1J1E
Crystal structure of the 52kDa domain of human cardiac troponin in the Ca2+ saturated form
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 | 0005861 | cellular_component | troponin complex |
| D | 0002086 | biological_process | diaphragm contraction |
| D | 0003009 | biological_process | skeletal muscle contraction |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0005861 | cellular_component | troponin complex |
| D | 0006937 | biological_process | regulation of muscle contraction |
| D | 0010038 | biological_process | response to metal ion |
| D | 0014883 | biological_process | transition between fast and slow fiber |
| D | 0031013 | molecular_function | troponin I binding |
| D | 0031014 | molecular_function | troponin T binding |
| D | 0032972 | biological_process | regulation of muscle filament sliding speed |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0043292 | cellular_component | contractile muscle fiber |
| D | 0043462 | biological_process | regulation of ATP-dependent activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0048306 | molecular_function | calcium-dependent protein binding |
| D | 0051015 | molecular_function | actin filament binding |
| D | 0055010 | biological_process | ventricular cardiac muscle tissue morphogenesis |
| D | 0060048 | biological_process | cardiac muscle contraction |
| D | 1990584 | cellular_component | cardiac Troponin complex |
| E | 0005861 | cellular_component | troponin complex |
| E | 0006937 | biological_process | regulation of muscle contraction |
| F | 0005861 | cellular_component | 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 | ASP73 |
| A | GLU76 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 202 |
| Chain | Residue |
| A | TYR111 |
| A | ASP113 |
| A | GLU116 |
| A | ASP105 |
| A | ASN107 |
| A | ASP109 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 203 |
| Chain | Residue |
| A | ASP141 |
| A | ASN143 |
| A | ASP145 |
| A | ARG147 |
| A | GLU152 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 201 |
| Chain | Residue |
| D | ASP65 |
| D | ASP67 |
| D | SER69 |
| D | THR71 |
| D | ASP73 |
| D | GLU76 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA D 202 |
| Chain | Residue |
| D | ASP105 |
| D | ASN107 |
| D | ASP109 |
| D | TYR111 |
| D | GLU116 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA D 203 |
| Chain | Residue |
| D | ASP141 |
| D | ASN143 |
| D | ASP145 |
| D | ARG147 |
| D | GLU152 |
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 | 4 |
| Details | SITE: Involved in TNI-TNT interactions |
| Chain | Residue | Details |
| C | GLN81 | |
| A | GLU116 | |
| A | ASP141 | |
| A | ASN143 | |
| A | ASP145 | |
| A | ARG147 | |
| A | GLU152 | |
| D | ASP65 | |
| D | ASP67 | |
| D | SER69 | |
| D | THR71 | |
| C | ARG98 | |
| D | GLU76 | |
| D | ASP105 | |
| D | ASN107 | |
| D | ASP109 | |
| D | TYR111 | |
| D | GLU116 | |
| D | ASP141 | |
| D | ASN143 | |
| D | ASP145 | |
| D | ARG147 | |
| F | GLN81 | |
| D | GLU152 | |
| F | ARG98 | |
| A | GLU76 | |
| A | ASP105 | |
| A | ASN107 | |
| A | ASP109 | |
| A | TYR111 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine; by STK4/MST1 => ECO:0000269|PubMed:18986304 |
| Chain | Residue | Details |
| C | GLU32 | |
| C | GLN130 | |
| F | GLU32 | |
| F | GLN130 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by PKC/PRKCE => ECO:0000250|UniProtKB:P48787 |
| Chain | Residue | Details |
| C | ALA43 | |
| C | ARG45 | |
| F | ALA43 | |
| F | ARG45 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine; by STK4/MST1 => ECO:0000269|PubMed:18986304, ECO:0000269|PubMed:22972900 |
| Chain | Residue | Details |
| C | LEU52 | |
| C | LEU144 | |
| F | LEU52 | |
| F | LEU144 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:22972900 |
| Chain | Residue | Details |
| C | THR78 | |
| C | LEU167 | |
| C | GLY200 | |
| F | THR78 | |
| F | LEU167 | |
| F | GLY200 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:22972900 |
| Chain | Residue | Details |
| C | ARG79 | |
| C | GLU182 | |
| F | ARG79 | |
| F | GLU182 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PAK3 => ECO:0000269|PubMed:12242269 |
| Chain | Residue | Details |
| C | ALA151 | |
| F | ALA151 |
