Unconventional myosin-X (MYO10) is a 2052-residue protein from Bos taurus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P79114.
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The mean pLDDT of this model is 76.4 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 23% |
| 70 to 90 | Confident: backbone generally right | 53% |
| 50 to 70 | Low: treat with caution | 11% |
| Below 50 | Very low: often disordered regions | 14% |
What pLDDT means and how to read it
Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as a plus end-directed motor. Moves with higher velocity and takes larger steps on actin bundles than on single actin filaments (By similarity). The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate, which are then moved relative to actin filaments. Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling…
Monomer, when in an inactive conformation in the cytosol. Homodimer in its active, membrane-bound conformation; antiparallel coiled coil-mediated dimer formation. Interacts with ECPAS. Interacts with NEO 1. Interacts with VASP. Interacts with DCC and ITGB5; the presence of DCC inhibits ITGB5 binding. Interacts with tubulin; ITGB5 or DCC binding inhibits tubulin binding. Interacts strongly with…
Cytoplasm, cytosol, Cell projection, lamellipodium, Cell projection, ruffle, Cytoplasm, cytoskeleton, Cell projection, filopodium tip, Cytoplasm, cell cortex, Cell projection, filopodium membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6HR1 | X-ray | 1.9 Å | A/B=826-837 |
| 5HMO | X-ray | 3.49 Å | A/C=796-929 |
| 2N9B | NMR | A/B=884-923 |
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