2jtz Summary

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Solution structure and chemical shift assignments of the F104-to-5-flurotryptophan mutant of cardiac troponin C

The structure was published by Wang, X., Mercier, P., Letourneau, P., and Sykes, B., in 2005 in a paper entitled "Effects of Phe-to-Trp mutation and fluorotryptophan incorporation on the solution structure of cardiac troponin C, and analysis of its suitability as a potential probe for in situ NMR studies" (abstract).

The structure was determined using NMR spectroscopy and deposited in 2007.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of Troponin C, slow skeletal and cardiac muscles. This molecule has the UniProt identifier P63316 (TNNC1_HUMAN)search. The sample contained 161 residues which is 100% of the natural sequence. Out of 161 residues 161 were observed and are deposited in the PDB.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Troponin C, slow skeletal and cardiac muscles P63316 (1-161) (TNNC1_HUMAN)search Homo sapienssearch 100% 161 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P63316 (1 - 161) Troponin C, slow skeletal and cardiac muscles Homo sapiens

Chain Structural classification (SCOP) Sequence family (Pfam)
A (P63316) Calmodulin-likesearch PF13499: EF-hand domain pairsearch, PF13833: EF-hand domain pairsearch

Chain ID Cellular component (GO) Biological process (GO) Molecular function (GO)
A (P63316) cytosolsearch nucleoplasmsearch mitochondrionsearch actin cytoskeletonsearch troponin complexsearch contractile fibersearch regulation of ATPase activitysearch diaphragm contractionsearch response to metal ionsearch cardiac muscle contractionsearch regulation of muscle contractionsearch regulation of muscle filament sliding speedsearch muscle filament slidingsearch ventricular cardiac muscle tissue morphogenesissearch metal ion bindingsearch calcium ion bindingsearch troponin I bindingsearch calcium-dependent protein bindingsearch actin filament bindingsearch protein homodimerization activitysearch troponin T bindingsearch protein bindingsearch

Chain InterPro annotation
A EF-hand domainsearch EF-hand domain pairsearch EF-Hand 1, calcium-binding sitesearch