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6MYR

Avian mitochondrial complex II with thiapronil bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005749cellular_componentobsolete mitochondrial 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
A0045273cellular_componentrespiratory chain complex II (succinate dehydrogenase)
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
C0006099biological_processtricarboxylic acid cycle
C0009055molecular_functionelectron transfer activity
C0016020cellular_componentmembrane
C0045281cellular_componentobsolete succinate dehydrogenase complex
C0046872molecular_functionmetal ion binding
D0005740cellular_componentmitochondrial envelope
D0016020cellular_componentmembrane
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
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

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

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PDB entries from 2024-07-10

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