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3P4P

Crystal structure of Menaquinol:fumarate oxidoreductase in complex with fumarate

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 Residues40
DetailsBINDING SITE FOR RESIDUE FAD A 601
ChainResidue
AGLY11
AHIS44
ATHR45
AALA48
AGLU49
AGLY50
AGLY51
AHIS155
APHE156
AVAL157
AALA191
AALA12
ATHR192
AGLY193
ATHR203
AASN204
AASP211
ALEU242
AHIS355
ATYR356
AGLY378
AGLU379
AGLY13
AARG390
ASER393
AASN394
ASER395
ALEU396
ALEU399
AFUM577
AHOH593
AHOH597
AHOH599
AGLY14
AHOH615
AALA15
ASER36
ALYS37
AVAL38
ASER43

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FUM A 577
ChainResidue
AGLY50
APHE116
AHIS232
ATHR244
AGLU245
AHIS355
AARG390
ASER393
AFAD601

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FES B 244
ChainResidue
BSER56
BCYS57
BARG58
BALA60
BCYS62
BGLY63
BSER64
BCYS65
BCYS77

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE F3S B 245
ChainResidue
BCYS158
BGLN160
BCYS204
BTHR205
BPHE206
BVAL207
BGLY208
BCYS210
BILE224

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SF4 B 246
ChainResidue
BCYS148
BILE149
BCYS151
BGLY152
BCYS154
BCYS214
BPRO220

site_idAC6
Number of Residues35
DetailsBINDING SITE FOR RESIDUE FAD M 601
ChainResidue
MHIS355
MTYR356
MGLY378
MGLU379
MARG390
MSER393
MASN394
MSER395
MLEU396
MLEU399
MVAL10
MGLY11
MALA12
MGLY13
MGLY14
MALA15
MSER36
MLYS37
MVAL38
MSER43
MHIS44
MTHR45
MALA47
MALA48
MGLY50
MGLY51
MPHE156
MVAL157
MALA191
MTHR192
MGLY193
MTHR203
MASN204
MVAL208
MLEU242

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FES N 244
ChainResidue
NLEU37
NSER56
NCYS57
NARG58
NALA60
NCYS62
NGLY63
NCYS65
NCYS77

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE F3S N 245
ChainResidue
NCYS158
NPRO159
NGLN160
NCYS204
NTHR205
NPHE206
NVAL207
NGLY208
NTYR209
NCYS210
NALA221
NILE224

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SF4 N 246
ChainResidue
NCYS148
NILE149
NCYS151
NGLY152
NLEU153
NCYS154
NCYS214

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
BCYS210
BCYS214
NCYS57
NCYS62
NCYS65
NCYS77
NCYS148
NCYS151
NCYS154
NCYS158
DSER60-ASP88
NCYS204
NCYS210
NCYS214
DGLY96-GLY114
PSER8-LEU34
PSER60-ASP88
PGLY96-GLY114
BCYS154
BCYS158
BCYS204

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

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PDB entries from 2024-07-24

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