Protein spire (spir) is a 1020-residue protein from Drosophila melanogaster. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9U1K1.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 53.8 (low 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 | 8% |
| 70 to 90 | Confident: backbone generally right | 17% |
| 50 to 70 | Low: treat with caution | 21% |
| Below 50 | Very low: often disordered regions | 53% |
What pLDDT means and how to read it
Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Promotes dissociation of capu from the barbed end of actin filaments. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for localization of determinants within the developing oocyte to the posterior pole and to the dorsal anterior corner. Links Rho family signaling and Jnk function to the actin cytoskeleton
Interacts with bsk, Rho1, Rac1, Cdc42 and wash. Interacts with capu
Cytoplasm, cytoskeleton, Cytoplasm, perinuclear region, Cell membrane, Cytoplasmic vesicle membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3MN5 | X-ray | 1.5 Å | S=448-485 |
| 3MN6 | X-ray | 2.0 Å | X/Y/Z=397-415 |
| 3MN7 | X-ray | 2.0 Å | S=437-483 |
| 3MN9 | X-ray | 2.0 Å | X=372-390 |
| 4EFH | X-ray | 2.48 Å | B=428-485 |
| 3UE5 | X-ray | 2.76 Å | B=428-485 |
| 3MMV | X-ray | 2.8 Å | X=429-447 |
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.