8FD7
Structure of the human L-type voltage-gated calcium channel Cav1.2 complexed with gabapentin
Functional Information from GO Data
Chain | GOid | namespace | contents |
C | 0005245 | molecular_function | voltage-gated calcium channel activity |
C | 0005246 | molecular_function | calcium channel regulator activity |
C | 0005262 | molecular_function | calcium channel activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005891 | cellular_component | voltage-gated calcium channel complex |
C | 0034702 | cellular_component | monoatomic ion channel complex |
C | 0061577 | biological_process | calcium ion transmembrane transport via high voltage-gated calcium channel |
C | 0070588 | biological_process | calcium ion transmembrane transport |
C | 1901843 | biological_process | positive regulation of high voltage-gated calcium channel activity |
C | 1990454 | cellular_component | L-type voltage-gated calcium channel complex |
K | 0005216 | molecular_function | monoatomic ion channel activity |
K | 0005245 | molecular_function | voltage-gated calcium channel activity |
K | 0005891 | cellular_component | voltage-gated calcium channel complex |
K | 0006811 | biological_process | monoatomic ion transport |
K | 0016020 | cellular_component | membrane |
K | 0055085 | biological_process | transmembrane transport |
K | 0070588 | biological_process | calcium ion transmembrane transport |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P54287 |
Chain | Residue | Details |
C | SER152 | |
K | LEU1182-GLN1239 | |
K | VAL1292-THR1301 | |
K | GLU1392-LEU1409 | |
C | SER393 | |
K | PRO252-LEU268 | |
K | GLY402-ASN524 | |
K | TYR576-SER586 | |
K | ASN635-SER653 | |
K | ASN746-THR900 | |
K | THR953-GLN987 | |
K | VAL1033-PHE1051 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S1 of repeat I => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | PRO125-ILE143 |
site_id | SWS_FT_FI3 |
Number of Residues | 335 |
Details | TOPO_DOM: Extracellular => ECO:0000305 |
Chain | Residue | Details |
K | TYR144-ASN158 | |
K | ARG1007-LYS1013 | |
K | ASN1072-LEU1121 | |
K | SER1143-ASN1159 | |
K | PHE1262-LYS1269 | |
K | ARG1322-PHE1372 | |
K | CYS1431-ALA1452 | |
K | VAL1472-ARG1499 | |
K | ALA210-ASP232 | |
K | MET291-ALA350 | |
K | ASN373-TRP380 | |
K | GLU544-GLU554 | |
K | GLU607-GLY615 | |
K | GLY674-PRO693 | |
K | ILE716-PRO725 | |
K | 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 |
K | LEU159-ILE179 | |
D | SER263 | |
D | SER265 |
site_id | SWS_FT_FI5 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S3 of repeat I => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | 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 |
K | VAL233-VAL251 | |
D | ASN138 | |
D | ASN186 | |
D | ASN326 | |
D | ASN350 | |
D | ASN615 | |
D | LYS784 | |
D | ILE891 |
site_id | SWS_FT_FI7 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=S5 of repeat I => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | LEU269-PHE290 |
site_id | SWS_FT_FI8 |
Number of Residues | 80 |
Details | INTRAMEM: Pore-forming => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | PHE351-VAL372 | |
K | GLN694-GLY715 | |
K | TYR1122-ILE1142 | |
K | VAL1453-PHE1471 |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S6 of repeat I => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | 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 |
K | 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 |
K | 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 |
K | 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 |
K | 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 |
K | 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 |
K | 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 |
K | ILE901-ALA919 |
site_id | SWS_FT_FI17 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S2 of repeat III => ECO:0000255 |
Chain | Residue | Details |
K | ILE932-MET952 |
site_id | SWS_FT_FI18 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S3 of repeat III => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | SER988-LEU1006 |
site_id | SWS_FT_FI19 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S4 of repeat III => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | GLY1014-ILE1032 |
site_id | SWS_FT_FI20 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S5 of repeat III => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | LYS1052-GLY1071 |
site_id | SWS_FT_FI21 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=S6 of repeat III => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | ILE1160-GLU1181 |
site_id | SWS_FT_FI22 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=S1 of repeat IV => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | HIS1240-LEU1261 |
site_id | SWS_FT_FI23 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=S2 of repeat IV => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | LEU1270-VAL1291 |
site_id | SWS_FT_FI24 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S3 of repeat IV => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | GLU1302-SER1321 |
site_id | SWS_FT_FI25 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | ILE1373-THR1391 |
site_id | SWS_FT_FI26 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | PHE1410-LYS1430 |
site_id | SWS_FT_FI27 |
Number of Residues | 24 |
Details | TRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | ILE1500-ILE1524 |
site_id | SWS_FT_FI28 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P07293 |
Chain | Residue | Details |
K | GLU363 | |
K | GLU706 | |
K | ILE1135 |
site_id | SWS_FT_FI29 |
Number of Residues | 3 |
Details | SITE: Calcium ion selectivity and permeability => ECO:0000269|PubMed:8099908 |
Chain | Residue | Details |
K | GLU363 | |
K | ILE1135 | |
K | ALA1464 |
site_id | SWS_FT_FI30 |
Number of Residues | 3 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q01815 |
Chain | Residue | Details |
K | SER469 | |
K | SER808 | |
K | SER815 |
site_id | SWS_FT_FI31 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q01815 |
Chain | Residue | Details |
K | THR476 |
site_id | SWS_FT_FI32 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
K | ASN153 | |
K | ASN328 | |
K | GLU1436 | |
K | SER1487 |