Protein diaphanous homolog 1 (Diaph1) is a 1255-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O08808.
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The mean pLDDT of this model is 74.0 (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 | 34% |
| 70 to 90 | Confident: backbone generally right | 32% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 24% |
What pLDDT means and how to read it
Actin nucleation and elongation factor required for the assembly of F-actin structures, such as actin cables and stress fibers (PubMed:10678165, PubMed:15044801, PubMed:18572016, PubMed:23558171). Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization (PubMed:10678165, PubMed:15044801, PubMed:18572016). Required for cytokinesis, and transcriptional activation of the serum response factor (PubMed:10678165, PubMed:15044801, PubMed:18572016). DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics (PubMed:10678165, PubMed:15044801, PubMed:18572016). Functions as a scaffold protein for MAPRE1 and APC…
Homodimer (PubMed:14992721, PubMed:15864301). Interacts with the GTP-bound form of RHOA (PubMed:9214622). Interacts with RHOC, PFY1, MAPRE1, BAIAP2 and APC (PubMed:10814512, PubMed:15311282, PubMed:15864301). Interacts with APC; acts as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration (PubMed:15311282). Interacts with SCAI (PubMed:19350017). Interacts…
Cell membrane, Cell projection, ruffle membrane, Cytoplasm, cytoskeleton, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Cytoplasm, cytoskeleton, spindle, Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2V8F | X-ray | 1.1 Å | C=635-655 |
| 4UWX | X-ray | 1.65 Å | A/B=135-369 |
| 2F31 | X-ray | 2.1 Å | B=1177-1196 |
| 2BNX | X-ray | 2.4 Å | A/B=131-516 |
| 1V9D | X-ray | 2.6 Å | A/B/C/D=826-1163 |
| 3EG5 | X-ray | 2.7 Å | B/D=69-451 |
| 3OBV | X-ray | 2.75 Å | A/B/C/D=131-457, E/F/G/H=753-1209 |
| 1Z2C | X-ray | 3.0 Å | B/D=69-451 |
| 3O4X | X-ray | 3.2 Å | A/B/C/D=131-458, E/F/G/H=736-1200 |
| 2BAP | X-ray | 3.3 Å | A/B=135-451, C/D=1145-1200 |
| 9B3D | EM | 3.41 Å | G/H=745-1143 |
| 8RU2 | EM | 3.49 Å | E/F=688-1255 |
| 9B27 | EM | 3.51 Å | G/H=745-1166 |
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