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3AEC

Crystal structure of porcine heart mitochondrial complex II bound with 2-Iodo-N-(1-methylethyl)-benzamid

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005749cellular_componentmitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone)
A0006099biological_processtricarboxylic acid cycle
A0006121biological_processmitochondrial electron transport, succinate to ubiquinone
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
A0022904biological_processrespiratory electron transport chain
A0050660molecular_functionflavin adenine dinucleotide binding
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0005749cellular_componentmitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone)
B0005886cellular_componentplasma membrane
B0006099biological_processtricarboxylic acid cycle
B0008177molecular_functionsuccinate dehydrogenase (quinone) activity
B0009055molecular_functionelectron transfer activity
B0009060biological_processaerobic respiration
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0022904biological_processrespiratory electron transport chain
B0031966cellular_componentmitochondrial membrane
B0046872molecular_functionmetal ion binding
B0048039molecular_functionubiquinone 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
C0006099biological_processtricarboxylic acid cycle
C0009055molecular_functionelectron transfer activity
C0016020cellular_componentmembrane
C0045281cellular_componentsuccinate dehydrogenase complex
D0005740cellular_componentmitochondrial envelope
D0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues30
DetailsBINDING SITE FOR RESIDUE FAD A 700
ChainResidue
AGLY26
AHIS57
ATHR58
AALA60
AALA61
AGLN62
AGLY63
AGLY64
ATYR177
APHE178
AALA179
AALA27
ATHR214
AGLY215
ATHR225
ASER226
AASP233
AGLU398
AARG409
AALA412
ASER414
ALEU415
AGLY28
ALEU418
AGLY29
AALA30
ATHR49
ALYS50
ALEU51
ASER56

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES B 302
ChainResidue
BSER64
BCYS65
BARG66
BGLY68
BCYS70
BGLY71
BCYS73
BCYS85

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 B 303
ChainResidue
BCYS158
BILE159
BCYS161
BALA162
BCYS164
BALA182
BCYS225
BPRO226

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE F3S B 304
ChainResidue
BCYS168
BTYR178
BPRO181
BCYS215
BHIS216
BTHR217
BILE218
BMET219
BASN220
BCYS221

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM C 1305
ChainResidue
BHIS216
CHIS45
CARG46
CGLY49
CLEU52
CSER53
CHIS101
CHIS108
DLEU53
DLEU57
DHIS79
DGLY83

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EPH D 1306
ChainResidue
CLEU140
DALA60
DTYR61
DLEU62
DPRO64
DCYS127
DALA131
DTRP134

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EBM C 1201
ChainResidue
BSER170
BTRP173
BHIS216
BILE218
CSER42
CARG46
DASP90
DTYR91

Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CREGICGSC
ChainResidueDetails
BCYS65-CYS73

site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiLCAcCStSCP
ChainResidueDetails
BCYS158-PRO169

site_idPS00504
Number of Residues10
DetailsFRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTvaAqGG
ChainResidueDetails
AARG55-GLY64

site_idPS01000
Number of Residues25
DetailsSDH_CYT_1 Succinate dehydrogenase cytochrome b subunit signature 1. RPLsphItiyrwsLpmamSicHRgT
ChainResidueDetails
CARG24-THR48

site_idPS01001
Number of Residues14
DetailsSDH_CYT_2 Succinate dehydrogenase cytochrome b subunit signature 2. HtwnGIRHLiWDlG
ChainResidueDetails
CHIS101-GLY114

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues62
DetailsTRANSMEM: Helical
ChainResidueDetails
DLEU41-LEU62
BCYS221
BCYS225
DMET68-VAL88
DGLN98-PHE119
BCYS85
BCYS158
BCYS161
BCYS164
BCYS168
BCYS215

site_idSWS_FT_FI2
Number of Residues20
DetailsTOPO_DOM: Mitochondrial intermembrane => ECO:0000305
ChainResidueDetails
DASN63-ALA67
DASN120-LEU136
CILE119-LEU140
AHIS254
ATHR266
AHIS365
AGLU398
AARG409
ASER414

site_idSWS_FT_FI3
Number of Residues8
DetailsTOPO_DOM: Mitochondrial matrix => ECO:0000305
ChainResidueDetails
DTHR89-LEU97
CALA141-MET143

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0
ChainResidueDetails
DHIS79
ALYS605
ALYS140
ALYS438
ALYS475
ALYS508
ALYS556
ALYS582
ALYS591
ALYS594

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15989954
ChainResidueDetails
DTYR91
ALYS293
ALYS443
ALYS456
ALYS496

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by SRC => ECO:0000250|UniProtKB:P31040
ChainResidueDetails
ATYR173

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P31040
ChainResidueDetails
ALYS566

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8K2B3
ChainResidueDetails
ALYS573

218853

數據於2024-04-24公開中

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