Solution NMR Structure of Antiparallel Myosin-10:GCN4 Tandem Coiled-Coil. Determined by solution NMR. Released 15 Jun 2016.
Explore 2N9B in 3D Show helices and sheets RCSB PDB PDBe
2N9B contains 2 α-helices and 0 β-strands across 2 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 | 885-947 | 63 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Unconventional myosin-X, General control protein GCN4 fusion | A, B | protein | 69 | Bos taurus, Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P03069 (AlphaFold model), P79114 (AlphaFold model) |
>2N9B_1 Unconventional myosin-X, General control protein GCN4 fusion (chains A, B) GSHENKQVEEILRLEKEIEDLQRMKERQELSLTEASLQKLQLEDKVEELLSKNYHLENEV ARLKKLVGE
Competition between Coiled-Coil Structures and the Impact on Myosin-10 Bundle Selection. Vavra, K.C., Xia, Y., Rock, R.S. Biophys J (2016) 110:2517-2527. DOI 10.1016/j.bpj.2016.04.048 · 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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