5GJV
Structure of the mammalian voltage-gated calcium channel Cav1.1 complex at near atomic resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0005886 | cellular_component | plasma membrane |
A | 0005891 | cellular_component | voltage-gated calcium channel complex |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0006936 | biological_process | muscle contraction |
A | 0008331 | molecular_function | high voltage-gated calcium channel activity |
A | 0016020 | cellular_component | membrane |
A | 0030315 | cellular_component | T-tubule |
A | 0034702 | cellular_component | monoatomic ion channel complex |
A | 0044325 | molecular_function | transmembrane transporter binding |
A | 0045933 | biological_process | positive regulation of muscle contraction |
A | 0046872 | molecular_function | metal ion binding |
A | 0051209 | biological_process | release of sequestered calcium ion into cytosol |
A | 0055085 | biological_process | transmembrane transport |
A | 0060314 | biological_process | regulation of ryanodine-sensitive calcium-release channel activity |
A | 0070588 | biological_process | calcium ion transmembrane transport |
A | 0071313 | biological_process | cellular response to caffeine |
A | 0098703 | biological_process | calcium ion import across plasma membrane |
A | 1990454 | cellular_component | L-type voltage-gated calcium channel complex |
B | 0005245 | molecular_function | voltage-gated calcium channel activity |
B | 0005891 | cellular_component | voltage-gated calcium channel complex |
B | 0070588 | biological_process | calcium ion transmembrane transport |
C | 0005245 | molecular_function | voltage-gated calcium channel activity |
C | 0005891 | cellular_component | voltage-gated calcium channel complex |
C | 0070588 | biological_process | calcium ion transmembrane transport |
E | 0005245 | molecular_function | voltage-gated calcium channel activity |
E | 0005246 | molecular_function | calcium channel regulator activity |
E | 0005262 | molecular_function | calcium channel activity |
E | 0005515 | molecular_function | protein binding |
E | 0005886 | cellular_component | plasma membrane |
E | 0005891 | cellular_component | voltage-gated calcium channel complex |
E | 0006816 | biological_process | calcium ion transport |
E | 0016020 | cellular_component | membrane |
E | 0030315 | cellular_component | T-tubule |
E | 0034702 | cellular_component | monoatomic ion channel complex |
E | 0042383 | cellular_component | sarcolemma |
E | 0045933 | biological_process | positive regulation of muscle contraction |
E | 0070588 | biological_process | calcium ion transmembrane transport |
E | 1902514 | biological_process | regulation of calcium ion transmembrane transport via high voltage-gated calcium channel |
E | 1990454 | cellular_component | L-type voltage-gated calcium channel complex |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1049 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
F | GLU27-GLY1076 | |
A | VAL1061-SER1118 | |
A | ALA1171-ASP1180 | |
A | GLU1251-PRO1268 | |
A | ASP1382-PRO1873 | |
E | ARG130-ASP134 | |
E | PRO205-HIS222 | |
A | GLY331-ARG432 | |
A | TYR484-SER494 | |
A | THR543-SER561 | |
A | ASN654-THR799 | |
A | MET851-ASN866 | |
A | LYS912-ASN930 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
F | VAL1077-LEU1097 | |
E | ALA109-PHE129 | |
E | TYR135-LEU155 | |
E | TRP180-LEU204 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
F | VAL1098-LEU1106 | |
A | GLU886-VAL892 | |
A | LYS951-VAL1000 | |
A | ARG1022-ARG1038 | |
A | HIS1141-HIS1148 | |
A | GLU1201-SER1231 | |
A | GLY1290-GLN1311 | |
A | ALA1331-PHE1356 | |
E | GLU156-SER179 | |
A | LYS219-GLY279 | |
A | ASN302-TRP309 | |
A | GLU452-HIS462 | |
A | GLU515-GLY523 | |
A | GLY582-PRO601 | |
A | ILE624-PRO633 | |
A | GLU819-GLN830 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
F | ASP261 | |
F | SER263 | |
F | SER265 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P54290 |
Chain | Residue | Details |
F | SER121 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
F | ASN94 | |
F | ASN133 | |
F | ASN186 | |
F | ASN326 | |
F | ASN350 | |
F | ASN615 | |
F | ASN784 | |
F | ASN891 |
site_id | SWS_FT_FI7 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=S5 of repeat I => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | PHE197-PHE218 |
site_id | SWS_FT_FI8 |
Number of Residues | 80 |
Details | INTRAMEM: Pore-forming => ECO:0000269|PubMed:26680202, ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | PHE280-VAL301 | |
A | GLN602-GLY623 | |
A | LEU1001-TYR1021 | |
A | ALA1312-LEU1330 |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S6 of repeat I => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | PRO310-LEU330 |
site_id | SWS_FT_FI10 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S1 of repeat II => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | VAL433-SER451 |
site_id | SWS_FT_FI11 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S2 of repeat II => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | LEU463-MET483 |
site_id | SWS_FT_FI12 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S3 of repeat II => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | ILE495-VAL514 |
site_id | SWS_FT_FI13 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S4 of repeat II => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | ILE524-TRP542 |
site_id | SWS_FT_FI14 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S5 of repeat II => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | LEU562-PHE581 |
site_id | SWS_FT_FI15 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S6 of repeat II => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | GLY634-LEU653 |
site_id | SWS_FT_FI16 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S1 of repeat III => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | TRP800-ALA818 |
site_id | SWS_FT_FI17 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S2 of repeat III => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | ILE831-LYS850 |
site_id | SWS_FT_FI18 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S3 of repeat III => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | TYR867-LEU885 |
site_id | SWS_FT_FI19 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S4 of repeat III => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | VAL893-ALA911 |
site_id | SWS_FT_FI20 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S5 of repeat III => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | ILE931-PHE950 |
site_id | SWS_FT_FI21 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=S6 of repeat III => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | VAL1039-PHE1060 |
site_id | SWS_FT_FI22 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=S1 of repeat IV => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | TYR1119-TYR1140 |
site_id | SWS_FT_FI23 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=S2 of repeat IV => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | ILE1149-LEU1170 |
site_id | SWS_FT_FI24 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S3 of repeat IV => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | PRO1181-SER1200 |
site_id | SWS_FT_FI25 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | SER1232-ALA1250 |
site_id | SWS_FT_FI26 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | TYR1269-PHE1289 |
site_id | SWS_FT_FI27 |
Number of Residues | 24 |
Details | TRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000269|PubMed:27580036 |
Chain | Residue | Details |
A | ALA1357-MET1381 |
site_id | SWS_FT_FI28 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27580036, ECO:0007744|PDB:5GJV |
Chain | Residue | Details |
A | GLU292 | |
A | GLU614 | |
A | GLU1014 |
site_id | SWS_FT_FI29 |
Number of Residues | 1 |
Details | SITE: Cleavage => ECO:0000305 |
Chain | Residue | Details |
A | PHE1690 |
site_id | SWS_FT_FI30 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q02789 |
Chain | Residue | Details |
A | SER393 | |
A | SER397 |
site_id | SWS_FT_FI31 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by PKA => ECO:0000305|PubMed:2844809 |
Chain | Residue | Details |
A | SER687 | |
A | SER1617 |
site_id | SWS_FT_FI32 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PKA and CAMK2 => ECO:0000305|PubMed:20937870 |
Chain | Residue | Details |
A | SER1575 |
site_id | SWS_FT_FI33 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by CK2 => ECO:0000305|PubMed:20937870 |
Chain | Residue | Details |
A | THR1579 |
site_id | SWS_FT_FI34 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN79 |
site_id | SWS_FT_FI35 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0007744|PDB:5GJV |
Chain | Residue | Details |
A | ASN257 |