2JT3
Solution Structure of F153W cardiac troponin C
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 | 0008092 | molecular_function | cytoskeletal protein binding |
| A | 0010038 | biological_process | response to metal ion |
| 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 |
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-TRP153 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 35 |
| Details | Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 35 |
| Details | Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 35 |
| Details | Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 33 |
| Details | Domain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"3951483","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P19123","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
