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 | 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 | 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 |
| 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 | 0008092 | molecular_function | cytoskeletal protein binding |
| D | 0010038 | biological_process | response to metal ion |
| D | 0014883 | biological_process | transition between fast and slow fiber |
| D | 0030017 | cellular_component | sarcomere |
| D | 0030049 | biological_process | muscle filament sliding |
| 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 | 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 | 0086003 | biological_process | cardiac muscle cell 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 | 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 | 70 |
| 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 | 70 |
| 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 | 66 |
| 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 | 30 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| 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 | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P19123","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by PKC/PRKCA and RAF1","evidences":[{"source":"UniProtKB","id":"P13789","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Site: {"description":"Involved in TNI-TNT interactions"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by PKC/PRKCE","evidences":[{"source":"UniProtKB","id":"P48787","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by STK4/MST1","evidences":[{"source":"PubMed","id":"18986304","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22972900","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22972900","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"22972900","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by STK4/MST1","evidences":[{"source":"PubMed","id":"18986304","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by PAK3","evidences":[{"source":"PubMed","id":"12242269","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
