Transcription initiation factor TFIID subunit 10 (TAF10) is a 218-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q12962.
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The mean pLDDT of this model is 66.9 (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 | 33% |
| 70 to 90 | Confident: backbone generally right | 9% |
| 50 to 70 | Low: treat with caution | 24% |
| Below 50 | Very low: often disordered regions | 34% |
What pLDDT means and how to read it
The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (PubMed:33795473). TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (PubMed:33795473). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473). TAF10 is also component of the PCAF histone acetylase complex, the TATA-binding protein-free TAF complex (TFTC) and the STAGA transcription coactivator-HAT complex…
Component of the TFIID basal transcription factor complex, composed of TATA-box-binding protein TBP, and a number of TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473). Component of the TATA-binding protein-free TAF complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2F69 | X-ray | 1.3 Å | B=186-195 |
| 3M58 | X-ray | 1.4 Å | B=186-195 |
| 3M55 | X-ray | 1.55 Å | B=186-195 |
| 5EG2 | X-ray | 1.55 Å | B=186-195 |
| 4J7F | X-ray | 1.59 Å | B=186-195 |
| 3M54 | X-ray | 1.6 Å | B=186-195 |
| 4J8O | X-ray | 1.63 Å | B=186-195 |
| 3M56 | X-ray | 1.65 Å | B=186-195 |
| 3M57 | X-ray | 1.7 Å | B=186-195 |
| 3M59 | X-ray | 1.7 Å | B=186-195 |
| 4J83 | X-ray | 1.7 Å | B=186-195 |
| 3M5A | X-ray | 1.75 Å | B=186-195 |
| 3M53 | X-ray | 1.85 Å | B=186-195 |
| 4WV4 | X-ray | 1.91 Å | A=112-212 |
| 9RDK | EM | 2.41 Å | H=1-218 |
| 4J7I | X-ray | 2.56 Å | B=186-195 |
| 7EGG | EM | 2.77 Å | J=1-218 |
| 7KTR | EM | 2.93 Å | H=1-218 |
| 7EGF | EM | 3.16 Å | j=1-218 |
| 7EGB | EM | 3.3 Å | J/j=1-218 |
Showing 20 of 48 experimental structures (best resolution first).
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