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4KX6

Plasticity of the quinone-binding site of the complex II homolog quinol:fumarate reductase

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
B0006099biological_processtricarboxylic acid cycle
B0009055molecular_functionelectron transfer activity
B0016491molecular_functionoxidoreductase activity
B0051536molecular_functioniron-sulfur cluster binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
C0016020cellular_componentmembrane
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
N0006099biological_processtricarboxylic acid cycle
N0009055molecular_functionelectron transfer activity
N0016491molecular_functionoxidoreductase activity
N0051536molecular_functioniron-sulfur cluster binding
N0051537molecular_function2 iron, 2 sulfur cluster binding
O0016020cellular_componentmembrane
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 Residues32
DetailsBINDING SITE FOR RESIDUE FAD A 601
ChainResidue
AGLY11
AHIS44
ATHR45
AALA48
AGLY50
AGLY51
AHIS155
AVAL157
AALA191
ATHR192
AGLY193
AALA12
ATHR203
AASP211
ALEU242
AHIS355
ATYR356
AGLY378
AGLU379
AARG390
ASER393
AASN394
AGLY13
ASER395
ALEU396
ALEU399
AGLY14
AALA15
ASER36
ALYS37
AVAL38
ASER43

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES B 301
ChainResidue
BSER56
BCYS57
BARG58
BCYS62
BGLY63
BCYS65
BCYS77

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE F3S B 302
ChainResidue
BCYS158
BGLN160
BCYS204
BTHR205
BPHE206
BGLY208
BCYS210
BALA221

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SF4 B 303
ChainResidue
BCYS148
BILE149
BCYS151
BGLY152
BCYS154
BCYS214

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MQ7 D 701
ChainResidue
BCYS204
BTHR205
BPHE206
BGLN225
BLYS228
CARG28
DGLU10
DTRP14
DPHE17
DGLY18
DHIS80
DHIS84

site_idAC6
Number of Residues31
DetailsBINDING SITE FOR RESIDUE FAD M 601
ChainResidue
MGLY11
MALA12
MGLY13
MGLY14
MALA15
MSER36
MLYS37
MVAL38
MSER43
MHIS44
MTHR45
MALA48
MGLY50
MGLY51
MPHE156
MVAL157
MALA191
MTHR192
MGLY193
MTHR203
MASP211
MLEU242
MHIS355
MTYR356
MGLU379
MARG390
MSER393
MASN394
MSER395
MLEU396
MLEU399

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES N 301
ChainResidue
NCYS62
NGLY63
NSER64
NCYS65
NCYS77
NSER56
NCYS57
NARG58

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE F3S N 302
ChainResidue
NCYS158
NGLN160
NCYS204
NTHR205
NGLY208
NCYS210
NALA221
NILE224

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SF4 N 303
ChainResidue
NCYS148
NCYS151
NGLY152
NCYS154
NCYS214
NVAL218

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MQ7 N 304
ChainResidue
NCYS204
NTHR205
NGLN225
NLYS228
OARG28
PTRP14
PHIS84

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

site_idSWS_FT_FI2
Number of Residues144
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:10373108
ChainResidueDetails
DSER8-LEU34
MSER43
MHIS155
MASP211
MGLU379
MARG390
DSER60-ASP88
DGLY96-GLY114
PSER8-LEU34
PSER60-ASP88
PGLY96-GLY114
AARG390
MGLY11
MILE35

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

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PDB entries from 2024-07-24

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