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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8CA4

Cryo-EM structure NDUFS4 knockout complex I from Mus musculus heart (Class 2 N-domain).

Functional Information from GO Data
ChainGOidnamespacecontents
E0003954molecular_functionNADH dehydrogenase activity
E0005739cellular_componentmitochondrion
E0005743cellular_componentmitochondrial inner membrane
E0006120biological_processmitochondrial electron transport, NADH to ubiquinone
E0007399biological_processnervous system development
E0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
E0009060biological_processaerobic respiration
E0016491molecular_functionoxidoreductase activity
E0022904biological_processrespiratory electron transport chain
E0042776biological_processproton motive force-driven mitochondrial ATP synthesis
E0043209cellular_componentmyelin sheath
E0045271cellular_componentrespiratory chain complex I
E0046872molecular_functionmetal ion binding
E0048738biological_processcardiac muscle tissue development
E0051536molecular_functioniron-sulfur cluster binding
E0051537molecular_function2 iron, 2 sulfur cluster binding
E1902600biological_processproton transmembrane transport
F0005515molecular_functionprotein binding
F0005739cellular_componentmitochondrion
F0005743cellular_componentmitochondrial inner membrane
F0006120biological_processmitochondrial electron transport, NADH to ubiquinone
F0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
F0009060biological_processaerobic respiration
F0010181molecular_functionFMN binding
F0016491molecular_functionoxidoreductase activity
F0022904biological_processrespiratory electron transport chain
F0042775biological_processmitochondrial ATP synthesis coupled electron transport
F0042776biological_processproton motive force-driven mitochondrial ATP synthesis
F0045271cellular_componentrespiratory chain complex I
F0046872molecular_functionmetal ion binding
F0051287molecular_functionNAD binding
F0051536molecular_functioniron-sulfur cluster binding
F0051539molecular_function4 iron, 4 sulfur cluster binding
F1902600biological_processproton transmembrane transport
G0005515molecular_functionprotein binding
G0005739cellular_componentmitochondrion
G0005743cellular_componentmitochondrial inner membrane
G0005758cellular_componentmitochondrial intermembrane space
G0006120biological_processmitochondrial electron transport, NADH to ubiquinone
G0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
G0009055molecular_functionelectron transfer activity
G0009060biological_processaerobic respiration
G0016020cellular_componentmembrane
G0016491molecular_functionoxidoreductase activity
G0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
G0022904biological_processrespiratory electron transport chain
G0032981biological_processmitochondrial respiratory chain complex I assembly
G0042773biological_processATP synthesis coupled electron transport
G0042776biological_processproton motive force-driven mitochondrial ATP synthesis
G0043209cellular_componentmyelin sheath
G0045271cellular_componentrespiratory chain complex I
G0045333biological_processcellular respiration
G0046872molecular_functionmetal ion binding
G0051536molecular_functioniron-sulfur cluster binding
G0051537molecular_function2 iron, 2 sulfur cluster binding
G0051539molecular_function4 iron, 4 sulfur cluster binding
G1902600biological_processproton transmembrane transport
S0001835biological_processblastocyst hatching
S0005739cellular_componentmitochondrion
S0005743cellular_componentmitochondrial inner membrane
S0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
S0009060biological_processaerobic respiration
S0022904biological_processrespiratory electron transport chain
S0031966cellular_componentmitochondrial membrane
S0042776biological_processproton motive force-driven mitochondrial ATP synthesis
S0045271cellular_componentrespiratory chain complex I
S1902600biological_processproton transmembrane transport
s0005739cellular_componentmitochondrion
s0005743cellular_componentmitochondrial inner membrane
s0009060biological_processaerobic respiration
s0022904biological_processrespiratory electron transport chain
s0042775biological_processmitochondrial ATP synthesis coupled electron transport
s0042776biological_processproton motive force-driven mitochondrial ATP synthesis
s0045271cellular_componentrespiratory chain complex I
Functional Information from PROSITE/UniProt
site_idPS00641
Number of Residues18
DetailsCOMPLEX1_75K_1 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. PrfCYherlsvaGnCRmC
ChainResidueDetails
GPRO38-CYS55
site_idPS00642
Number of Residues13
DetailsCOMPLEX1_75K_2 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. CPiCDqGGeCdLQ
ChainResidueDetails
GCYS105-GLN117
site_idPS00643
Number of Residues11
DetailsCOMPLEX1_75K_3 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. RCIqCtRCIrF
ChainResidueDetails
GARG152-PHE162
site_idPS00644
Number of Residues16
DetailsCOMPLEX1_51K_1 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. GAGAYICGEETALIES
ChainResidueDetails
FGLY180-SER195
site_idPS00645
Number of Residues12
DetailsCOMPLEX1_51K_2 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. ESCGqCtPCReG
ChainResidueDetails
FGLU357-GLY368
site_idPS01099
Number of Residues19
DetailsCOMPLEX1_24K Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. DklFTlieveCLGaCvnAP
ChainResidueDetails
EASP134-PRO152
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29915388","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6G2J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6G72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23576753","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"UniProtKB","id":"P19404","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues57
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues78
DetailsDomain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues39
DetailsDomain: {"description":"4Fe-4S His(Cys)3-ligated-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01184","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues56
DetailsDomain: {"description":"4Fe-4S Mo/W bis-MGD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01004","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"38575788","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01184","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"38575788","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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