4DJC
1.35 A crystal structure of the NaV1.5 DIII-IV-Ca/CaM complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000086 | biological_process | G2/M transition of mitotic cell cycle |
A | 0000922 | cellular_component | spindle pole |
A | 0002027 | biological_process | regulation of heart rate |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005513 | biological_process | detection of calcium ion |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005813 | cellular_component | centrosome |
A | 0005819 | cellular_component | spindle |
A | 0005829 | cellular_component | cytosol |
A | 0005856 | cellular_component | cytoskeleton |
A | 0005876 | cellular_component | spindle microtubule |
A | 0005886 | cellular_component | plasma membrane |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0008076 | cellular_component | voltage-gated potassium channel complex |
A | 0010800 | biological_process | positive regulation of peptidyl-threonine phosphorylation |
A | 0010801 | biological_process | negative regulation of peptidyl-threonine phosphorylation |
A | 0010856 | molecular_function | adenylate cyclase activator activity |
A | 0010880 | biological_process | regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
A | 0010881 | biological_process | regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion |
A | 0016020 | cellular_component | membrane |
A | 0016240 | biological_process | autophagosome membrane docking |
A | 0019855 | molecular_function | calcium channel inhibitor activity |
A | 0019901 | molecular_function | protein kinase binding |
A | 0021762 | biological_process | substantia nigra development |
A | 0030017 | cellular_component | sarcomere |
A | 0031432 | molecular_function | titin binding |
A | 0031514 | cellular_component | motile cilium |
A | 0031954 | biological_process | positive regulation of protein autophosphorylation |
A | 0031982 | cellular_component | vesicle |
A | 0032465 | biological_process | regulation of cytokinesis |
A | 0032516 | biological_process | obsolete positive regulation of phosphoprotein phosphatase activity |
A | 0032991 | cellular_component | protein-containing complex |
A | 0034704 | cellular_component | calcium channel complex |
A | 0035307 | biological_process | obsolete positive regulation of protein dephosphorylation |
A | 0035458 | biological_process | cellular response to interferon-beta |
A | 0043209 | cellular_component | myelin sheath |
A | 0043539 | molecular_function | protein serine/threonine kinase activator activity |
A | 0044305 | cellular_component | calyx of Held |
A | 0044325 | molecular_function | transmembrane transporter binding |
A | 0046427 | biological_process | positive regulation of receptor signaling pathway via JAK-STAT |
A | 0046872 | molecular_function | metal ion binding |
A | 0048306 | molecular_function | calcium-dependent protein binding |
A | 0050848 | biological_process | regulation of calcium-mediated signaling |
A | 0051343 | biological_process | positive regulation of cyclic-nucleotide phosphodiesterase activity |
A | 0051592 | biological_process | response to calcium ion |
A | 0055117 | biological_process | regulation of cardiac muscle contraction |
A | 0060314 | biological_process | regulation of ryanodine-sensitive calcium-release channel activity |
A | 0060315 | biological_process | negative regulation of ryanodine-sensitive calcium-release channel activity |
A | 0060316 | biological_process | positive regulation of ryanodine-sensitive calcium-release channel activity |
A | 0071346 | biological_process | cellular response to type II interferon |
A | 0071902 | biological_process | positive regulation of protein serine/threonine kinase activity |
A | 0072542 | molecular_function | protein phosphatase activator activity |
A | 0097225 | cellular_component | sperm midpiece |
A | 0098901 | biological_process | regulation of cardiac muscle cell action potential |
A | 0099523 | cellular_component | presynaptic cytosol |
A | 0140056 | biological_process | organelle localization by membrane tethering |
A | 0140238 | biological_process | presynaptic endocytosis |
A | 1901020 | biological_process | negative regulation of calcium ion transmembrane transporter activity |
A | 1901842 | biological_process | negative regulation of high voltage-gated calcium channel activity |
A | 1901844 | biological_process | regulation of cell communication by electrical coupling involved in cardiac conduction |
A | 1902494 | cellular_component | catalytic complex |
A | 1905913 | biological_process | negative regulation of calcium ion export across plasma membrane |
A | 1990456 | biological_process | mitochondrion-endoplasmic reticulum membrane tethering |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 201 |
Chain | Residue |
A | ASP21 |
A | ASP23 |
A | ASP25 |
A | THR27 |
A | GLU32 |
A | HOH346 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 202 |
Chain | Residue |
A | THR63 |
A | GLU68 |
A | HOH344 |
A | ASP57 |
A | ASP59 |
A | ASN61 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 203 |
Chain | Residue |
A | ASP94 |
A | ASP96 |
A | ASN98 |
A | TYR100 |
A | GLU105 |
A | HOH316 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 204 |
Chain | Residue |
A | ASP130 |
A | ASP132 |
A | ASP134 |
A | GLN136 |
A | GLU141 |
A | HOH348 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IPA A 205 |
Chain | Residue |
A | LYS14 |
A | PHE66 |
A | ASP134 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IPA A 206 |
Chain | Residue |
A | ALA47 |
A | ASP123 |
A | HOH383 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IPA A 207 |
Chain | Residue |
A | TYR100 |
A | HOH302 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE IPA A 208 |
Chain | Residue |
A | THR30 |
A | LYS31 |
A | ASP59 |
A | GLY60 |
A | ASP96 |
A | ASN98 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IPA A 209 |
Chain | Residue |
A | ILE64 |
A | MET72 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IPA A 210 |
Chain | Residue |
A | GLY24 |
A | ARG127 |
A | GLY135 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IPA A 212 |
Chain | Residue |
A | THR30 |
A | GLN50 |
A | ALA58 |
A | HOH364 |
A | HOH450 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IPA A 213 |
Chain | Residue |
A | MET37 |
A | GLN42 |
A | GLU48 |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL |
Chain | Residue | Details |
A | ASP21-LEU33 | |
A | ASP57-PHE69 | |
A | ASP94-LEU106 | |
A | ASP130-PHE142 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PKC => ECO:0000305|PubMed:19666841 |
Chain | Residue | Details |
B | SER1503 | |
A | GLU68 | |
A | ASP23 | |
A | ASP25 | |
A | THR27 | |
A | GLU32 | |
A | ASP57 | |
A | ASP59 | |
A | ASN61 | |
A | THR63 |
site_id | SWS_FT_FI2 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0000269|PubMed:29724949, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03, ECO:0007744|PDB:6CNN, ECO:0007744|PDB:6CNO |
Chain | Residue | Details |
A | ASP94 | |
A | ASP96 | |
A | ASN98 | |
A | TYR100 | |
A | GLU105 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 |
Chain | Residue | Details |
A | ASP130 | |
A | ASP132 | |
A | ASP134 | |
A | GLN136 | |
A | GLU141 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:7093203, ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712 |
Chain | Residue | Details |
A | ALA2 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS22 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29 |
Chain | Residue | Details |
A | THR45 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER82 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS95 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
A | TYR100 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER102 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | THR111 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315 |
Chain | Residue | Details |
A | LYS116 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
A | TYR139 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157 |
Chain | Residue | Details |
A | LYS22 |