3D structure of the leiomodin/tropomyosin binding interface. Determined by solution NMR. Released 30 Sept 2020.
Explore 6UT2 in 3D Show helices and sheets RCSB PDB PDBe
6UT2 contains 5 α-helices and 0 β-strands across 3 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 | 3-6 | 4 | |
| α-helix | 18-21 | 4 | |
| α-helix | 27-40 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1-28 | 28 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-28 | 27 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Leiomodin-2 | A | protein | 40 | Homo sapiens | Q6P5Q4 (AlphaFold model) |
| Tropomyosin alpha-1 chain chimeric peptide | B, C | protein | 33 | Homo sapiens | P03069 (AlphaFold model), P09493 (AlphaFold model) |
>6UT2_1 Leiomodin-2 (chains A) STFGYRRGLSKYESIDEDELLASLSAEELKELERELEDIE
>6UT2_2 Tropomyosin alpha-1 chain chimeric peptide (chains B, C) GMDAIKKKMQMLKLDNYHLENEVARLKKLVGER
Leiomodin creates a leaky cap at the pointed end of actin-thin filaments. Tolkatchev, D., Smith Jr., G.E., Schultz, L.E. et al. PLoS Biol (2020) 18:e3000848-e3000848. DOI 10.1371/journal.pbio.3000848 · PubMed
Other PDB entries of the same protein (UniProt Q6P5Q4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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