Crystal structure of the N-terminal fragment of tropomyosin isoform Tpm1.1 at 1.5 A resolution. Determined by X-ray diffraction at 1.5 Å resolution. Released 21 Jun 2017.
Explore 5KHT in 3D Show helices and sheets RCSB PDB PDBe
5KHT contains 4 α-helices and 0 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1-43 | 43 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-43 | 42 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-43 | 40 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tropomyosin alpha-1 chain,General control protein GCN4 | A, B, C, D | protein | 47 | Homo sapiens, Saccharomyces cerevisiae | P03069 (AlphaFold model), P09493 (AlphaFold model) |
>5KHT_1 Tropomyosin alpha-1 chain,General control protein GCN4 (chains A, B, C, D) GMDAIKKKMQMLKLDKENALDRAEQAEADNYHLENEVARLKKLVGER
Structural destabilization of tropomyosin induced by the cardiomyopathy-linked mutation R21H. Ly, T., Krieger, I., Tolkatchev, D. et al. Protein Sci (2018) 27:498-508. DOI 10.1002/pro.3341 · PubMed
Other PDB entries of the same protein (UniProt P03069 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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