1j1d Summary

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Crystal structure of the 46kDa domain of human cardiac troponin in the Ca2+ saturated form

The structure was published by Takeda, S., Yamashita, A., Maeda, K., and Maeda, Y., in 2003 in a paper entitled "Structure of the core domain of human cardiac troponin in the Ca2+-saturated form" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.61 Å and deposited in 2002.

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

This PDB entry contains a complex of 3 biomacromolecules, namely Troponin C, Troponin T, and Troponin I.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 P63316 (1-161) (TNNC1_HUMAN)search Homo sapienssearch 100% 161 99%
D Troponin C P63316 (1-161) (TNNC1_HUMAN)search Homo sapienssearch 100% 161 99%
B Troponin T P45379 (193-298) (TNNT2_HUMAN)search Homo sapienssearch < 90% 106 70%
E Troponin T P45379 (193-298) (TNNT2_HUMAN)search Homo sapienssearch < 90% 106 70%
C Troponin I P19429 (31-163) (TNNI3_HUMAN)search Homo sapienssearch < 90% 133 88%
F Troponin I P19429 (31-163) (TNNI3_HUMAN)search Homo sapienssearch < 90% 133 88%


This entry contains 3 unique UniProt proteins:

UniProt accession Name Organism PDB
P63316 (1 - 161) Troponin C Homo sapiens
P45379 (193 - 298) Troponin T Homo sapiens
P19429 (31 - 163) Troponin I Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, D (P63316) Calmodulin-likesearch EF-handsearch PF13499: EF-hand domain pairsearch, PF13833: EF-hand domain pairsearch
B, E Troponin Tsearch Single alpha-helices involved in coiled-coils or other helix-helix interfacessearch Troponinsearch
C, F Troponin Isearch Single alpha-helices involved in coiled-coils or other helix-helix interfacessearch Troponinsearch, Troponin I residues 1-32search

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, D (P63316) protein homodimerization activitysearch actin filament bindingsearch troponin I bindingsearch protein bindingsearch calcium ion bindingsearch calcium-dependent protein bindingsearch metal ion bindingsearch troponin T bindingsearch regulation of muscle filament sliding speedsearch diaphragm contractionsearch regulation of ATPase activitysearch regulation of muscle contractionsearch response to metal ionsearch muscle filament slidingsearch ventricular cardiac muscle tissue morphogenesissearch cardiac muscle contractionsearch actin cytoskeletonsearch cytosolsearch nucleussearch troponin complexsearch mitochondrionsearch nucleolussearch contractile fibersearch
B, E (P45379) regulation of muscle contractionsearch troponin complexsearch
C, F (P19429) troponin complexsearch

Chain InterPro annotation
A, D EF-hand domainsearch EF-hand domain pairsearch EF-Hand 1, calcium-binding sitesearch
B, E Troponinsearch Troponin Tsearch
C, F Troponinsearch