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6MYO

Avian mitochondrial complex II with flutolanyl bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0000104molecular_functionsuccinate dehydrogenase activity
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005749cellular_componentmitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone)
A0006099biological_processtricarboxylic acid cycle
A0006105biological_processsuccinate metabolic process
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
A0050660molecular_functionflavin adenine dinucleotide binding
B0006099biological_processtricarboxylic acid cycle
B0009055molecular_functionelectron transfer activity
B0016491molecular_functionoxidoreductase activity
B0051536molecular_functioniron-sulfur cluster binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
C0005739cellular_componentmitochondrion
C0005749cellular_componentmitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone)
C0005886cellular_componentplasma membrane
C0006099biological_processtricarboxylic acid cycle
C0006121biological_processmitochondrial electron transport, succinate to ubiquinone
C0009055molecular_functionelectron transfer activity
C0016020cellular_componentmembrane
C0045281cellular_componentsuccinate dehydrogenase complex
C0046872molecular_functionmetal ion binding
D0005740cellular_componentmitochondrial envelope
D0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues42
Detailsbinding site for residue FAD A 1001
ChainResidue
AVAL24
ALEU50
ASER55
AHIS56
ATHR57
AALA59
AALA60
AGLN61
AGLY62
AGLY63
ATYR176
AGLY25
APHE177
AALA178
AALA212
ATHR213
AGLY214
ATHR224
AASP232
ALEU263
AHIS364
ATYR365
AALA26
AGLY396
AGLU397
AARG408
AALA411
ASER413
ALEU414
ALEU417
AOAA1002
AHOH1112
AHOH1165
AGLY27
AHOH1169
AHOH1179
AHOH1215
AGLY28
AALA29
AVAL47
ATHR48
ALYS49

site_idAC2
Number of Residues11
Detailsbinding site for residue OAA A 1002
ChainResidue
AGLY62
AHIS253
ALEU263
ATHR265
AGLU266
AARG297
AHIS364
AARG408
AGLY410
AALA411
AFAD1001

site_idAC3
Number of Residues6
Detailsbinding site for residue K A 1003
ChainResidue
ATYR365
AASN366
AMET367
AGLY368
AGLU397
AALA399

site_idAC4
Number of Residues3
Detailsbinding site for residue MN A 1004
ChainResidue
AGLU121
AHIS505
AHOH1245

site_idAC5
Number of Residues8
Detailsbinding site for residue PEG A 1005
ChainResidue
AARG218
AHIS227
AARG469
AGLN473
AGLU521
AHOH1238
BARG63
BHOH1193

site_idAC6
Number of Residues8
Detailsbinding site for residue FES B 1001
ChainResidue
BSER64
BCYS65
BARG66
BGLY68
BCYS70
BGLY71
BCYS73
BCYS85

site_idAC7
Number of Residues7
Detailsbinding site for residue SF4 B 1002
ChainResidue
BCYS158
BILE159
BCYS161
BALA162
BCYS164
BCYS225
BPRO226

site_idAC8
Number of Residues10
Detailsbinding site for residue F3S B 1003
ChainResidue
BCYS168
BTYR178
BCYS215
BHIS216
BTHR217
BILE218
BMET219
BASN220
BCYS221
BILE235

site_idAC9
Number of Residues13
Detailsbinding site for residue FTN C 202
ChainResidue
BILE218
BHOH1118
CILE27
CTRP32
CSER39
CILE40
CARG43
DASP57
DTYR58
BPRO169
BSER170
BTRP173
BHIS216

site_idAD1
Number of Residues18
Detailsbinding site for residue HEM C 201
ChainResidue
BHIS216
BHOH1187
CHIS42
CARG43
CGLY46
CVAL47
CLEU49
CSER50
CHIS98
CTHR99
CGLY102
CHOH1103
DARG14
DLEU20
DLEU43
DHIS46
DGLY50
DHOH301

site_idAD2
Number of Residues12
Detailsbinding site for residue UMQ C 1002
ChainResidue
BARG223
CLYS31
CTRP32
CSER33
CLEU34
CPRO35
CALA37
CTHR41
CGLU120
CHOH1120
DTYR88
DTYR89

site_idAD3
Number of Residues8
Detailsbinding site for residue 3PE D 201
ChainResidue
CLEU49
CGLY52
CVAL53
CLEU91
CMET140
DALA27
DTYR28
DVAL97

Functional Information from PROSITE/UniProt
site_idPS00504
Number of Residues10
DetailsFRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTvaAqGG
ChainResidueDetails
AARG54-GLY63

site_idPS01000
Number of Residues25
DetailsSDH_CYT_1 Succinate dehydrogenase cytochrome b subunit signature 1. RPLsphIsiykwsLpmamSitHRgT
ChainResidueDetails
CARG21-THR45

site_idPS01001
Number of Residues14
DetailsSDH_CYT_2 Succinate dehydrogenase cytochrome b subunit signature 2. HtwnGIRHLvWDmG
ChainResidueDetails
CHIS98-GLY111

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:16371358
ChainResidueDetails
AARG297
BCYS221
BCYS225
DVAL35-ILE55
DILE65-PHE86
BCYS85
BCYS158
BCYS161
BCYS164
BCYS168
BCYS215

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:15805592, ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256
ChainResidueDetails
AGLY25
ATHR48
AASP232
AGLU397
ASER413

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256
ChainResidueDetails
AHIS253
ATHR265
AHIS364
AARG408

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Tele-8alpha-FAD histidine => ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256
ChainResidueDetails
AHIS56

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256
ChainResidueDetails
DTYR58

Catalytic Information from CSA
site_idMCSA1
Number of Residues8
DetailsM-CSA 294
ChainResidueDetails
APHE130steric role
AGLN251electrostatic stabiliser, hydrogen bond acceptor, steric role
AHIS253electrostatic stabiliser, hydrogen bond donor, steric role
ALEU263steric role
AGLU266electrostatic stabiliser, hydrogen bond acceptor, steric role
AARG297hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS364electrostatic stabiliser, hydrogen bond donor, steric role
AARG408electrostatic stabiliser, hydrogen bond donor, steric role

219140

PDB entries from 2024-05-01

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