Villin-1 (VIL1) is a 826-residue protein from Gallus gallus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P02640.
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The mean pLDDT of this model is 77.3 (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 | 17% |
| 70 to 90 | Confident: backbone generally right | 61% |
| 50 to 70 | Low: treat with caution | 15% |
| Below 50 | Very low: often disordered regions | 8% |
What pLDDT means and how to read it
Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced…
Monomer. Homodimer (By similarity). Associates with F-actin; the association with F-actin is inhibited by tropomyosin
Cytoplasm, cytoskeleton, Cell projection, microvillus, Cell projection, lamellipodium, Cell projection, ruffle, Cell projection, filopodium tip, Cell projection, filopodium
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1WY3 | X-ray | 0.95 Å | A=792-826 |
| 1YRI | X-ray | 1.0 Å | A=792-826 |
| 3TRV | X-ray | 1.0 Å | A/B=792-826 |
| 2F4K | X-ray | 1.05 Å | A=792-826 |
| 1YRF | X-ray | 1.07 Å | A=792-826 |
| 5I1S | X-ray | 1.12 Å | A/B=792-826 |
| 5I1N | X-ray | 1.3 Å | A/B/C/D=792-826 |
| 5I1O | X-ray | 1.35 Å | A/B/C/D=792-826 |
| 1YU5 | X-ray | 1.4 Å | X=760-826 |
| 2RJY | X-ray | 1.4 Å | A=760-826 |
| 5I1P | X-ray | 1.4 Å | A/B/C/D=792-826 |
| 1YU8 | X-ray | 1.45 Å | X=760-826 |
| 2RJV | X-ray | 1.45 Å | A=760-826 |
| 3TJW | X-ray | 1.46 Å | A/B=792-825 |
| 1YU7 | X-ray | 1.5 Å | X=760-826 |
| 1WY4 | X-ray | 1.55 Å | A=792-826 |
| 2RJW | X-ray | 1.55 Å | A/B=760-826 |
| 3NKJ | X-ray | 1.6 Å | A=760-826 |
| 2RJX | X-ray | 1.7 Å | A/B=760-826 |
| 3MYC | X-ray | 1.7 Å | A=760-826 |
Showing 20 of 46 experimental structures (best resolution first).
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