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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9B29

Cryo-EM structure of the mouse TRPM3 alpha 2 channel in complex with cholesteryl hemisuccinate

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005262molecular_functioncalcium channel activity
A0005385molecular_functionzinc ion transmembrane transporter activity
A0005516molecular_functioncalmodulin binding
A0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0016020cellular_componentmembrane
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
A0034220biological_processmonoatomic ion transmembrane transport
A0051262biological_processprotein tetramerization
A0051289biological_processprotein homotetramerization
A0055085biological_processtransmembrane transport
A0070588biological_processcalcium ion transmembrane transport
A0071577biological_processzinc ion transmembrane transport
A0097603molecular_functiontemperature-gated ion channel activity
B0005216molecular_functionmonoatomic ion channel activity
B0005262molecular_functioncalcium channel activity
B0005385molecular_functionzinc ion transmembrane transporter activity
B0005516molecular_functioncalmodulin binding
B0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0016020cellular_componentmembrane
B0031683molecular_functionG-protein beta/gamma-subunit complex binding
B0034220biological_processmonoatomic ion transmembrane transport
B0051262biological_processprotein tetramerization
B0051289biological_processprotein homotetramerization
B0055085biological_processtransmembrane transport
B0070588biological_processcalcium ion transmembrane transport
B0071577biological_processzinc ion transmembrane transport
B0097603molecular_functiontemperature-gated ion channel activity
C0005216molecular_functionmonoatomic ion channel activity
C0005262molecular_functioncalcium channel activity
C0005385molecular_functionzinc ion transmembrane transporter activity
C0005516molecular_functioncalmodulin binding
C0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0016020cellular_componentmembrane
C0031683molecular_functionG-protein beta/gamma-subunit complex binding
C0034220biological_processmonoatomic ion transmembrane transport
C0051262biological_processprotein tetramerization
C0051289biological_processprotein homotetramerization
C0055085biological_processtransmembrane transport
C0070588biological_processcalcium ion transmembrane transport
C0071577biological_processzinc ion transmembrane transport
C0097603molecular_functiontemperature-gated ion channel activity
D0005216molecular_functionmonoatomic ion channel activity
D0005262molecular_functioncalcium channel activity
D0005385molecular_functionzinc ion transmembrane transporter activity
D0005516molecular_functioncalmodulin binding
D0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
D0005886cellular_componentplasma membrane
D0006811biological_processmonoatomic ion transport
D0016020cellular_componentmembrane
D0031683molecular_functionG-protein beta/gamma-subunit complex binding
D0034220biological_processmonoatomic ion transmembrane transport
D0051262biological_processprotein tetramerization
D0051289biological_processprotein homotetramerization
D0055085biological_processtransmembrane transport
D0070588biological_processcalcium ion transmembrane transport
D0071577biological_processzinc ion transmembrane transport
D0097603molecular_functiontemperature-gated ion channel activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues92
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"36283409","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues136
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues88
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"36283409","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"36283409","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues92
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"36283409","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues56
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues108
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"36283409","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues108
DetailsIntramembrane: {"description":"Pore-forming","evidences":[{"source":"PubMed","id":"32780479","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues100
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"36283409","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"36283409","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8DDT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8DDU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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