8WEA
Human L-type voltage-gated calcium channel Cav1.2 (Class II) in the presence of pinaverium at 3.2 Angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002520 | biological_process | immune system development |
| A | 0005216 | molecular_function | monoatomic ion channel activity |
| A | 0005245 | molecular_function | voltage-gated calcium channel activity |
| A | 0005262 | molecular_function | calcium channel activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005516 | molecular_function | calmodulin binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005891 | cellular_component | voltage-gated calcium channel complex |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0007204 | biological_process | positive regulation of cytosolic calcium ion concentration |
| A | 0007507 | biological_process | heart development |
| A | 0008331 | molecular_function | high voltage-gated calcium channel activity |
| A | 0010881 | biological_process | regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion |
| A | 0014069 | cellular_component | postsynaptic density |
| A | 0016020 | cellular_component | membrane |
| A | 0030018 | cellular_component | Z disc |
| A | 0030315 | cellular_component | T-tubule |
| A | 0030425 | cellular_component | dendrite |
| A | 0034702 | cellular_component | monoatomic ion channel complex |
| A | 0035115 | biological_process | embryonic forelimb morphogenesis |
| A | 0042383 | cellular_component | sarcolemma |
| A | 0042995 | cellular_component | cell projection |
| A | 0043010 | biological_process | camera-type eye development |
| A | 0043204 | cellular_component | perikaryon |
| A | 0045202 | cellular_component | synapse |
| A | 0045211 | cellular_component | postsynaptic membrane |
| A | 0045762 | biological_process | positive regulation of adenylate cyclase activity |
| A | 0045933 | biological_process | positive regulation of muscle contraction |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051393 | molecular_function | alpha-actinin binding |
| A | 0055085 | biological_process | transmembrane transport |
| A | 0060402 | biological_process | calcium ion transport into cytosol |
| A | 0061337 | biological_process | cardiac conduction |
| A | 0061577 | biological_process | calcium ion transmembrane transport via high voltage-gated calcium channel |
| A | 0070588 | biological_process | calcium ion transmembrane transport |
| A | 0086002 | biological_process | cardiac muscle cell action potential involved in contraction |
| A | 0086007 | molecular_function | voltage-gated calcium channel activity involved in cardiac muscle cell action potential |
| A | 0086012 | biological_process | membrane depolarization during cardiac muscle cell action potential |
| A | 0086045 | biological_process | membrane depolarization during AV node cell action potential |
| A | 0086056 | molecular_function | voltage-gated calcium channel activity involved in AV node cell action potential |
| A | 0086064 | biological_process | cell communication by electrical coupling involved in cardiac conduction |
| A | 0086091 | biological_process | regulation of heart rate by cardiac conduction |
| A | 0098703 | biological_process | calcium ion import across plasma membrane |
| A | 0098839 | cellular_component | postsynaptic density membrane |
| A | 0098911 | biological_process | regulation of ventricular cardiac muscle cell action potential |
| A | 0098912 | biological_process | membrane depolarization during atrial cardiac muscle cell action potential |
| A | 1990454 | cellular_component | L-type voltage-gated calcium channel complex |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1048 |
| Details | TOPO_DOM: Extracellular => ECO:0000255 |
| Chain | Residue | Details |
| D | GLU25-GLY1073 | |
| A | LEU1202-GLN1259 | |
| A | ILE1312-SER1321 | |
| A | ALA1412-VAL1429 | |
| A | ALA180-ASN188 | |
| A | PRO252-LEU268 | |
| A | GLY402-ASN524 | |
| A | TYR576-SER586 | |
| A | ASN635-SER653 | |
| A | ASN746-THR900 | |
| A | THR973-GLN1007 | |
| A | VAL1053-PHE1071 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| D | VAL1074-LEU1094 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
| Chain | Residue | Details |
| D | VAL1095-LEU1103 | |
| A | ARG1027-LYS1033 | |
| A | ASN1092-LEU1141 | |
| A | SER1163-ASN1179 | |
| A | PHE1282-LYS1289 | |
| A | SER1342-GLU1392 | |
| A | PRO1451-ALA1472 | |
| A | GLU1492-PHE1519 | |
| A | ALA210-ASP232 | |
| A | MET291-ALA350 | |
| A | ASN373-TRP380 | |
| A | GLU544-GLU554 | |
| A | GLU607-GLY615 | |
| A | GLY674-PRO693 | |
| A | ILE716-PRO725 | |
| A | GLU920-HIS931 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| D | ASP259 | |
| D | SER261 | |
| D | SER263 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P54290 |
| Chain | Residue | Details |
| D | SER119 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 7 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY |
| Chain | Residue | Details |
| D | ASN92 | |
| D | ASN184 | |
| D | ASN348 | |
| D | ASN468 | |
| D | ASN613 | |
| D | ASN781 | |
| D | ASN895 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 9 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| D | ASN136 | |
| D | ASN324 | |
| D | ASN475 | |
| D | ASN604 | |
| D | ASN675 | |
| D | ASN824 | |
| D | ASN888 | |
| D | ASN985 | |
| D | ASN998 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 80 |
| Details | INTRAMEM: Pore-forming => ECO:0000250|UniProtKB:P07293 |
| Chain | Residue | Details |
| A | PHE351-VAL372 | |
| A | GLN694-GLY715 | |
| A | TYR1142-ILE1162 | |
| A | CYS1473-GLY1491 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=S6 of repeat I => ECO:0000250|UniProtKB:P07293 |
| Chain | Residue | Details |
| A | 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 |
| A | 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 |
| A | 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 |
| A | 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 |
| A | 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 |
| A | 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 |
| A | 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 |
| A | ILE901-ALA919 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=S2 of repeat III => ECO:0000255 |
| Chain | Residue | Details |
| A | ILE952-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 |
| A | 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 |
| A | 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 |
| A | 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 |
| A | 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 |
| A | 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 |
| A | 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 |
| A | GLU1322-GLY1341 |
| site_id | SWS_FT_FI25 |
| Number of Residues | 18 |
| Details | TRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000250|UniProtKB:P07293 |
| Chain | Residue | Details |
| A | GLY1393-VAL1411 |
| site_id | SWS_FT_FI26 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000250|UniProtKB:P07293 |
| Chain | Residue | Details |
| A | PHE1430-PHE1450 |
| site_id | SWS_FT_FI27 |
| Number of Residues | 24 |
| Details | TRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000250|UniProtKB:P07293 |
| Chain | Residue | Details |
| A | VAL1520-GLU1544 |
| site_id | SWS_FT_FI28 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P07293 |
| Chain | Residue | Details |
| A | GLU363 | |
| A | GLU706 | |
| A | ILE1155 |
| site_id | SWS_FT_FI29 |
| Number of Residues | 3 |
| Details | SITE: Calcium ion selectivity and permeability => ECO:0000269|PubMed:8099908 |
| Chain | Residue | Details |
| A | GLU363 | |
| A | ILE1155 | |
| A | GLU1484 |
| site_id | SWS_FT_FI30 |
| Number of Residues | 5 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q01815 |
| Chain | Residue | Details |
| A | SER469 | |
| A | SER808 | |
| A | SER815 | |
| A | ALA1738 | |
| A | GLN1759 |
| site_id | SWS_FT_FI31 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q01815 |
| Chain | Residue | Details |
| A | THR476 |
| site_id | SWS_FT_FI32 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:28119464 |
| Chain | Residue | Details |
| A | THR2001 |
| site_id | SWS_FT_FI33 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN153 | |
| A | ASN328 | |
| A | LEU1456 | |
| A | PHE1507 |
