Tubulin beta-3 chain (TUBB3) is a 450-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13509.
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The mean pLDDT of this model is 91.4 (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 | 82% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
Tubulin is the major constituent of microtubules, protein filaments consisting of alpha- and beta-tubulin heterodimers (PubMed:34996871, PubMed:38305685, PubMed:38609661). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms (PubMed:34996871, PubMed:38305685, PubMed:38609661). Below the cap, alpha-beta tubulin heterodimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (PubMed:34996871, PubMed:38609661). TUBB3 plays a critical role in proper axon guidance and maintenance (PubMed:20074521). Binding of NTN1/Netrin-1 to its receptor UNC5C might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and…
Heterodimer of alpha- and beta-tubulin (PubMed:34996871, PubMed:35482892, PubMed:38305685, PubMed:38609661). A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM (PubMed:34996871, PubMed:35482892). Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin…
Cytoplasm, cytoskeleton, Cell projection, growth cone, Cell projection, lamellipodium, Cell projection, filopodium
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6S8L | X-ray | 1.8 Å | B=1-450 |
| 7PJF | X-ray | 1.86 Å | B=1-450 |
| 9WD9 | EM | 2.26 Å | b=1-450 |
| 9WD7 | EM | 2.34 Å | b=1-450 |
| 9WDA | EM | 2.35 Å | b=1-450 |
| 9WDB | EM | 2.39 Å | b=1-450 |
| 22AK | EM | 2.41 Å | B=1-450 |
| 22AJ | EM | 2.48 Å | B=1-450 |
| 8VT7 | EM | 2.66 Å | A/F=1-450 |
| 7Z6S | EM | 2.9 Å | B/H=1-450 |
| 6WSL | EM | 3.1 Å | B/F=1-450 |
| 7LXB | EM | 3.26 Å | B/D/F/H/J/L/N/P=1-450 |
| 7M18 | EM | 3.38 Å | B/D/F/H/J/L/N/P=1-450 |
| 6E7B | EM | 3.5 Å | B=1-426 |
| 7SJ8 | EM | 3.6 Å | B/D/F/G/H/I=1-450 |
| 9F3B | EM | 3.6 Å | B/D/F/N/P/R=1-450 |
| 5IJ9 | EM | 3.7 Å | B=1-426 |
| 5IJ0 | EM | 3.8 Å | B=1-426 |
| 7SJ7 | EM | 3.8 Å | B/D/F/G/H/I=1-450 |
| 7SJ9 | EM | 3.8 Å | B/D/F/G/H/I=1-450 |
Showing 20 of 28 experimental structures (best resolution first).
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