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2ACZ

Complex II (Succinate Dehydrogenase) From E. Coli with Atpenin A5 inhibitor co-crystallized at the ubiquinone binding site

Functional Information from GO Data
ChainGOidnamespacecontents
A0000104molecular_functionsuccinate dehydrogenase activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006099biological_processtricarboxylic acid cycle
A0008177molecular_functionsuccinate dehydrogenase (quinone) activity
A0009055molecular_functionelectron transfer activity
A0009060biological_processaerobic respiration
A0009061biological_processanaerobic respiration
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0019646biological_processaerobic electron transport chain
A0022900biological_processelectron transport chain
A0045281cellular_componentobsolete succinate dehydrogenase complex
A0045282cellular_componentobsolete plasma membrane succinate dehydrogenase complex
A0050660molecular_functionflavin adenine dinucleotide binding
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0006099biological_processtricarboxylic acid cycle
B0008177molecular_functionsuccinate dehydrogenase (quinone) activity
B0009055molecular_functionelectron transfer activity
B0009060biological_processaerobic respiration
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0019646biological_processaerobic electron transport chain
B0022904biological_processrespiratory electron transport chain
B0045281cellular_componentobsolete succinate dehydrogenase 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
C0005886cellular_componentplasma membrane
C0006099biological_processtricarboxylic acid cycle
C0008177molecular_functionsuccinate dehydrogenase (quinone) activity
C0009055molecular_functionelectron transfer activity
C0009060biological_processaerobic respiration
C0016020cellular_componentmembrane
C0017004biological_processcytochrome complex assembly
C0019646biological_processaerobic electron transport chain
C0020037molecular_functionheme binding
C0045281cellular_componentobsolete succinate dehydrogenase complex
C0046872molecular_functionmetal ion binding
C0048039molecular_functionubiquinone binding
D0005886cellular_componentplasma membrane
D0006099biological_processtricarboxylic acid cycle
D0009055molecular_functionelectron transfer activity
D0009060biological_processaerobic respiration
D0016020cellular_componentmembrane
D0017004biological_processcytochrome complex assembly
D0019646biological_processaerobic electron transport chain
D0020037molecular_functionheme binding
D0045281cellular_componentobsolete succinate dehydrogenase complex
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE OAA A 589
ChainResidue
AGLY51
AGLY401
AGLY402
AFAD601
APHE126
AHIS242
ALEU252
ATHR254
AGLU255
AARG286
AHIS354
AARG399

site_idAC2
Number of Residues32
DetailsBINDING SITE FOR RESIDUE FAD A 601
ChainResidue
AGLY14
AALA15
AGLY16
AGLY17
AALA18
ASER37
ALYS38
AVAL39
ASER44
AHIS45
ATHR46
ASER48
AALA49
AGLN50
AGLY51
AGLY52
ATRP164
ATYR165
AALA166
AALA201
ATHR202
AGLY203
AASN214
AASP221
ATYR355
AGLU388
AARG399
AGLY402
ASER404
ALEU405
ALEU408
AOAA589

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FES B 302
ChainResidue
BSER54
BCYS55
BARG56
BGLY58
BVAL59
BCYS60
BGLY61
BASP63
BCYS75

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 B 303
ChainResidue
BCYS149
BILE150
BCYS152
BALA153
BCYS154
BCYS155
BCYS216
BPRO217

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE F3S B 304
ChainResidue
BCYS159
BPRO172
BCYS206
BHIS207
BSER208
BILE209
BMET210
BASN211
BCYS212
BTHR223

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEB C 130
ChainResidue
BHIS207
CHIS30
CARG31
CTHR37
CPHE38
CHIS84
CVAL85
CGLY88
CCDN132
DARG20
DALA23
DTHR27
DILE68
DHIS71
DGLY75
DMET76
DGLN78

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE AT5 C 131
ChainResidue
DTYR83
BPRO160
BTRP164
BHIS207
BILE209
CLEU15
CPHE20
CALA24
CSER27
CILE28
CARG31
DASP82

site_idAC8
Number of Residues18
DetailsBINDING SITE FOR RESIDUE CDN C 132
ChainResidue
CLEU44
CSER51
CALA61
CSER62
CMET65
CMET74
CLEU78
CVAL115
CLEU123
CALA124
CVAL126
CLEU127
CTRP129
CHEB130
DILE30
DGLY41
DLEU43
DILE68

Functional Information from PROSITE/UniProt
site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiLCAcCStSCP
ChainResidueDetails
BCYS149-PRO160

site_idPS00504
Number of Residues10
DetailsFRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTvsAqGG
ChainResidueDetails
AARG43-GLY52

site_idPS01000
Number of Residues25
DetailsSDH_CYT_1 Succinate dehydrogenase cytochrome b subunit signature 1. RPVnldLqtirfpItaiaSilHRvS
ChainResidueDetails
CARG9-SER33

site_idPS01001
Number of Residues14
DetailsSDH_CYT_2 Succinate dehydrogenase cytochrome b subunit signature 2. HvvvGIRHMmMDfG
ChainResidueDetails
CHIS84-GLY97

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues23
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
DMET1-ASP15
BCYS216
DTHR81-ARG90
BCYS75
BCYS149
BCYS152
BCYS155
BCYS159
BCYS206
BCYS212

site_idSWS_FT_FI2
Number of Residues65
DetailsTRANSMEM: Helical
ChainResidueDetails
DPHE16-PHE36
DVAL59-LEU80
DLEU91-VAL115
AGLU388
ASER404

site_idSWS_FT_FI3
Number of Residues21
DetailsTOPO_DOM: Periplasmic => ECO:0000305
ChainResidueDetails
DPHE37-LYS58
ATHR254
AHIS354
AARG399

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
DHIS71

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12560550
ChainResidueDetails
DTYR83

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d4c
ChainResidueDetails
AHIS242
AARG286
AHIS354
AARG399

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PDB entries from 2024-07-17

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