Actin (ACT1) is a 375-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P60010.
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The mean pLDDT of this model is 95.2 (very high 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 | 93% |
| 70 to 90 | Confident: backbone generally right | 4% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells
Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix (Probable). Treatments with Lantrunculin A, the microbial peptide Chondramide or the microbial metabolite Chivazole F inhibit actin polymerization (PubMed:28796488). Each actin can bind to 4 others. Interacts with YIH1 (via C-terminus); this interaction occurs in a…
Cytoplasm, cytoskeleton
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1YAG | X-ray | 1.9 Å | A=1-375 |
| 1YVN | X-ray | 2.1 Å | A=1-375 |
| 9GO5 | EM | 2.5 Å | A/B/C/D/E=1-375 |
| 5NBL | X-ray | 2.8 Å | C/D=1-375 |
| 7VVY | EM | 3.1 Å | G=1-375 |
| 8ESC | EM | 3.1 Å | A=1-375 |
| 8A5O | EM | 3.2 Å | V=1-375 |
| 8A5A | EM | 3.3 Å | V=1-375 |
| 5NBM | X-ray | 3.4 Å | C/D=1-375 |
| 7YFN | EM | 3.8 Å | A=4-375 |
| 5NBN | X-ray | 4.0 Å | C/D=1-375 |
| 7YFP | EM | 4.0 Å | A=4-375 |
| 5Y81 | EM | 4.7 Å | G=1-375 |
| 7VVZ | EM | 8.8 Å | G=1-375 |
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