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2JT8

Solution structure of the F153-to-5-flurotryptophan mutant of human cardiac troponin C

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
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-FTR153

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
AASP65
AGLU116
AASP141
AASN143
AASP145
AARG147
AGLU152
AASP67
ASER69
ATHR71
AGLU76
AASP105
AASN107
AASP109
ATYR111

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|PubMed:3951483
ChainResidueDetails
AMET1

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P19123
ChainResidueDetails
ASER98

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PDB entries from 2024-07-24

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