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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9QDL

CRYO-EM STRUCTURE OF THE YEAST RESPIRATORY COMPLEX II

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0006099biological_processtricarboxylic acid cycle
A0006121biological_processmitochondrial electron transport, succinate to ubiquinone
A0008177molecular_functionsuccinate dehydrogenase (quinone) activity
A0009055molecular_functionelectron transfer activity
A0009060biological_processaerobic respiration
A0031966cellular_componentmitochondrial membrane
A0045273cellular_componentrespiratory chain complex II (succinate dehydrogenase)
A0045333biological_processcellular respiration
A0050660molecular_functionflavin adenine dinucleotide binding
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0005829cellular_componentcytosol
B0006099biological_processtricarboxylic acid cycle
B0006121biological_processmitochondrial electron transport, succinate to ubiquinone
B0008177molecular_functionsuccinate dehydrogenase (quinone) activity
B0009060biological_processaerobic respiration
B0019646biological_processaerobic electron transport chain
B0022904biological_processrespiratory electron transport chain
B0031966cellular_componentmitochondrial membrane
B0032991cellular_componentprotein-containing complex
B0045273cellular_componentrespiratory chain complex II (succinate dehydrogenase)
B0045333biological_processcellular respiration
C0005739cellular_componentmitochondrion
C0005743cellular_componentmitochondrial inner membrane
C0005829cellular_componentcytosol
C0006099biological_processtricarboxylic acid cycle
C0006121biological_processmitochondrial electron transport, succinate to ubiquinone
C0008177molecular_functionsuccinate dehydrogenase (quinone) activity
C0009060biological_processaerobic respiration
C0019646biological_processaerobic electron transport chain
C0031966cellular_componentmitochondrial membrane
C0032991cellular_componentprotein-containing complex
C0042721cellular_componentTIM22 mitochondrial import inner membrane insertion complex
C0045039biological_processprotein insertion into mitochondrial inner membrane
C0045273cellular_componentrespiratory chain complex II (succinate dehydrogenase)
C0045333biological_processcellular respiration
D0005739cellular_componentmitochondrion
D0005743cellular_componentmitochondrial inner membrane
D0005829cellular_componentcytosol
D0006099biological_processtricarboxylic acid cycle
D0006121biological_processmitochondrial electron transport, succinate to ubiquinone
D0008177molecular_functionsuccinate dehydrogenase (quinone) activity
D0009060biological_processaerobic respiration
D0019646biological_processaerobic electron transport chain
D0020037molecular_functionheme binding
D0032991cellular_componentprotein-containing complex
D0045273cellular_componentrespiratory chain complex II (succinate dehydrogenase)
D0045333biological_processcellular respiration
D0048039molecular_functionubiquinone binding
D0098796cellular_componentmembrane protein complex
Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CREGICGSC
ChainResidueDetails
BCYS87-CYS95
site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiLCAcCStSCP
ChainResidueDetails
BCYS179-PRO190
site_idPS00504
Number of Residues10
DetailsFRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTvaAqGG
ChainResidueDetails
AARG88-GLY97
site_idPS01000
Number of Residues25
DetailsSDH_CYT_1 Succinate dehydrogenase cytochrome b subunit signature 1. RPIsphLtiyqpqLtwylSsfHRiS
ChainResidueDetails
CARG75-SER99
site_idPS01001
Number of Residues14
DetailsSDH_CYT_2 Succinate dehydrogenase cytochrome b subunit signature 2. HyggAIRHLiWDtA
ChainResidueDetails
CHIS156-ALA169
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q9YHT1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues25
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9YHT1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Tele-8alpha-FAD histidine","evidences":[{"source":"UniProtKB","id":"Q9YHT1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues30
DetailsDomain: {"description":"4Fe-4S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues15
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues120
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues28
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues22
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

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PDB entries from 2026-05-13

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