1LIN
CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 0008179 | molecular_function | adenylate cyclase binding |
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 | 0019901 | molecular_function | protein kinase binding |
A | 0019904 | molecular_function | protein domain specific binding |
A | 0030017 | cellular_component | sarcomere |
A | 0031432 | molecular_function | titin binding |
A | 0032465 | biological_process | regulation of cytokinesis |
A | 0032991 | cellular_component | protein-containing complex |
A | 0034704 | cellular_component | calcium channel complex |
A | 0043209 | cellular_component | myelin sheath |
A | 0043539 | molecular_function | protein serine/threonine kinase activator activity |
A | 0044325 | molecular_function | transmembrane transporter binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0051592 | biological_process | response to calcium ion |
A | 0055117 | biological_process | regulation of cardiac muscle contraction |
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 | 0072542 | molecular_function | protein phosphatase activator activity |
A | 0097720 | biological_process | calcineurin-mediated signaling |
A | 0098901 | biological_process | regulation of cardiac muscle cell action potential |
A | 1902494 | cellular_component | catalytic complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 149 |
Chain | Residue |
A | ASP20 |
A | ASP22 |
A | ASP24 |
A | THR26 |
A | GLU31 |
A | HOH173 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 150 |
Chain | Residue |
A | THR62 |
A | GLU67 |
A | HOH181 |
A | ASP56 |
A | ASP58 |
A | ASN60 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 151 |
Chain | Residue |
A | ASP93 |
A | ASP95 |
A | ASN97 |
A | TYR99 |
A | GLU104 |
A | HOH205 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 152 |
Chain | Residue |
A | ASP129 |
A | ASP131 |
A | ASP133 |
A | GLN135 |
A | GLU140 |
A | HOH166 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE TFP A 153 |
Chain | Residue |
A | MET124 |
A | GLU127 |
A | VAL136 |
A | MET144 |
A | TFP154 |
A | TFP155 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TFP A 154 |
Chain | Residue |
A | GLU11 |
A | GLU14 |
A | LEU18 |
A | MET109 |
A | GLU114 |
A | LEU116 |
A | GLU120 |
A | MET124 |
A | TFP153 |
A | TFP155 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE TFP A 155 |
Chain | Residue |
A | GLN8 |
A | GLU11 |
A | MET72 |
A | PHE92 |
A | MET144 |
A | MET145 |
A | ALA147 |
A | TFP153 |
A | TFP154 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE TFP A 156 |
Chain | Residue |
A | MET51 |
A | ILE52 |
A | GLU54 |
A | VAL55 |
A | ILE63 |
A | PHE68 |
A | MET71 |
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 | ASP20-LEU32 | |
A | ASP56-PHE68 | |
A | ASP93-LEU105 | |
A | ASP129-PHE141 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 |
Chain | Residue | Details |
A | LYS21 | |
A | PHE68 | |
A | LYS94 | |
A | GLY96 | |
A | GLY98 | |
A | ILE100 | |
A | LEU105 | |
A | ILE130 | |
A | GLY132 | |
A | GLY134 | |
A | VAL136 | |
A | GLY23 | |
A | PHE141 | |
A | GLY25 | |
A | ILE27 | |
A | LEU32 | |
A | ALA57 | |
A | GLY59 | |
A | GLY61 | |
A | ILE63 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:7356670 |
Chain | Residue | Details |
A | ASP2 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | ASP22 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29 |
Chain | Residue | Details |
A | GLU45 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | GLU82 | |
A | ALA102 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | ASP95 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | ILE100 | |
A | GLU139 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | ASN111 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | LEU116 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:9716384 |
Chain | Residue | Details |
A | ASP22 |