6KLT
Troponin of cardiac thin filament in low-calcium state
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 | 0005861 | cellular_component | troponin complex |
| A | 0006937 | biological_process | regulation of muscle contraction |
| A | 0008092 | molecular_function | cytoskeletal protein binding |
| A | 0010038 | biological_process | response to metal ion |
| A | 0014883 | biological_process | transition between fast and slow fiber |
| A | 0030017 | cellular_component | sarcomere |
| A | 0030049 | biological_process | muscle filament sliding |
| A | 0031013 | molecular_function | troponin I binding |
| A | 0031014 | molecular_function | troponin T binding |
| A | 0032780 | biological_process | negative regulation of ATP-dependent activity |
| 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 | 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 | 0086003 | biological_process | cardiac muscle cell 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 201 |
| Chain | Residue |
| A | ASP142 |
| A | ASN144 |
| A | ASP146 |
| A | ARG148 |
| A | GLU153 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 202 |
| Chain | Residue |
| A | GLU117 |
| A | ASP106 |
| A | ASN108 |
| A | ASP110 |
| A | TYR112 |
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 | ASP67-PHE79 | |
| A | ASP106-LEU118 | |
| A | ASP142-PHE154 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by PKC/PRKCA and RAF1","evidences":[{"source":"PubMed","id":"12832403","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Involved in TNI-TNT interactions"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by STK4/MST1","evidences":[{"source":"UniProtKB","id":"P19429","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P19429","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P19429","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
