4Y99
Core domain of human cardiac troponin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002086 | biological_process | diaphragm contraction |
| A | 0003009 | biological_process | skeletal muscle contraction |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0005861 | cellular_component | troponin complex |
| A | 0006937 | biological_process | regulation of muscle contraction |
| A | 0010038 | biological_process | response to metal ion |
| A | 0014883 | biological_process | transition between fast and slow fiber |
| A | 0031013 | molecular_function | troponin I binding |
| A | 0031014 | molecular_function | troponin T binding |
| A | 0032972 | biological_process | regulation of muscle filament sliding speed |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043292 | cellular_component | contractile muscle fiber |
| A | 0043462 | biological_process | regulation of ATP-dependent activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048306 | molecular_function | calcium-dependent protein binding |
| A | 0051015 | molecular_function | actin filament binding |
| A | 0055010 | biological_process | ventricular cardiac muscle tissue morphogenesis |
| A | 0060048 | biological_process | cardiac muscle contraction |
| A | 1990584 | cellular_component | cardiac Troponin complex |
| B | 0005861 | cellular_component | troponin complex |
| B | 0006937 | biological_process | regulation of muscle contraction |
| C | 0001570 | biological_process | vasculogenesis |
| C | 0001980 | biological_process | regulation of systemic arterial blood pressure by ischemic conditions |
| C | 0003009 | biological_process | skeletal muscle contraction |
| C | 0003779 | molecular_function | actin binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0005861 | cellular_component | troponin complex |
| C | 0006874 | biological_process | intracellular calcium ion homeostasis |
| C | 0006937 | biological_process | regulation of muscle contraction |
| C | 0006940 | biological_process | regulation of smooth muscle contraction |
| C | 0006941 | biological_process | striated muscle contraction |
| C | 0007507 | biological_process | heart development |
| C | 0010882 | biological_process | regulation of cardiac muscle contraction by calcium ion signaling |
| C | 0019855 | molecular_function | calcium channel inhibitor activity |
| C | 0019901 | molecular_function | protein kinase binding |
| C | 0019904 | molecular_function | protein domain specific binding |
| C | 0030016 | cellular_component | myofibril |
| C | 0030017 | cellular_component | sarcomere |
| C | 0030172 | molecular_function | troponin C binding |
| C | 0031014 | molecular_function | troponin T binding |
| C | 0032780 | biological_process | negative regulation of ATP-dependent activity |
| C | 0043292 | cellular_component | contractile muscle fiber |
| C | 0048306 | molecular_function | calcium-dependent protein binding |
| C | 0051015 | molecular_function | actin filament binding |
| C | 0055010 | biological_process | ventricular cardiac muscle tissue morphogenesis |
| C | 0060047 | biological_process | heart contraction |
| C | 0060048 | biological_process | cardiac muscle contraction |
| C | 0097512 | cellular_component | cardiac myofibril |
| C | 1990584 | cellular_component | cardiac Troponin complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 201 |
| Chain | Residue |
| A | ASP65 |
| A | ASP67 |
| A | SER69 |
| A | THR71 |
| A | GLU76 |
| A | HOH319 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 202 |
| Chain | Residue |
| A | ARG147 |
| A | GLU152 |
| A | HOH321 |
| A | ASP141 |
| A | ASN143 |
| A | ASP145 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 203 |
| Chain | Residue |
| A | ASP105 |
| A | ASN107 |
| A | ASP109 |
| A | TYR111 |
| A | GLU116 |
| A | HOH320 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue DMS A 204 |
| Chain | Residue |
| A | MET60 |
| A | MET80 |
| C | ILE149 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue DMS A 205 |
| Chain | Residue |
| A | PRO52 |
| A | GLU56 |
| C | ARG148 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue DMS B 301 |
| Chain | Residue |
| B | VAL218 |
| B | LYS232 |
| B | GLU235 |
| B | HOH401 |
| B | HOH420 |
| C | HIS101 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue DMS B 302 |
| Chain | Residue |
| A | SER98 |
| A | TYR150 |
| B | GLU260 |
| B | VAL263 |
| B | LEU264 |
| B | ARG267 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue DMS C 501 |
| Chain | Residue |
| B | ARG215 |
| C | ASP108 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue DMS C 502 |
| Chain | Residue |
| C | TYR112 |
| C | GLU115 |
| C | ALA116 |
| C | THR119 |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DEDGSGTVDfdEF |
| Chain | Residue | Details |
| A | ASP65-PHE77 | |
| A | ASP105-LEU117 | |
| A | ASP141-PHE153 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | SITE: Involved in TNI-TNT interactions |
| Chain | Residue | Details |
| C | ALA80 | |
| A | GLU116 | |
| A | ASP141 | |
| A | ASN143 | |
| A | ASP145 | |
| A | ARG147 | |
| A | GLU152 | |
| C | ALA97 | |
| A | SER69 | |
| A | THR71 | |
| A | GLU76 | |
| A | ASP105 | |
| A | ASN107 | |
| A | ASP109 | |
| A | TYR111 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:2226863 |
| Chain | Residue | Details |
| C | ALA2 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:22972900 |
| Chain | Residue | Details |
| C | SER5 | |
| C | SER6 | |
| C | SER77 | |
| C | SER166 | |
| C | SER199 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PKA and PKD/PRKD1 => ECO:0000269|PubMed:15514163, ECO:0000269|PubMed:2226863, ECO:0000269|PubMed:22972900, ECO:0000269|PubMed:9346285 |
| Chain | Residue | Details |
| C | SER23 | |
| C | SER24 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:22972900 |
| Chain | Residue | Details |
| C | TYR26 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by STK4/MST1 => ECO:0000269|PubMed:18986304 |
| Chain | Residue | Details |
| C | THR31 | |
| C | THR129 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PKC/PRKCE => ECO:0000250|UniProtKB:P48787 |
| Chain | Residue | Details |
| C | SER42 | |
| C | SER44 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by STK4/MST1 => ECO:0000269|PubMed:18986304, ECO:0000269|PubMed:22972900 |
| Chain | Residue | Details |
| C | THR51 | |
| C | THR143 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:22972900 |
| Chain | Residue | Details |
| C | THR78 | |
| C | THR181 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PAK3 => ECO:0000269|PubMed:12242269 |
| Chain | Residue | Details |
| C | SER150 |
