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8FMM

Complex structure of wild type Troponin complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0002086biological_processdiaphragm contraction
A0003009biological_processskeletal muscle contraction
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0005861cellular_componenttroponin complex
A0006937biological_processregulation of muscle contraction
A0010038biological_processresponse to metal ion
A0014883biological_processtransition between fast and slow fiber
A0031013molecular_functiontroponin I binding
A0031014molecular_functiontroponin T binding
A0032972biological_processregulation of muscle filament sliding speed
A0042803molecular_functionprotein homodimerization activity
A0043292cellular_componentcontractile muscle fiber
A0043462biological_processregulation of ATP-dependent activity
A0046872molecular_functionmetal ion binding
A0048306molecular_functioncalcium-dependent protein binding
A0051015molecular_functionactin filament binding
A0055010biological_processventricular cardiac muscle tissue morphogenesis
A0060048biological_processcardiac muscle contraction
A1990584cellular_componentcardiac Troponin complex
D0002086biological_processdiaphragm contraction
D0003009biological_processskeletal muscle contraction
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005829cellular_componentcytosol
D0005861cellular_componenttroponin complex
D0006937biological_processregulation of muscle contraction
D0010038biological_processresponse to metal ion
D0014883biological_processtransition between fast and slow fiber
D0031013molecular_functiontroponin I binding
D0031014molecular_functiontroponin T binding
D0032972biological_processregulation of muscle filament sliding speed
D0042803molecular_functionprotein homodimerization activity
D0043292cellular_componentcontractile muscle fiber
D0043462biological_processregulation of ATP-dependent activity
D0046872molecular_functionmetal ion binding
D0048306molecular_functioncalcium-dependent protein binding
D0051015molecular_functionactin filament binding
D0055010biological_processventricular cardiac muscle tissue morphogenesis
D0060048biological_processcardiac muscle contraction
D1990584cellular_componentcardiac Troponin complex
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DEDGSGTVDfdEF
ChainResidueDetails
AASP65-PHE77
AASP105-LEU117
AASP141-PHE153

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSITE: Involved in TNI-TNT interactions
ChainResidueDetails
CALA80
AGLU116
AASP141
AASN143
AASP145
AARG147
AGLU152
DASP65
DASP67
DSER69
DTHR71
CALA97
DGLU76
DASP105
DASN107
DASP109
DTYR111
DGLU116
DASP141
DASN143
DASP145
DARG147
FALA80
DGLU152
FALA97
AGLU76
AASP105
AASN107
AASP109
ATYR111

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKC/PRKCE => ECO:0000250|UniProtKB:P48787
ChainResidueDetails
CSER42
CSER44
FSER42
FSER44

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by STK4/MST1 => ECO:0000269|PubMed:18986304, ECO:0000269|PubMed:22972900
ChainResidueDetails
CTHR51
CTHR143
FTHR51
FTHR143

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:22972900
ChainResidueDetails
CSER77
CSER166
FSER77
FSER166

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:22972900
ChainResidueDetails
CTHR78
FTHR78

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by STK4/MST1 => ECO:0000269|PubMed:18986304
ChainResidueDetails
CTHR129
FTHR129

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PAK3 => ECO:0000269|PubMed:12242269
ChainResidueDetails
CSER150
FSER150

221051

PDB entries from 2024-06-12

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