respiration
N0016020cellular_componentmembrane
N0016491molecular_functionoxidoreductase activity
N0019645biological_processanaerobic electron transport chain
N0044780biological_processbacterial-type flagellum assembly
N0045284cellular_componentobsolete plasma membrane fumarate reductase complex
N0046872molecular_functionmetal ion binding
N0051536molecular_functioniron-sulfur cluster binding
N0051537molecular_function2 iron, 2 sulfur cluster binding
N0051538molecular_function3 iron, 4 sulfur cluster binding
N0051539molecular_function4 iron, 4 sulfur cluster binding
O0000104molecular_functionsuccinate dehydrogenase activity
O0005886cellular_componentplasma membrane
O0006113biological_processfermentation
O0009061biological_processanaerobic respiration
O0016020cellular_componentmembrane
O0019645biological_processanaerobic electron transport chain
O0044780biological_processbacterial-type flagellum assembly
O0045284cellular_componentobsolete plasma membrane fumarate reductase complex
P0000104molecular_functionsuccinate dehydrogenase activity
P0005886cellular_componentplasma membrane
P0006106biological_processfumarate metabolic process
P0006113biological_processfermentation
P0009061biological_processanaerobic respiration
P0016020cellular_componentmembrane
P0019645biological_processanaerobic electron transport chain
P0044780biological_processbacterial-type flagellum assembly
P0045284cellular_componentobsolete plasma membrane fumarate reductase complex
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE OAA A 702
ChainResidue
AGLY50
AHIS232
ALEU242
ATHR244
AGLU245
AHIS355
AARG390
ASER393
AFAD703

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE OAA M 802
ChainResidue
MGLY50
MPHE116
MHIS232
MLEU242
MTHR244
MGLU245
MHIS355
MARG390
MSER393
MFAD803

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES B 244
ChainResidue
BSER56
BCYS57
BARG58
BCYS62
BGLY63
BCYS65
BCYS77

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE F3S B 245
ChainResidue
BCYS158
BGLN160
BCYS204
BTHR205
BPHE206
BVAL207
BGLY208
BTYR209
BCYS210
BILE224

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 B 246
ChainResidue
BCYS148
BILE149
BASN150
BCYS151
BGLY152
BLEU153
BCYS154
BCYS214

site_idAC6
Number of Residues34
DetailsBINDING SITE FOR RESIDUE FAD A 703
ChainResidue
AGLY11
AALA12
AGLY13
AGLY14
AALA15
ASER36
ALYS37
AVAL38
ASER43
AHIS44
ATHR45
AALA48
AGLY50
AGLY51
AHIS155
APHE156
AVAL157
AALA191
ATHR192
AGLY193
ATHR203
AASN204
AASP211
AHIS355
ATYR356
AGLY378
AGLU379
AARG390
ASER393
AASN394
ASER395
ALEU396
ALEU399
AOAA702

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES N 244
ChainResidue
NSER56
NCYS57
NARG58
NCYS62
NGLY63
NCYS65
NCYS77

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE F3S N 245
ChainResidue
NCYS158
NGLN160
NCYS204
NPHE206
NVAL207
NGLY208
NCYS210
NILE224

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 N 246
ChainResidue
NCYS214
NVAL218
NCYS148
NILE149
NASN150
NCYS151
NGLY152
NCYS154

site_idBC1
Number of Residues32
DetailsBINDING SITE FOR RESIDUE FAD M 803
ChainResidue
MGLY11
MALA12
MGLY13
MGLY14
MALA15
MSER36
MLYS37
MVAL38
MSER43
MHIS44
MTHR45
MALA48
MGLU49
MGLY50
MGLY51
MHIS155
MPHE156
MVAL157
MALA191
MTHR192
MGLY193
MTHR203
MASN204
MLEU242
MTYR356
MGLU379
MSER393
MASN394
MSER395
MLEU396
MLEU399
MOAA802

site_idBC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE BRS B 700
ChainResidue
BCYS204
BTHR205
BPHE206
BGLN225
BLYS228
CARG28
CLEU89
DTRP14
DGLY18
DARG81

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CE1 P 810
ChainResidue
BTHR239
DASP9
DTRP76
DCE1710
PASP9
PLYS97
PTRP98
PTYR101

site_idBC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CE1 D 710
ChainResidue
DASP9
DPHE13
DTRP98
DTYR101
DGLY102
PASP9
PPHE13
PTRP76
PCE1810

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CE1 O 811
ChainResidue
DGLY42
DLEU43
DPHE44
DGLY46
OLEU73
OILE74
OALA77

site_idBC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BRS N 800
ChainResidue
NCYS204
NTHR205
NPHE206
NGLN225
NLYS228
OARG28
OLEU89
PTRP14
PGLY18

Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CRMAICGSC
ChainResidueDetails
BCYS57-CYS65

site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiNCGlCYaACP
ChainResidueDetails
BCYS148-PRO159

site_idPS00504
Number of Residues10
DetailsFRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTvaAeGG
ChainResidueDetails
AARG42-GLY51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues26
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:10373108
ChainResidueDetails
DMET0-ARG7
DLEU89-ALA95
PMET0-ARG7
PLEU89-ALA95
OASN65-LEU89
OGLY104-ALA127

site_idSWS_FT_FI2
Number of Residues144
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:10373108
ChainResidueDetails
DSER8-LEU34
BSER211
BPRO215
NARG58
NGLY63
NGLY66
NLYS78
NILE149
NGLY152
NTYR155
NPRO159
DSER60-ASP88
NTHR205
NSER211
NPRO215
DGLY96-GLY114
PSER8-LEU34
PSER60-ASP88
PGLY96-GLY114
BTYR155
BPRO159
BTHR205

site_idSWS_FT_FI3
Number of Residues48
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:10373108
ChainResidueDetails
DVAL35-GLN59
PVAL35-GLN59

site_idSWS_FT_FI4
Number of Residues6
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:10373108, ECO:0000269|PubMed:15919996
ChainResidueDetails
DVAL115-ILE118
PVAL115-ILE118

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1L0V
ChainResidueDetails
DTRP14
PTRP14

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1L0V
ChainResidueDetails
CTRP86
OTRP86

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d4c
ChainResidueDetails
AARG287
AHIS355
AARG390
AHIS232

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d4c
ChainResidueDetails
MARG287
MHIS355
MARG390
MHIS232

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PDB entries from 2024-07-17

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