Actin, cytoplasmic 1 (ACTB) is a 375-residue protein from Sus scrofa. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q6QAQ1.
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The mean pLDDT of this model is 95.4 (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 | 5% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells (By similarity). Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction (By similarity). In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA (By similarity). Plays a role in the assembly of the gamma-tubulin ring complex (gTuRC), which regulates the minus-end nucleation of alpha-beta tubulin heterodimers that grow into microtubule protafilaments (By…
Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix (By similarity). Each actin can bind to 4 others (By similarity). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (By similarity). Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2,…
Cytoplasm, cytoskeleton, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9I2B | EM | 3.0 Å | I/J/S/T=1-375 |
| 8P94 | EM | 3.3 Å | H/J/K/N/O/P/Q/R/S/W=1-375 |
| 7Z8M | EM | 3.37 Å | H=1-375 |
| 5AFU | EM | 3.5 Å | H=6-375 |
| 6F1T | EM | 3.5 Å | H=1-375 |
| 8IAI | EM | 3.5 Å | A/B/C/D/E/F/G/H/I/J/K=1-375 |
| 8IAH | EM | 3.6 Å | A/B/C/D/E/F/G/H/I/J/K/L=1-375 |
| 6ZNL | EM | 3.8 Å | H=1-375 |
| 8IB2 | EM | 3.8 Å | B/C/D/E/F=1-375 |
| 9DGS | EM | 3.9 Å | H=1-375 |
| 5ADX | EM | 4.0 Å | H=6-375 |
| 9YNG | EM | 4.07 Å | H=1-375 |
| 6ZNM | EM | 4.1 Å | H=1-375 |
| 6ZNN | EM | 4.5 Å | H=1-375 |
| 9HHL | EM | 6.53 Å | H=1-375 |
| 6F38 | EM | 6.7 Å | H=1-375 |
| 6ZNO | EM | 6.8 Å | H=1-375 |
| 9DGU | EM | 7.1 Å | H=1-375 |
| 9DGT | EM | 7.2 Å | H=1-375 |
| 6F3A | EM | 8.2 Å | H=1-375 |
Showing 20 of 25 experimental structures (best resolution first).
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