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8HMA

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

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
E0005216molecular_functionmonoatomic ion channel activity
E0005245molecular_functionvoltage-gated calcium channel activity
E0005262molecular_functioncalcium channel activity
E0005516molecular_functioncalmodulin binding
E0005891cellular_componentvoltage-gated calcium channel complex
E0006811biological_processmonoatomic ion transport
E0016020cellular_componentmembrane
E0030315cellular_componentT-tubule
E0030425cellular_componentdendrite
E0034702cellular_componentmonoatomic ion channel complex
E0042383cellular_componentsarcolemma
E0042995cellular_componentcell projection
E0043204cellular_componentperikaryon
E0045202cellular_componentsynapse
E0045211cellular_componentpostsynaptic membrane
E0046872molecular_functionmetal ion binding
E0055085biological_processtransmembrane transport
E0070588biological_processcalcium ion transmembrane transport
E0098839cellular_componentpostsynaptic density membrane
H0005245molecular_functionvoltage-gated calcium channel activity
H0005262molecular_functioncalcium channel activity
H0005515molecular_functionprotein binding
H0005886cellular_componentplasma membrane
H0005891cellular_componentvoltage-gated calcium channel complex
H0006816biological_processcalcium ion transport
H0007268biological_processchemical synaptic transmission
H0007528biological_processneuromuscular junction development
H0007601biological_processvisual perception
H0008331molecular_functionhigh voltage-gated calcium channel activity
H0034702cellular_componentmonoatomic ion channel complex
H0042383cellular_componentsarcolemma
H0045933biological_processpositive regulation of muscle contraction
H0051015molecular_functionactin filament binding
H0051928biological_processpositive regulation of calcium ion transport
H0070509biological_processcalcium ion import
H0070588biological_processcalcium ion transmembrane transport
H0072659biological_processprotein localization to plasma membrane
H0086007molecular_functionvoltage-gated calcium channel activity involved in cardiac muscle cell action potential
H0086045biological_processmembrane depolarization during AV node cell action potential
H0086056molecular_functionvoltage-gated calcium channel activity involved in AV node cell action potential
H0086091biological_processregulation of heart rate by cardiac conduction
H0098684cellular_componentphotoreceptor ribbon synapse
H0098793cellular_componentpresynapse
H0098912biological_processmembrane depolarization during atrial cardiac muscle cell action potential
H0099509biological_processregulation of presynaptic cytosolic calcium ion concentration
H0099626molecular_functionvoltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels
H1901843biological_processpositive regulation of high voltage-gated calcium channel activity
H1904879biological_processpositive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel
H1990454cellular_componentL-type voltage-gated calcium channel complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1282
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
EMET1-LYS124
ELEU1202-GLN1259
EILE1312-SER1321
EGLU1440-LEU1457
EALA180-ASN188
EPRO252-LEU268
EGLY402-ASN524
ETYR576-SER586
EASN635-SER653
EASN746-THR900
ETHR973-GLN1007
EVAL1053-PHE1071

site_idSWS_FT_FI2
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat I => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
EPRO125-ILE143

site_idSWS_FT_FI3
Number of Residues335
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
ETYR144-ASN158
EARG1027-LYS1033
EASN1092-LEU1141
ESER1163-ASN1179
EPHE1282-LYS1289
EARG1370-PHE1420
ECYS1479-ALA1500
EVAL1520-ARG1547
EALA210-ASP232
EMET291-ALA350
EASN373-TRP380
EGLU544-GLU554
EGLU607-GLY615
EGLY674-PRO693
EILE716-PRO725
EGLU920-HIS931

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=S2 of repeat I => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
ELEU159-ILE179
FASN324
FASN475
FASN604
FASN675
FASN824
FASN888
FASN985
FASN998

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=S3 of repeat I => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
EALA189-SER209

site_idSWS_FT_FI6
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat I => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
EVAL233-VAL251

site_idSWS_FT_FI7
Number of Residues21
DetailsTRANSMEM: Helical; Name=S5 of repeat I => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
ELEU269-PHE290

site_idSWS_FT_FI8
Number of Residues80
DetailsINTRAMEM: Pore-forming => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
EPHE351-VAL372
EGLN694-GLY715
ETYR1142-ILE1162
EVAL1501-PHE1519

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=S6 of repeat I => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
EPRO381-LEU401

site_idSWS_FT_FI10
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat II => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
EVAL525-SER543

site_idSWS_FT_FI11
Number of Residues20
DetailsTRANSMEM: Helical; Name=S2 of repeat II => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
EVAL555-MET575

site_idSWS_FT_FI12
Number of Residues19
DetailsTRANSMEM: Helical; Name=S3 of repeat II => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
ELEU587-VAL606

site_idSWS_FT_FI13
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat II => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
EILE616-TRP634

site_idSWS_FT_FI14
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat II => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
ELEU654-PHE673

site_idSWS_FT_FI15
Number of Residues19
DetailsTRANSMEM: Helical; Name=S6 of repeat II => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
EGLY726-LEU745

site_idSWS_FT_FI16
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat III => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
EILE901-ALA919

site_idSWS_FT_FI17
Number of Residues20
DetailsTRANSMEM: Helical; Name=S2 of repeat III => ECO:0000255
ChainResidueDetails
EILE932-MET972

site_idSWS_FT_FI18
Number of Residues18
DetailsTRANSMEM: Helical; Name=S3 of repeat III => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
ESER1008-LEU1026

site_idSWS_FT_FI19
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat III => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
EGLY1034-ILE1052

site_idSWS_FT_FI20
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat III => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
ELYS1072-GLY1091

site_idSWS_FT_FI21
Number of Residues21
DetailsTRANSMEM: Helical; Name=S6 of repeat III => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
EILE1180-GLU1201

site_idSWS_FT_FI22
Number of Residues21
DetailsTRANSMEM: Helical; Name=S1 of repeat IV => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
EHIS1260-LEU1281

site_idSWS_FT_FI23
Number of Residues21
DetailsTRANSMEM: Helical; Name=S2 of repeat IV => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
ELEU1290-VAL1311

site_idSWS_FT_FI24
Number of Residues19
DetailsTRANSMEM: Helical; Name=S3 of repeat IV => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
EGLU1350-SER1369

site_idSWS_FT_FI25
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
EILE1421-THR1439

site_idSWS_FT_FI26
Number of Residues20
DetailsTRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
EPHE1458-LYS1478

site_idSWS_FT_FI27
Number of Residues24
DetailsTRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
EILE1548-ILE1572

site_idSWS_FT_FI28
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
EGLU363
EGLU706
EILE1155

site_idSWS_FT_FI29
Number of Residues3
DetailsSITE: Calcium ion selectivity and permeability => ECO:0000269|PubMed:8099908
ChainResidueDetails
EGLU363
EILE1155
EALA1512

site_idSWS_FT_FI30
Number of Residues5
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q01815
ChainResidueDetails
ESER469
ESER808
ESER815
EPHE1766
EASP1787

site_idSWS_FT_FI31
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q01815
ChainResidueDetails
ETHR476

site_idSWS_FT_FI32
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:28119464
ChainResidueDetails
EALA2029

site_idSWS_FT_FI33
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
EASN153
EASN328
EGLU1484
ESER1535

227344

PDB entries from 2024-11-13

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