6MBA
Crystal Structure of Human Nav1.4 CTerminal Domain in Complex with apo Calmodulin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005261 | molecular_function | monoatomic cation channel activity |
| A | 0005886 | cellular_component | plasma membrane |
| B | 0000086 | biological_process | G2/M transition of mitotic cell cycle |
| B | 0000922 | cellular_component | spindle pole |
| B | 0001975 | biological_process | response to amphetamine |
| B | 0002027 | biological_process | regulation of heart rate |
| B | 0005246 | molecular_function | calcium channel regulator activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005513 | biological_process | detection of calcium ion |
| B | 0005515 | molecular_function | protein binding |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005813 | cellular_component | centrosome |
| B | 0005819 | cellular_component | spindle |
| B | 0005829 | cellular_component | cytosol |
| B | 0005856 | cellular_component | cytoskeleton |
| B | 0005876 | cellular_component | spindle microtubule |
| B | 0005929 | cellular_component | cilium |
| B | 0008076 | cellular_component | voltage-gated potassium channel complex |
| B | 0008179 | molecular_function | adenylate cyclase binding |
| B | 0010856 | molecular_function | adenylate cyclase activator activity |
| B | 0010880 | biological_process | regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
| B | 0010881 | biological_process | regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion |
| B | 0016020 | cellular_component | membrane |
| B | 0016240 | biological_process | autophagosome membrane docking |
| B | 0019855 | molecular_function | calcium channel inhibitor activity |
| B | 0019901 | molecular_function | protein kinase binding |
| B | 0019904 | molecular_function | protein domain specific binding |
| B | 0030017 | cellular_component | sarcomere |
| B | 0030235 | molecular_function | nitric-oxide synthase regulator activity |
| B | 0030426 | cellular_component | growth cone |
| B | 0030672 | cellular_component | synaptic vesicle membrane |
| B | 0031432 | molecular_function | titin binding |
| B | 0031514 | cellular_component | motile cilium |
| B | 0031800 | molecular_function | type 3 metabotropic glutamate receptor binding |
| B | 0031966 | cellular_component | mitochondrial membrane |
| B | 0031982 | cellular_component | vesicle |
| B | 0032465 | biological_process | regulation of cytokinesis |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0034704 | cellular_component | calcium channel complex |
| B | 0035458 | biological_process | cellular response to interferon-beta |
| B | 0042995 | cellular_component | cell projection |
| B | 0043209 | cellular_component | myelin sheath |
| B | 0043539 | molecular_function | protein serine/threonine kinase activator activity |
| B | 0043548 | molecular_function | phosphatidylinositol 3-kinase binding |
| B | 0044305 | cellular_component | calyx of Held |
| B | 0044325 | molecular_function | transmembrane transporter binding |
| B | 0046427 | biological_process | positive regulation of receptor signaling pathway via JAK-STAT |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048306 | molecular_function | calcium-dependent protein binding |
| B | 0050848 | biological_process | regulation of calcium-mediated signaling |
| B | 0050998 | molecular_function | nitric-oxide synthase binding |
| B | 0051592 | biological_process | response to calcium ion |
| B | 0055117 | biological_process | regulation of cardiac muscle contraction |
| B | 0060314 | biological_process | regulation of ryanodine-sensitive calcium-release channel activity |
| B | 0060315 | biological_process | negative regulation of ryanodine-sensitive calcium-release channel activity |
| B | 0071346 | biological_process | cellular response to type II interferon |
| B | 0072542 | molecular_function | protein phosphatase activator activity |
| B | 0090150 | biological_process | establishment of protein localization to membrane |
| B | 0090151 | biological_process | establishment of protein localization to mitochondrial membrane |
| B | 0097225 | cellular_component | sperm midpiece |
| B | 0097720 | biological_process | calcineurin-mediated signaling |
| B | 0098685 | cellular_component | Schaffer collateral - CA1 synapse |
| B | 0098901 | biological_process | regulation of cardiac muscle cell action potential |
| B | 0099523 | cellular_component | presynaptic cytosol |
| B | 0099524 | cellular_component | postsynaptic cytosol |
| B | 0140056 | biological_process | organelle localization by membrane tethering |
| B | 0140238 | biological_process | presynaptic endocytosis |
| B | 0141110 | molecular_function | transporter inhibitor activity |
| B | 1900242 | biological_process | regulation of synaptic vesicle endocytosis |
| B | 1902494 | cellular_component | catalytic complex |
| B | 1905913 | biological_process | negative regulation of calcium ion export across plasma membrane |
| B | 1990456 | biological_process | mitochondrion-endoplasmic reticulum membrane tethering |
| B | 2000300 | biological_process | regulation of synaptic vesicle exocytosis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 2001 |
| Chain | Residue |
| A | LYS1673 |
| A | ARG1745 |
| B | GLU123 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 2002 |
| Chain | Residue |
| A | PRO1656 |
| A | ASN1657 |
| A | LYS1658 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 201 |
| Chain | Residue |
| B | ASP24 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 202 |
| Chain | Residue |
| B | GLU82 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 203 |
| Chain | Residue |
| B | ASP118 |
| B | GLU119 |
| B | GLN135 |
| B | HOH307 |
| B | THR117 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue CO3 B 204 |
| Chain | Residue |
| B | PHE92 |
| B | LYS94 |
| B | ILE100 |
| B | SER101 |
| B | GLU104 |
| B | HOH303 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue TRS B 205 |
| Chain | Residue |
| A | PRO1670 |
| A | GLY1671 |
| A | ILE1718 |
| A | HOH2106 |
| B | ALA102 |
| B | ARG106 |
| B | ASP129 |
| B | GLY134 |
| B | HOH320 |
| B | HOH358 |
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 |
| B | ASP20-LEU32 | |
| B | ASP56-PHE68 | |
| B | ASP93-LEU105 | |
| B | ASP129-PHE141 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:11323678, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1G4Y, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3B32, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3IFK, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4G27, ECO:0007744|PDB:4G28, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4J9Y, ECO:0007744|PDB:4J9Z, ECO:0007744|PDB:4QNH |
| Chain | Residue | Details |
| B | ASP20 | |
| B | ASP22 | |
| B | ASP24 | |
| B | THR26 | |
| B | GLU31 |
| Chain | Residue | Details |
| B | ASP56 | |
| B | ASP58 | |
| B | ASN60 | |
| B | THR62 | |
| B | GLU67 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3EK4, ECO:0007744|PDB:3EK7, ECO:0007744|PDB:3EK8, ECO:0007744|PDB:3EKH, ECO:0007744|PDB:3EVR, ECO:0007744|PDB:3EVU, ECO:0007744|PDB:3SG2, ECO:0007744|PDB:3SG3, ECO:0007744|PDB:3SG4, ECO:0007744|PDB:3SG5, ECO:0007744|PDB:3SG6, ECO:0007744|PDB:3SG7, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:3WLC, ECO:0007744|PDB:3WLD, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4RJD |
| Chain | Residue | Details |
| B | ASP93 | |
| B | ASP95 | |
| B | ASN97 | |
| B | TYR99 | |
| B | GLU104 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3EK7, ECO:0007744|PDB:3EK8, ECO:0007744|PDB:3EKH, ECO:0007744|PDB:3EVR, ECO:0007744|PDB:3EVU, ECO:0007744|PDB:3SG2, ECO:0007744|PDB:3SG3, ECO:0007744|PDB:3SG4, ECO:0007744|PDB:3SG5, ECO:0007744|PDB:3SG7, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:3WLC, ECO:0007744|PDB:3WLD, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4RJD |
| Chain | Residue | Details |
| B | ASP129 | |
| B | ASP131 | |
| B | ASP133 | |
| B | GLN135 | |
| B | GLU140 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:201628, ECO:0000269|Ref.8 |
| Chain | Residue | Details |
| B | ALA1 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P0DP23 |
| Chain | Residue | Details |
| B | LYS21 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by CaMK4 => ECO:0000269|PubMed:12392717 |
| Chain | Residue | Details |
| B | THR44 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP23 |
| Chain | Residue | Details |
| B | SER81 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DP23 |
| Chain | Residue | Details |
| B | LYS94 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:22673903 |
| Chain | Residue | Details |
| B | TYR99 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
| Chain | Residue | Details |
| B | SER101 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0DP23 |
| Chain | Residue | Details |
| B | THR110 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP23 |
| Chain | Residue | Details |
| B | LYS115 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P0DP23 |
| Chain | Residue | Details |
| B | TYR138 |
| site_id | SWS_FT_FI15 |
| 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 |
| B | LYS21 |
