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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8GS8

cryo-EM structure of the human respiratory complex II

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005759cellular_componentmitochondrial matrix
A0006099biological_processtricarboxylic acid cycle
A0006105biological_processsuccinate metabolic process
A0006121biological_processmitochondrial electron transport, succinate to ubiquinone
A0007399biological_processnervous system development
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
A0042776biological_processproton motive force-driven mitochondrial ATP synthesis
A0045273cellular_componentrespiratory chain complex II (succinate dehydrogenase)
A0050660molecular_functionflavin adenine dinucleotide binding
A0071949molecular_functionFAD binding
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0005759cellular_componentmitochondrial matrix
B0006099biological_processtricarboxylic acid cycle
B0006105biological_processsuccinate metabolic process
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
B0042776biological_processproton motive force-driven mitochondrial ATP synthesis
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
C0005759cellular_componentmitochondrial matrix
C0006099biological_processtricarboxylic acid cycle
C0006121biological_processmitochondrial electron transport, succinate to ubiquinone
C0008177molecular_functionsuccinate dehydrogenase (quinone) activity
C0009055molecular_functionelectron transfer activity
C0009060biological_processaerobic respiration
C0016020cellular_componentmembrane
C0020037molecular_functionheme binding
C0042776biological_processproton motive force-driven mitochondrial ATP synthesis
C0045273cellular_componentrespiratory chain complex II (succinate dehydrogenase)
C0046872molecular_functionmetal ion binding
D0005515molecular_functionprotein binding
D0005739cellular_componentmitochondrion
D0005740cellular_componentmitochondrial envelope
D0005743cellular_componentmitochondrial inner membrane
D0005759cellular_componentmitochondrial matrix
D0006099biological_processtricarboxylic acid cycle
D0006121biological_processmitochondrial electron transport, succinate to ubiquinone
D0008177molecular_functionsuccinate dehydrogenase (quinone) activity
D0009055molecular_functionelectron transfer activity
D0016020cellular_componentmembrane
D0020037molecular_functionheme binding
D0042776biological_processproton motive force-driven mitochondrial ATP synthesis
D0045273cellular_componentrespiratory chain complex II (succinate dehydrogenase)
D0046872molecular_functionmetal ion binding
D0048039molecular_functionubiquinone binding
Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CREGICGSC
ChainResidueDetails
BCYS93-CYS101
site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiLCAcCStSCP
ChainResidueDetails
BCYS186-PRO197
site_idPS00504
Number of Residues10
DetailsFRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTvaAqGG
ChainResidueDetails
AARG97-GLY106
site_idPS01000
Number of Residues25
DetailsSDH_CYT_1 Succinate dehydrogenase cytochrome b subunit signature 1. RPLsphItiyswsLpmamSicHRgT
ChainResidueDetails
CARG50-THR74
site_idPS01001
Number of Residues14
DetailsSDH_CYT_2 Succinate dehydrogenase cytochrome b subunit signature 2. HtwnGIRHLmWDlG
ChainResidueDetails
CHIS127-GLY140
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 Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32887801","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37098072","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6VAX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8GS8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32887801","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6VAX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37098072","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8GS8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37098072","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6VAX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8DYD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8DYE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8GS8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Tele-8alpha-FAD histidine","evidences":[{"source":"PubMed","id":"32887801","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37098072","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6VAX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8GS8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues9
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8K2B3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues7
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q8K2B3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"22823520","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8K2B3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues93
DetailsDomain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues30
DetailsDomain: {"description":"4Fe-4S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues72
DetailsRegion: {"description":"Interaction with SDHAF1","evidences":[{"source":"PubMed","id":"26749241","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQA3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues134
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"37098072","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8GS8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues38
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"37098072","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8GS8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues16
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"37098072","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8GS8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"37098072","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8GS8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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