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4YXD

CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II BOUND WITH flutolanil

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005749cellular_componentobsolete mitochondrial 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
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0022900biological_processelectron transport chain
A0022904biological_processrespiratory electron transport chain
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
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
C0005515molecular_functionprotein binding
C0005739cellular_componentmitochondrion
C0005743cellular_componentmitochondrial inner membrane
C0005749cellular_componentobsolete mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone)
C0006099biological_processtricarboxylic acid cycle
C0006121biological_processmitochondrial electron transport, succinate to ubiquinone
C0009055molecular_functionelectron transfer activity
C0016020cellular_componentmembrane
C0020037molecular_functionheme binding
C0045273cellular_componentrespiratory chain complex II (succinate dehydrogenase)
C0045281cellular_componentobsolete succinate dehydrogenase complex
C0046872molecular_functionmetal ion binding
D0005515molecular_functionprotein binding
D0005739cellular_componentmitochondrion
D0005740cellular_componentmitochondrial envelope
D0005743cellular_componentmitochondrial inner membrane
D0005749cellular_componentobsolete mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone)
D0006099biological_processtricarboxylic acid cycle
D0006121biological_processmitochondrial electron transport, succinate to ubiquinone
D0016020cellular_componentmembrane
D0020037molecular_functionheme binding
D0045273cellular_componentrespiratory chain complex II (succinate dehydrogenase)
D0046872molecular_functionmetal ion binding
D0048039molecular_functionubiquinone binding
Functional Information from PDB Data
site_idAC1
Number of Residues35
Detailsbinding site for residue FAD A 700
ChainResidue
AGLY26
AHIS57
ATHR58
AALA60
AALA61
AGLN62
AGLY63
AGLY64
ATYR177
APHE178
AALA179
AALA27
AALA213
ATHR214
AGLY215
ATHR225
AASP233
ALEU264
AHIS365
ATYR366
AGLY397
AGLU398
AGLY28
AARG409
AALA412
AASN413
ASER414
ALEU415
ALEU418
AGLY29
AALA30
ATHR49
ALYS50
ALEU51
ASER56

site_idAC2
Number of Residues7
Detailsbinding site for residue FES B 301
ChainResidue
BSER64
BCYS65
BARG66
BCYS70
BGLY71
BCYS73
BCYS85

site_idAC3
Number of Residues6
Detailsbinding site for residue SF4 B 302
ChainResidue
BCYS158
BILE159
BCYS161
BCYS164
BCYS225
BPRO226

site_idAC4
Number of Residues7
Detailsbinding site for residue F3S B 303
ChainResidue
BCYS168
BTYR178
BCYS215
BHIS216
BMET219
BASN220
BCYS221

site_idAC5
Number of Residues14
Detailsbinding site for residue HEM C 301
ChainResidue
CHIS45
CARG46
CGLY49
CLEU52
CSER53
CVAL56
CHIS101
CTHR102
CHIS108
DARG47
DSER50
DLEU54
DHIS79
DGLY83

site_idAC6
Number of Residues11
Detailsbinding site for residue FTN C 302
ChainResidue
BPRO169
BSER170
BTRP173
BHIS216
CILE30
CTRP35
CMET39
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 Residues34
DetailsTOPO_DOM: Mitochondrial matrix => ECO:0000305
ChainResidueDetails
DASP14-SER40
BCYS221
BCYS225
DTHR89-LEU97
BCYS73
BCYS85
BCYS158
BCYS161
BCYS164
BCYS168
BCYS215

site_idSWS_FT_FI2
Number of Residues62
DetailsTRANSMEM: Helical
ChainResidueDetails
DLEU41-LEU62
DMET68-VAL88
DGLN98-PHE119
AHIS254
ATHR266
AHIS365
AGLU398
AARG409
ASER414

site_idSWS_FT_FI3
Number of Residues20
DetailsTOPO_DOM: Mitochondrial intermembrane => ECO:0000305
ChainResidueDetails
DASN63-ALA67
DASN120-LEU136

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

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PDB entries from 2024-07-24

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