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2BS3

GLU C180 -> GLN VARIANT QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES

Functional Information from GO Data
ChainGOidnamespacecontents
A0000104molecular_functionsuccinate dehydrogenase activity
A0005886cellular_componentplasma membrane
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
A0022900biological_processelectron transport chain
A0050660molecular_functionflavin adenine dinucleotide binding
B0005886cellular_componentplasma membrane
B0006099biological_processtricarboxylic acid cycle
B0009055molecular_functionelectron transfer activity
B0009060biological_processaerobic respiration
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
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
C0016020cellular_componentmembrane
C0046872molecular_functionmetal ion binding
D0000104molecular_functionsuccinate dehydrogenase activity
D0005886cellular_componentplasma membrane
D0008177molecular_functionsuccinate dehydrogenase (quinone) activity
D0009055molecular_functionelectron transfer activity
D0009061biological_processanaerobic respiration
D0016020cellular_componentmembrane
D0016491molecular_functionoxidoreductase activity
D0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
D0022900biological_processelectron transport chain
D0050660molecular_functionflavin adenine dinucleotide binding
E0005886cellular_componentplasma membrane
E0006099biological_processtricarboxylic acid cycle
E0009055molecular_functionelectron transfer activity
E0009060biological_processaerobic respiration
E0016020cellular_componentmembrane
E0016491molecular_functionoxidoreductase activity
E0022904biological_processrespiratory electron transport chain
E0046872molecular_functionmetal ion binding
E0051536molecular_functioniron-sulfur cluster binding
E0051537molecular_function2 iron, 2 sulfur cluster binding
E0051538molecular_function3 iron, 4 sulfur cluster binding
E0051539molecular_function4 iron, 4 sulfur cluster binding
F0005886cellular_componentplasma membrane
F0006099biological_processtricarboxylic acid cycle
F0016020cellular_componentmembrane
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A1658
ChainResidue
ASER371
AMET372
AGLY373
AGLU393
AALA395
AHOH2156

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA D1658
ChainResidue
DGLU393
DALA395
DHOH2162
DSER371
DMET372
DGLY373

site_idAC3
Number of Residues37
DetailsBINDING SITE FOR RESIDUE FAD A1656
ChainResidue
AGLY12
AGLY13
AGLY14
ALEU15
AALA16
ASER35
ALEU36
AILE37
ASER42
AHIS43
ASER44
AALA47
AGLY49
AGLY50
ALYS179
AALA181
AALA215
ATHR216
AGLY217
ATHR227
AASN228
ATHR235
AHIS369
ATYR370
AGLY392
AGLU393
AARG404
AGLY407
AASN408
ASER409
AVAL410
ACIT1657
AHOH2269
AHOH2270
AHOH2271
AHOH2272
AHOH2273

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE CIT A1657
ChainResidue
AALA46
AGLN48
AGLY49
APHE141
AGLN255
AHIS257
ALEU267
ATHR269
AGLU270
AARG301
AHIS369
AARG404
AGLY406
AFAD1656
AHOH2274

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FES B1240
ChainResidue
BVAL56
BCYS57
BARG58
BGLY60
BILE61
BCYS62
BGLY63
BCYS65
BCYS77

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE F3S B1241
ChainResidue
BCYS161
BTHR163
BCYS208
BMET209
BTHR210
BLEU211
BLEU212
BALA213
BCYS214

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SF4 B1242
ChainResidue
BCYS151
BILE152
BGLU153
BCYS154
BGLY155
BCYS157
BCYS218
BPRO219
BLYS220

site_idAC8
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM C1255
ChainResidue
CALA97
CLYS100
CPHE101
CTRP126
CGLY133
CMET136
CPHE137
CHIS182
CGLY186
CLEU190
CLYS193
CHEM1256
CHOH2046
CHOH2047
BHOH2142
CGLN30
CSER31
CGLY34
CLEU37
CPHE90
CHIS93
CALA94

site_idAC9
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM C1256
ChainResidue
CPHE40
CMET41
CHIS44
CLEU82
CALA83
CHIS143
CMET147
CILE154
CSER159
CARG162
CTYR172
CLEU176
CGLY224
CPHE228
CHEM1255

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE LMT C1257
ChainResidue
CPHE101
CPRO102
CASN104
CTYR108
CMET131
FPHE95
FMET98
FARG99

site_idBC2
Number of Residues38
DetailsBINDING SITE FOR RESIDUE FAD D1656
ChainResidue
DGLY12
DGLY13
DGLY14
DLEU15
DALA16
DSER35
DLEU36
DILE37
DSER42
DHIS43
DSER44
DALA47
DGLY49
DGLY50
DLYS179
DGLU180
DALA181
DALA215
DTHR216
DGLY217
DTHR227
DASN228
DTHR235
DHIS369
DTYR370
DGLY392
DGLU393
DARG404
DGLY407
DASN408
DSER409
DVAL410
DCIT1657
DHOH2128
DHOH2285
DHOH2286
DHOH2287
DHOH2288

site_idBC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE CIT D1657
ChainResidue
DALA46
DGLN48
DGLY49
DPHE141
DGLN255
DHIS257
DLEU267
DTHR269
DGLU270
DARG301
DHIS369
DARG404
DFAD1656
DHOH2289
DHOH2291

site_idBC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FES E1240
ChainResidue
EVAL56
ECYS57
EARG58
EGLY60
EILE61
ECYS62
EGLY63
ECYS65
ECYS77

site_idBC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE F3S E1241
ChainResidue
ECYS161
ETHR163
ECYS208
EMET209
ETHR210
ELEU211
ELEU212
EALA213
ECYS214

site_idBC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SF4 E1242
ChainResidue
ECYS151
EILE152
EGLU153
ECYS154
EGLY155
ECYS157
ECYS218
EPRO219
ELYS220

site_idBC7
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM F1255
ChainResidue
FGLN30
FSER31
FGLY34
FLEU37
FPHE90
FHIS93
FALA94
FALA97
FLYS100
FPHE101
FTRP126
FGLY133
FMET136
FPHE137
FVAL179
FHIS182
FGLY186
FLEU190
FLYS193
FHEM1256
FHOH2057
FHOH2058
FHOH2059

site_idBC8
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM F1256
ChainResidue
FPHE40
FMET41
FHIS44
FLEU82
FALA83
FHIS143
FMET147
FILE154
FSER159
FARG162
FTYR172
FLEU176
FGLY224
FPHE228
FHEM1255

site_idBC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE LMT F1257
ChainResidue
CLEU26
CPHE95
CMET98
CARG99
FPHE101
FPRO102
FASN104
FTYR108
FMET131

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

site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiECGcCIaACG
ChainResidueDetails
BCYS151-GLY162

site_idPS00504
Number of Residues10
DetailsFRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHSaaAqGG
ChainResidueDetails
AARG41-GLY50

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"P00363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues38
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10586875","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11248702","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QLB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10586875","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QLB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Tele-8alpha-FAD histidine","evidences":[{"source":"PubMed","id":"10586875","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11248702","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QLB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues180
DetailsDomain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues58
DetailsDomain: {"description":"4Fe-4S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues58
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"10586875","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues222
DetailsTransmembrane: {"description":"Helical"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues76
DetailsTopological domain: {"description":"Periplasmic"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues84
DetailsTopological domain: {"description":"Cytoplasmic"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues8
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10586875","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11248702","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QLB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BS4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d4c
ChainResidueDetails
AHIS257
AARG404
AHIS369
AARG301

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d4c
ChainResidueDetails
DHIS257
DARG404
DHIS369
DARG301

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PDB entries from 2025-07-09

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