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
Chain | GOid | namespace | contents |
E | 0005216 | molecular_function | monoatomic ion channel activity |
E | 0005245 | molecular_function | voltage-gated calcium channel activity |
E | 0005262 | molecular_function | calcium channel activity |
E | 0005516 | molecular_function | calmodulin binding |
E | 0005891 | cellular_component | voltage-gated calcium channel complex |
E | 0006811 | biological_process | monoatomic ion transport |
E | 0016020 | cellular_component | membrane |
E | 0030315 | cellular_component | T-tubule |
E | 0030425 | cellular_component | dendrite |
E | 0034702 | cellular_component | monoatomic ion channel complex |
E | 0042383 | cellular_component | sarcolemma |
E | 0042995 | cellular_component | cell projection |
E | 0043204 | cellular_component | perikaryon |
E | 0045202 | cellular_component | synapse |
E | 0045211 | cellular_component | postsynaptic membrane |
E | 0046872 | molecular_function | metal ion binding |
E | 0055085 | biological_process | transmembrane transport |
E | 0070588 | biological_process | calcium ion transmembrane transport |
E | 0098839 | cellular_component | postsynaptic density membrane |
H | 0005245 | molecular_function | voltage-gated calcium channel activity |
H | 0005262 | molecular_function | calcium channel activity |
H | 0005515 | molecular_function | protein binding |
H | 0005886 | cellular_component | plasma membrane |
H | 0005891 | cellular_component | voltage-gated calcium channel complex |
H | 0006816 | biological_process | calcium ion transport |
H | 0007268 | biological_process | chemical synaptic transmission |
H | 0007528 | biological_process | neuromuscular junction development |
H | 0007601 | biological_process | visual perception |
H | 0008331 | molecular_function | high voltage-gated calcium channel activity |
H | 0034702 | cellular_component | monoatomic ion channel complex |
H | 0042383 | cellular_component | sarcolemma |
H | 0045933 | biological_process | positive regulation of muscle contraction |
H | 0051015 | molecular_function | actin filament binding |
H | 0051928 | biological_process | positive regulation of calcium ion transport |
H | 0070509 | biological_process | calcium ion import |
H | 0070588 | biological_process | calcium ion transmembrane transport |
H | 0072659 | biological_process | protein localization to plasma membrane |
H | 0086007 | molecular_function | voltage-gated calcium channel activity involved in cardiac muscle cell action potential |
H | 0086045 | biological_process | membrane depolarization during AV node cell action potential |
H | 0086056 | molecular_function | voltage-gated calcium channel activity involved in AV node cell action potential |
H | 0086091 | biological_process | regulation of heart rate by cardiac conduction |
H | 0098684 | cellular_component | photoreceptor ribbon synapse |
H | 0098793 | cellular_component | presynapse |
H | 0098912 | biological_process | membrane depolarization during atrial cardiac muscle cell action potential |
H | 0099509 | biological_process | regulation of presynaptic cytosolic calcium ion concentration |
H | 0099626 | molecular_function | voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels |
H | 1901843 | biological_process | positive regulation of high voltage-gated calcium channel activity |
H | 1904879 | biological_process | positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel |
H | 1990454 | cellular_component | L-type voltage-gated calcium channel complex |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1282 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
Chain | Residue | Details |
E | MET1-LYS124 | |
E | LEU1202-GLN1259 | |
E | ILE1312-SER1321 | |
E | GLU1440-LEU1457 | |
E | ALA180-ASN188 | |
E | PRO252-LEU268 | |
E | GLY402-ASN524 | |
E | TYR576-SER586 | |
E | ASN635-SER653 | |
E | ASN746-THR900 | |
E | THR973-GLN1007 | |
E | VAL1053-PHE1071 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S1 of repeat I => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | PRO125-ILE143 |
site_id | SWS_FT_FI3 |
Number of Residues | 335 |
Details | TOPO_DOM: Extracellular => ECO:0000305 |
Chain | Residue | Details |
E | TYR144-ASN158 | |
E | ARG1027-LYS1033 | |
E | ASN1092-LEU1141 | |
E | SER1163-ASN1179 | |
E | PHE1282-LYS1289 | |
E | ARG1370-PHE1420 | |
E | CYS1479-ALA1500 | |
E | VAL1520-ARG1547 | |
E | ALA210-ASP232 | |
E | MET291-ALA350 | |
E | ASN373-TRP380 | |
E | GLU544-GLU554 | |
E | GLU607-GLY615 | |
E | GLY674-PRO693 | |
E | ILE716-PRO725 | |
E | GLU920-HIS931 |
site_id | SWS_FT_FI4 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S2 of repeat I => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | LEU159-ILE179 | |
F | ASN324 | |
F | ASN475 | |
F | ASN604 | |
F | ASN675 | |
F | ASN824 | |
F | ASN888 | |
F | ASN985 | |
F | ASN998 |
site_id | SWS_FT_FI5 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S3 of repeat I => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | ALA189-SER209 |
site_id | SWS_FT_FI6 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S4 of repeat I => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | VAL233-VAL251 |
site_id | SWS_FT_FI7 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=S5 of repeat I => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | LEU269-PHE290 |
site_id | SWS_FT_FI8 |
Number of Residues | 80 |
Details | INTRAMEM: Pore-forming => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | PHE351-VAL372 | |
E | GLN694-GLY715 | |
E | TYR1142-ILE1162 | |
E | VAL1501-PHE1519 |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S6 of repeat I => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | PRO381-LEU401 |
site_id | SWS_FT_FI10 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S1 of repeat II => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | VAL525-SER543 |
site_id | SWS_FT_FI11 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S2 of repeat II => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | VAL555-MET575 |
site_id | SWS_FT_FI12 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S3 of repeat II => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | LEU587-VAL606 |
site_id | SWS_FT_FI13 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S4 of repeat II => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | ILE616-TRP634 |
site_id | SWS_FT_FI14 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S5 of repeat II => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | LEU654-PHE673 |
site_id | SWS_FT_FI15 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S6 of repeat II => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | GLY726-LEU745 |
site_id | SWS_FT_FI16 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S1 of repeat III => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | ILE901-ALA919 |
site_id | SWS_FT_FI17 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S2 of repeat III => ECO:0000255 |
Chain | Residue | Details |
E | ILE932-MET972 |
site_id | SWS_FT_FI18 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S3 of repeat III => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | SER1008-LEU1026 |
site_id | SWS_FT_FI19 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S4 of repeat III => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | GLY1034-ILE1052 |
site_id | SWS_FT_FI20 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S5 of repeat III => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | LYS1072-GLY1091 |
site_id | SWS_FT_FI21 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=S6 of repeat III => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | ILE1180-GLU1201 |
site_id | SWS_FT_FI22 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=S1 of repeat IV => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | HIS1260-LEU1281 |
site_id | SWS_FT_FI23 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=S2 of repeat IV => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | LEU1290-VAL1311 |
site_id | SWS_FT_FI24 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S3 of repeat IV => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | GLU1350-SER1369 |
site_id | SWS_FT_FI25 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | ILE1421-THR1439 |
site_id | SWS_FT_FI26 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | PHE1458-LYS1478 |
site_id | SWS_FT_FI27 |
Number of Residues | 24 |
Details | TRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | ILE1548-ILE1572 |
site_id | SWS_FT_FI28 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
E | GLU363 | |
E | GLU706 | |
E | ILE1155 |
site_id | SWS_FT_FI29 |
Number of Residues | 3 |
Details | SITE: Calcium ion selectivity and permeability => ECO:0000269|PubMed:8099908 |
Chain | Residue | Details |
E | GLU363 | |
E | ILE1155 | |
E | ALA1512 |
site_id | SWS_FT_FI30 |
Number of Residues | 5 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q01815 |
Chain | Residue | Details |
E | SER469 | |
E | SER808 | |
E | SER815 | |
E | PHE1766 | |
E | ASP1787 |
site_id | SWS_FT_FI31 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q01815 |
Chain | Residue | Details |
E | THR476 |
site_id | SWS_FT_FI32 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:28119464 |
Chain | Residue | Details |
E | ALA2029 |
site_id | SWS_FT_FI33 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
E | ASN153 | |
E | ASN328 | |
E | GLU1484 | |
E | SER1535 |