Tubulin alpha-1B chain (TUBA1B) is a 451-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P68363.
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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 | 83% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 3% |
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:38305685, PubMed:34996871, PubMed:38609661). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms (PubMed:38305685, PubMed:34996871, PubMed:38609661). Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (PubMed:34996871, PubMed:38609661)
Heterodimer of alpha- and beta-tubulin (PubMed:17563362, 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…
Cytoplasm, cytoskeleton
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6S8L | X-ray | 1.8 Å | A=1-451 |
| 6J8O | X-ray | 1.85 Å | C=444-451 |
| 7PJF | X-ray | 1.86 Å | A=1-451 |
| 6J4V | X-ray | 2.1 Å | C=431-451 |
| 8VT7 | EM | 2.66 Å | B/J=1-451 |
| 7Z6S | EM | 2.9 Å | A/K=1-451 |
| 8V2J | EM | 2.9 Å | A/D=1-451 |
| 9COC | EM | 2.9 Å | A/C/D/I=1-451 |
| 9BP6 | EM | 3.1 Å | A/I=1-451 |
| 9CMM | EM | 3.1 Å | A/C/E/I=1-451 |
| 7LXB | EM | 3.26 Å | A/C/E/G/I/K/M/O=1-451 |
| 9HQ4 | EM | 3.28 Å | A/C=1-451 |
| 7M18 | EM | 3.38 Å | A/C/E/G/I/K/M/O=1-451 |
| 6E7B | EM | 3.5 Å | A=1-437 |
| 6I2I | EM | 3.6 Å | A=1-451 |
| 7SJ8 | EM | 3.6 Å | A/C/E/J/K/L=1-451 |
| 7ZCW | EM | 3.6 Å | A/E=1-451 |
| 8T42 | EM | 3.6 Å | A/F=1-451 |
| 8U3Z | EM | 3.6 Å | A/F=1-451 |
| 9F3B | EM | 3.6 Å | A/C/E/G/I/K=1-42, A/C/E/G/I/K=47-441 |
Showing 20 of 39 experimental structures (best resolution first).
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