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 | 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 |
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 | 2 |
Details | SITE: Involved in TNI-TNT interactions |
Chain | Residue | Details |
C | CYS80 | |
A | LEU118 | |
A | LYS143 | |
A | ASN145 | |
A | GLY147 | |
A | ILE149 | |
A | PHE154 | |
C | CYS97 | |
A | GLY72 | |
A | VAL74 | |
A | PHE79 | |
A | LYS107 | |
A | ALA109 | |
A | GLY111 | |
A | ILE113 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | MOD_RES: Phosphothreonine; by STK4/MST1 => ECO:0000250|UniProtKB:P19429 |
Chain | Residue | Details |
C | THR51 | |
C | THR129 | |
C | THR143 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P19429 |
Chain | Residue | Details |
C | THR78 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P19429 |
Chain | Residue | Details |
C | SER150 |