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3VRB

Mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum with the specific inhibitor flutolanil and substrate fumarate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0006099biological_processtricarboxylic acid cycle
A0006121biological_processmitochondrial electron transport, succinate to ubiquinone
A0008177molecular_functionsuccinate dehydrogenase (quinone) activity
A0009055molecular_functionelectron transfer activity
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0022900biological_processelectron transport chain
A0031966cellular_componentmitochondrial membrane
A0045273cellular_componentrespiratory chain complex II (succinate dehydrogenase)
A0050660molecular_functionflavin adenine dinucleotide binding
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0006099biological_processtricarboxylic acid cycle
B0006121biological_processmitochondrial electron transport, succinate to ubiquinone
B0008177molecular_functionsuccinate dehydrogenase (quinone) activity
B0009055molecular_functionelectron transfer activity
B0009060biological_processaerobic respiration
B0016491molecular_functionoxidoreductase activity
B0022904biological_processrespiratory electron transport chain
B0031966cellular_componentmitochondrial membrane
B0045273cellular_componentrespiratory chain complex II (succinate dehydrogenase)
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
C0005515molecular_functionprotein binding
C0005739cellular_componentmitochondrion
C0005743cellular_componentmitochondrial inner membrane
C0006099biological_processtricarboxylic acid cycle
C0006121biological_processmitochondrial electron transport, succinate to ubiquinone
C0009055molecular_functionelectron transfer activity
C0016020cellular_componentmembrane
C0020037molecular_functionheme binding
C0031966cellular_componentmitochondrial membrane
C0045273cellular_componentrespiratory chain complex II (succinate dehydrogenase)
C0046872molecular_functionmetal ion binding
D0005515molecular_functionprotein binding
D0005739cellular_componentmitochondrion
D0005740cellular_componentmitochondrial envelope
D0005743cellular_componentmitochondrial inner membrane
D0006099biological_processtricarboxylic acid cycle
D0006121biological_processmitochondrial electron transport, succinate to ubiquinone
D0016020cellular_componentmembrane
D0020037molecular_functionheme binding
D0031966cellular_componentmitochondrial membrane
D0045273cellular_componentrespiratory chain complex II (succinate dehydrogenase)
D0046872molecular_functionmetal ion binding
D0048039molecular_functionubiquinone binding
E0000166molecular_functionnucleotide binding
E0005515molecular_functionprotein binding
E0005739cellular_componentmitochondrion
E0005743cellular_componentmitochondrial inner membrane
E0006099biological_processtricarboxylic acid cycle
E0006121biological_processmitochondrial electron transport, succinate to ubiquinone
E0008177molecular_functionsuccinate dehydrogenase (quinone) activity
E0009055molecular_functionelectron transfer activity
E0016491molecular_functionoxidoreductase activity
E0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
E0022900biological_processelectron transport chain
E0031966cellular_componentmitochondrial membrane
E0045273cellular_componentrespiratory chain complex II (succinate dehydrogenase)
E0050660molecular_functionflavin adenine dinucleotide binding
F0005515molecular_functionprotein binding
F0005739cellular_componentmitochondrion
F0005743cellular_componentmitochondrial inner membrane
F0006099biological_processtricarboxylic acid cycle
F0006121biological_processmitochondrial electron transport, succinate to ubiquinone
F0008177molecular_functionsuccinate dehydrogenase (quinone) activity
F0009055molecular_functionelectron transfer activity
F0009060biological_processaerobic respiration
F0016491molecular_functionoxidoreductase activity
F0022904biological_processrespiratory electron transport chain
F0031966cellular_componentmitochondrial membrane
F0045273cellular_componentrespiratory chain complex II (succinate dehydrogenase)
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
G0005515molecular_functionprotein binding
G0005739cellular_componentmitochondrion
G0005743cellular_componentmitochondrial inner membrane
G0006099biological_processtricarboxylic acid cycle
G0006121biological_processmitochondrial electron transport, succinate to ubiquinone
G0009055molecular_functionelectron transfer activity
G0016020cellular_componentmembrane
G0020037molecular_functionheme binding
G0031966cellular_componentmitochondrial membrane
G0045273cellular_componentrespiratory chain complex II (succinate dehydrogenase)
G0046872molecular_functionmetal ion binding
H0005515molecular_functionprotein binding
H0005739cellular_componentmitochondrion
H0005740cellular_componentmitochondrial envelope
H0005743cellular_componentmitochondrial inner membrane
H0006099biological_processtricarboxylic acid cycle
H0006121biological_processmitochondrial electron transport, succinate to ubiquinone
H0016020cellular_componentmembrane
H0020037molecular_functionheme binding
H0031966cellular_componentmitochondrial membrane
H0045273cellular_componentrespiratory chain complex II (succinate dehydrogenase)
H0046872molecular_functionmetal ion binding
H0048039molecular_functionubiquinone binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FUM A 701
ChainResidue
AGLY85
AHIS276
ATHR288
AGLU289
AARG320
AHIS387
AARG432
AALA435
AFAD702

site_idAC2
Number of Residues33
DetailsBINDING SITE FOR RESIDUE FAD A 702
ChainResidue
AGLY48
AALA49
AGLY50
AGLY51
AALA52
ATHR71
ALYS72
AMET73
ASER78
AHIS79
ATHR80
AALA83
AGLN84
AGLY85
AGLY86
ATYR199
AALA201
AALA235
ATHR236
AGLY237
ATHR247
AASP255
ALEU286
AHIS387
ATYR388
AGLY420
AGLU421
AARG432
AALA435
AASN436
ASER437
ALEU438
AFUM701

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES B 301
ChainResidue
BSER88
BCYS89
BILE93
BCYS94
BGLY95
BCYS97
BCYS109

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SF4 B 302
ChainResidue
BCYS182
BILE183
BLEU184
BCYS185
BALA186
BCYS187
BCYS188
BCYS249
BLEU253

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE F3S B 303
ChainResidue
BCYS192
BTYR202
BCYS239
BHIS240
BTHR241
BILE242
BMET243
BCYS245

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM C 201
ChainResidue
BHIS240
CHIS75
CARG76
CGLY79
CMET82
CHIS131
CTHR132
DARG63
DALA66
DMET69
DVAL70
DHIS95

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FTN C 202
ChainResidue
BPRO193
BSER194
BTRP197
BHIS240
CTRP69
CSER72
CARG76
DASP106
DTYR107

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE EPH D 201
ChainResidue
CMET82
CTHR85
CPRO127
CLEU133
CVAL170
DALA76
DTYR77
DHIS80
DPHE150
DGLU151
DTRP154

site_idAC9
Number of Residues11
DetailsBINDING SITE FOR RESIDUE FUM E 701
ChainResidue
EGLY85
EPHE153
EHIS276
ETHR288
EGLU289
EARG320
EHIS387
EARG432
EALA435
EFAD702
EGLN84

site_idBC1
Number of Residues32
DetailsBINDING SITE FOR RESIDUE FAD E 702
ChainResidue
EALA49
EGLY50
EGLY51
EALA52
ETHR71
ELYS72
EMET73
ESER78
EHIS79
ETHR80
EALA83
EGLN84
EGLY85
EGLY86
ETYR199
EPHE200
EALA201
EALA235
ETHR236
EGLY237
EASN252
EASP255
ELEU286
EHIS387
ETYR388
EGLY420
EGLU421
EARG432
EALA435
ESER437
ELEU438
EFUM701

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES F 301
ChainResidue
FSER88
FCYS89
FGLY92
FILE93
FCYS94
FGLY95
FCYS97
FCYS109

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SF4 F 302
ChainResidue
FCYS182
FILE183
FCYS185
FALA186
FCYS187
FCYS188
FCYS249
FPRO250
FLEU253

site_idBC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE F3S F 303
ChainResidue
FCYS192
FTYR202
FPRO205
FCYS239
FHIS240
FTHR241
FILE242
FMET243
FCYS245
FILE259

site_idBC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FTN F 304
ChainResidue
FPRO193
FSER194
FTRP196
FTRP197
FHIS240
GTRP69
GSER72
GARG76
HASP106
HTYR107

site_idBC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM G 201
ChainResidue
FHIS240
GHIS75
GARG76
GGLY79
GMET82
GHIS131
GTHR132
GGLY135
HARG63
HMET69
HHIS95
HVAL96
HGLY99

site_idBC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE EPH H 201
ChainResidue
GMET82
GTHR85
GILE123
GPRO174
HILE73
HALA76
HTYR77
HHIS80
HPHE150
HTRP154
HGLU155

Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CREGICGSC
ChainResidueDetails
BCYS89-CYS97

site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiLCAcCSaSCP
ChainResidueDetails
BCYS182-PRO193

site_idPS00504
Number of Residues10
DetailsFRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTtaAqGG
ChainResidueDetails
AARG77-GLY86

site_idPS01000
Number of Residues25
DetailsSDH_CYT_1 Succinate dehydrogenase cytochrome b subunit signature 1. RPIaphLtiykpqMtwmvSglHRvT
ChainResidueDetails
CARG54-THR78

site_idPS01001
Number of Residues14
DetailsSDH_CYT_2 Succinate dehydrogenase cytochrome b subunit signature 2. HtlnGIRFIgFDmA
ChainResidueDetails
CHIS131-ALA144

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues94
DetailsTOPO_DOM: Mitochondrial matrix => ECO:0000305|PubMed:22577165
ChainResidueDetails
DGLY26-PHE59
BCYS245
BCYS249
FCYS89
FCYS94
FCYS97
FCYS109
FCYS182
FCYS185
FCYS188
FCYS192
DASN105-ALA119
FCYS239
FCYS245
FCYS249
HGLY26-PHE59
HASN105-ALA119
BCYS182
BCYS185
BCYS188
BCYS192
BCYS239

site_idSWS_FT_FI2
Number of Residues118
DetailsTRANSMEM: Helical => ECO:0000305|PubMed:22577165
ChainResidueDetails
DLYS60-PHE78
ETHR71
ESER78
ETHR80
EGLY86
EALA201
ESER437
ELEU438
DMET84-VAL104
DALA120-GLU141
HLYS60-PHE78
HMET84-VAL104
HALA120-GLU141
ASER437
ALEU438
EALA49

site_idSWS_FT_FI3
Number of Residues36
DetailsTOPO_DOM: Mitochondrial intermembrane => ECO:0000305|PubMed:22577165
ChainResidueDetails
DILE79-GLU83
DHIS142-LEU156
HILE79-GLU83
HHIS142-LEU156

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:22577165, ECO:0000269|PubMed:26198225, ECO:0007744|PDB:3VR8, ECO:0007744|PDB:3VR9, ECO:0007744|PDB:3VRA, ECO:0007744|PDB:3VRB, ECO:0007744|PDB:4YSX, ECO:0007744|PDB:4YSY, ECO:0007744|PDB:4YSZ, ECO:0007744|PDB:4YT0, ECO:0007744|PDB:4YTM, ECO:0007744|PDB:4YTN, ECO:0007744|PDB:5C2T, ECO:0007744|PDB:5C3J
ChainResidueDetails
DHIS95
HHIS95
GSER72
GARG76

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22577165, ECO:0007744|PDB:3VR8
ChainResidueDetails
DTYR107
HTYR107

site_idSWS_FT_FI6
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:22577165, ECO:0007744|PDB:3VR8, ECO:0007744|PDB:3VRB
ChainResidueDetails
AGLY85
EARG432
AHIS276
ATHR288
AGLU289
AARG432
EGLY85
EHIS276
ETHR288
EGLU289

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22577165, ECO:0000269|PubMed:26198225, ECO:0007744|PDB:3VR8, ECO:0007744|PDB:4YSX, ECO:0007744|PDB:4YSY, ECO:0007744|PDB:4YSZ, ECO:0007744|PDB:4YT0, ECO:0007744|PDB:4YTM, ECO:0007744|PDB:5C2T, ECO:0007744|PDB:5C3J
ChainResidueDetails
AASP255
EASP255

site_idSWS_FT_FI8
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22577165, ECO:0007744|PDB:3VRB
ChainResidueDetails
AHIS387
AALA435
EHIS387
EALA435

site_idSWS_FT_FI9
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22577165, ECO:0000269|PubMed:26198225, ECO:0007744|PDB:3VR8, ECO:0007744|PDB:3VR9, ECO:0007744|PDB:3VRA, ECO:0007744|PDB:3VRB, ECO:0007744|PDB:4YSX, ECO:0007744|PDB:4YSY, ECO:0007744|PDB:4YSZ, ECO:0007744|PDB:4YT0, ECO:0007744|PDB:4YTN, ECO:0007744|PDB:5C2T, ECO:0007744|PDB:5C3J
ChainResidueDetails
AGLU421
EGLU421

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Tele-8alpha-FAD histidine => ECO:0000255|PIRSR:PIRSR611281-4, ECO:0000269|PubMed:22577165, ECO:0007744|PDB:3VR8, ECO:0007744|PDB:3VR9, ECO:0007744|PDB:3VRA, ECO:0007744|PDB:3VRB
ChainResidueDetails
AHIS79
EHIS79

227561

PDB entries from 2024-11-20

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