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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8E5B

Human L-type voltage-gated calcium channel Cav1.3 in the presence of Amiodarone and Sofosbuvir at 3.3 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005245molecular_functionvoltage-gated calcium channel activity
A0005262molecular_functioncalcium channel activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0005891cellular_componentvoltage-gated calcium channel complex
A0006811biological_processmonoatomic ion transport
A0006816biological_processcalcium ion transport
A0006936biological_processmuscle contraction
A0007154biological_processcell communication
A0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
A0007605biological_processsensory perception of sound
A0008092molecular_functioncytoskeletal protein binding
A0008331molecular_functionhigh voltage-gated calcium channel activity
A0010959biological_processregulation of metal ion transport
A0016020cellular_componentmembrane
A0023052biological_processsignaling
A0030018cellular_componentZ disc
A0030315cellular_componentT-tubule
A0030506molecular_functionankyrin binding
A0034220biological_processmonoatomic ion transmembrane transport
A0034702cellular_componentmonoatomic ion channel complex
A0045762biological_processpositive regulation of adenylate cyclase activity
A0046872molecular_functionmetal ion binding
A0050877biological_processnervous system process
A0051050biological_processpositive regulation of transport
A0051393molecular_functionalpha-actinin binding
A0051928biological_processpositive regulation of calcium ion transport
A0055085biological_processtransmembrane transport
A0060372biological_processregulation of atrial cardiac muscle cell membrane repolarization
A0070509biological_processcalcium ion import
A0070588biological_processcalcium ion transmembrane transport
A0086002biological_processcardiac muscle cell action potential involved in contraction
A0086007molecular_functionvoltage-gated calcium channel activity involved in cardiac muscle cell action potential
A0086012biological_processmembrane depolarization during cardiac muscle cell action potential
A0086046biological_processmembrane depolarization during SA node cell action potential
A0086059molecular_functionvoltage-gated calcium channel activity involved SA node cell action potential
A0086091biological_processregulation of heart rate by cardiac conduction
A0098703biological_processcalcium ion import across plasma membrane
A1901379biological_processregulation of potassium ion transmembrane transport
A1990454cellular_componentL-type voltage-gated calcium channel complex
C0005245molecular_functionvoltage-gated calcium channel activity
C0005246molecular_functioncalcium channel regulator activity
C0005262molecular_functioncalcium channel activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005891cellular_componentvoltage-gated calcium channel complex
C0006811biological_processmonoatomic ion transport
C0006816biological_processcalcium ion transport
C0007268biological_processchemical synaptic transmission
C0008331molecular_functionhigh voltage-gated calcium channel activity
C0016020cellular_componentmembrane
C0034220biological_processmonoatomic ion transmembrane transport
C0034702cellular_componentmonoatomic ion channel complex
C0045202cellular_componentsynapse
C0050852biological_processT cell receptor signaling pathway
C0060402biological_processcalcium ion transport into cytosol
C0061577biological_processcalcium ion transmembrane transport via high voltage-gated calcium channel
C0070588biological_processcalcium ion transmembrane transport
C0072659biological_processprotein localization to plasma membrane
C0098903biological_processregulation of membrane repolarization during action potential
C1901843biological_processpositive regulation of high voltage-gated calcium channel activity
C1990454cellular_componentL-type voltage-gated calcium channel complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S1 of repeat I","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues364
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S3 of repeat I","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S4 of repeat I","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues141
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=S5 of repeat I","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=S6 of repeat I","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=S1 of repeat II","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S2 of repeat II","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S3 of repeat II","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S4 of repeat II","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=S5 of repeat II","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=S6 of repeat II","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S1 of repeat III","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=S2 of repeat III","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=S4 of repeat III","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=S5 of repeat III","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=S6 of repeat III","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S1 of repeat IV","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=S2 of repeat IV","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=S3 of repeat IV","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=S4 of repeat IV","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=S5 of repeat IV","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=S6 of repeat IV","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues17
DetailsRegion: {"description":"Binding to the beta subunit","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues156
DetailsRegion: {"description":"Dihydropyridine binding","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues43
DetailsRegion: {"description":"Phenylalkylamine binding","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues10
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues177
DetailsDomain: {"description":"VWFA","evidences":[{"source":"PROSITE-ProRule","id":"PRU00219","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues4
DetailsMotif: {"description":"MIDAS-like motif"}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues3
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P54290","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI34
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
site_idSWS_FT_FI35
Number of Residues69
DetailsDomain: {"description":"SH3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00192","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues41
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues150
DetailsRegion: {"description":"Mediates interaction with the alpha subunit","evidences":[{"source":"UniProtKB","id":"P54287","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI38
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P54287","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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