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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8HMB

Cryo-EM structure of human high-voltage activated L-type calcium channel CaV1.2 in complex with benidipine (BEN)

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
C0005245molecular_functionvoltage-gated calcium channel activity
C0005262molecular_functioncalcium channel activity
C0005515molecular_functionprotein binding
C0005886cellular_componentplasma membrane
C0005891cellular_componentvoltage-gated calcium channel complex
C0006811biological_processmonoatomic ion transport
C0006816biological_processcalcium ion transport
C0007268biological_processchemical synaptic transmission
C0007528biological_processneuromuscular junction development
C0007601biological_processvisual perception
C0008331molecular_functionhigh voltage-gated calcium channel activity
C0016020cellular_componentmembrane
C0034220biological_processmonoatomic ion transmembrane transport
C0034702cellular_componentmonoatomic ion channel complex
C0042383cellular_componentsarcolemma
C0045933biological_processpositive regulation of muscle contraction
C0051015molecular_functionactin filament binding
C0051928biological_processpositive regulation of calcium ion transport
C0070509biological_processcalcium ion import
C0070588biological_processcalcium ion transmembrane transport
C0072659biological_processprotein localization to plasma membrane
C0086007molecular_functionvoltage-gated calcium channel activity involved in cardiac muscle cell action potential
C0086045biological_processmembrane depolarization during AV node cell action potential
C0086056molecular_functionvoltage-gated calcium channel activity involved in AV node cell action potential
C0086091biological_processregulation of heart rate by cardiac conduction
C0098684cellular_componentphotoreceptor ribbon synapse
C0098793cellular_componentpresynapse
C0098912biological_processmembrane depolarization during atrial cardiac muscle cell action potential
C0099509biological_processregulation of presynaptic cytosolic calcium ion concentration
C0099626molecular_functionvoltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels
C1904879biological_processpositive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel
C1990454cellular_componentL-type voltage-gated calcium channel complex
D0002520biological_processimmune system development
D0005216molecular_functionmonoatomic ion channel activity
D0005245molecular_functionvoltage-gated calcium channel activity
D0005262molecular_functioncalcium channel activity
D0005515molecular_functionprotein binding
D0005516molecular_functioncalmodulin binding
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005886cellular_componentplasma membrane
D0005891cellular_componentvoltage-gated calcium channel complex
D0005929cellular_componentcilium
D0006811biological_processmonoatomic ion transport
D0006816biological_processcalcium ion transport
D0006936biological_processmuscle contraction
D0007204biological_processpositive regulation of cytosolic calcium ion concentration
D0007507biological_processheart development
D0008331molecular_functionhigh voltage-gated calcium channel activity
D0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
D0014069cellular_componentpostsynaptic density
D0016020cellular_componentmembrane
D0030018cellular_componentZ disc
D0030315cellular_componentT-tubule
D0030425cellular_componentdendrite
D0034220biological_processmonoatomic ion transmembrane transport
D0034702cellular_componentmonoatomic ion channel complex
D0035115biological_processembryonic forelimb morphogenesis
D0042383cellular_componentsarcolemma
D0042995cellular_componentcell projection
D0043010biological_processcamera-type eye development
D0043204cellular_componentperikaryon
D0045202cellular_componentsynapse
D0045211cellular_componentpostsynaptic membrane
D0045762biological_processpositive regulation of adenylate cyclase activity
D0045933biological_processpositive regulation of muscle contraction
D0046872molecular_functionmetal ion binding
D0051393molecular_functionalpha-actinin binding
D0055085biological_processtransmembrane transport
D0060402biological_processcalcium ion transport into cytosol
D0061337biological_processcardiac conduction
D0061577biological_processcalcium ion transmembrane transport via high voltage-gated calcium channel
D0070588biological_processcalcium ion transmembrane transport
D0086002biological_processcardiac muscle cell action potential involved in contraction
D0086007molecular_functionvoltage-gated calcium channel activity involved in cardiac muscle cell action potential
D0086012biological_processmembrane depolarization during cardiac muscle cell action potential
D0086045biological_processmembrane depolarization during AV node cell action potential
D0086056molecular_functionvoltage-gated calcium channel activity involved in AV node cell action potential
D0086064biological_processcell communication by electrical coupling involved in cardiac conduction
D0086091biological_processregulation of heart rate by cardiac conduction
D0098703biological_processcalcium ion import across plasma membrane
D0098839cellular_componentpostsynaptic density membrane
D0098911biological_processregulation of ventricular cardiac muscle cell action potential
D0098912biological_processmembrane depolarization during atrial cardiac muscle cell action potential
D1990454cellular_componentL-type voltage-gated calcium channel complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S1 of repeat II","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=S6 of repeat IV","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues11
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S1 of repeat I","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues236
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=S2 of repeat I","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues153
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=S3 of repeat I","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S4 of repeat I","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=S5 of repeat I","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues80
DetailsIntramembrane: {"description":"Pore-forming","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=S6 of repeat I","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=S2 of repeat II","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=S3 of repeat II","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S4 of repeat II","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=S5 of repeat II","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=S6 of repeat II","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S1 of repeat III","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S3 of repeat III","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S4 of repeat III","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=S5 of repeat III","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=S6 of repeat III","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=S1 of repeat IV","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=S2 of repeat IV","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=S3 of repeat IV","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S4 of repeat IV","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=S5 of repeat IV","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues246
DetailsRepeat: {"description":"II"}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues17
DetailsRegion: {"description":"AID/alpha-interaction domain; mediates interaction with the beta subunit","evidences":[{"source":"PubMed","id":"15141227","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues89
DetailsRegion: {"description":"Dihydropyridine binding","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues3
DetailsMotif: {"description":"Selectivity filter of repeat I","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues3
DetailsMotif: {"description":"Selectivity filter of repeat II","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues3
DetailsMotif: {"description":"Selectivity filter of repeat III","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues3
DetailsMotif: {"description":"Selectivity filter of repeat IV","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues3
DetailsSite: {"description":"Calcium ion selectivity and permeability","evidences":[{"source":"PubMed","id":"8099908","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI38
Number of Residues177
DetailsDomain: {"description":"VWFA","evidences":[{"source":"PROSITE-ProRule","id":"PRU00219","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI39
Number of Residues4
DetailsMotif: {"description":"MIDAS-like motif"}
ChainResidueDetails
site_idSWS_FT_FI40
Number of Residues3
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI41
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P54290","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI42
Number of Residues7
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"34234349","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7MIX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7MIY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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