F-actin-capping protein subunit alpha-1 (CAPZA1) is a 286-residue protein from Gallus gallus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P13127.
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The mean pLDDT of this model is 91.6 (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 | 75% |
| 70 to 90 | Confident: backbone generally right | 22% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the formation of epithelial cell junctions (By similarity). Forms, with CAPZB, the barbed end of the fast growing ends of actin filaments in the dynactin complex and stabilizes dynactin structure. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity)
Component of the F-actin capping complex, composed of a heterodimer of an alpha and a beta subunit. Subunit of dynactin, a multiprotein complex part of a tripartite complex with dynein and a adapter, such as BICDL1, BICD2 or HOOK3. The dynactin complex is built around ACTR1A/ACTB filament and consists of an actin-related filament composed of a shoulder domain, a pointed end and a barbed end. Its…
Cytoplasm, myofibril, sarcomere, Z line, Cytoplasm, cytoskeleton
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7DS6 | X-ray | 1.69 Å | A=1-286 |
| 3AA0 | X-ray | 1.7 Å | A=1-286 |
| 7DS4 | X-ray | 1.85 Å | A=1-286 |
| 3AA1 | X-ray | 1.9 Å | A=1-286 |
| 3AA6 | X-ray | 1.9 Å | A=1-286 |
| 3AA7 | X-ray | 1.9 Å | A=1-286 |
| 7DS2 | X-ray | 1.95 Å | A=1-286 |
| 7DS8 | X-ray | 1.95 Å | A=1-286 |
| 3LK4 | X-ray | 1.99 Å | 1/4/7/A/D/G/J/M/P/S/V/Y=1-286 |
| 9BLI | X-ray | 2.0 Å | A=1-286 |
| 7DS3 | X-ray | 2.09 Å | A=1-286 |
| 1IZN | X-ray | 2.1 Å | A/C=1-286 |
| 3AAA | X-ray | 2.2 Å | A=1-286 |
| 3LK2 | X-ray | 2.2 Å | A=1-286 |
| 7DSB | X-ray | 2.44 Å | A=1-286 |
| 3LK3 | X-ray | 2.68 Å | A=1-286 |
| 7DSA | X-ray | 2.8 Å | A=1-286 |
| 3AAE | X-ray | 3.3 Å | A/C/E/G/I=1-286 |
| 2KXP | NMR | A=7-281 | |
| 2KZ7 | NMR | A=1-286 |
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