TATA-box-binding protein (SPT15) is a 240-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P13393.
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The mean pLDDT of this model is 88.5 (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 | 83% |
| 70 to 90 | Confident: backbone generally right | 5% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 10% |
What pLDDT means and how to read it
General transcription factor that functions at the core of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription
Binds DNA as monomer. The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14. Interacts with TFC8
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1YTB | X-ray | 1.8 Å | A/B=61-240 |
| 1NH2 | X-ray | 1.9 Å | A=61-240 |
| 4B0A | X-ray | 1.97 Å | A=61-240 |
| 6E16 | X-ray | 2.4 Å | A=61-240 |
| 1RM1 | X-ray | 2.5 Å | A=1-240 |
| 1YTF | X-ray | 2.5 Å | A=61-240 |
| 1TBP | X-ray | 2.6 Å | A/B=62-240 |
| 7Z0O | EM | 2.8 Å | H=1-240 |
| 7O4J | EM | 2.9 Å | O=1-240 |
| 7OHA | EM | 2.9 Å | K=1-240 |
| 1NGM | X-ray | 2.95 Å | A/E/I/M=61-240 |
| 6E24 | X-ray | 3.0 Å | A=61-240 |
| 7ML0 | EM | 3.0 Å | O=1-240 |
| 7OH9 | EM | 3.0 Å | K=1-240 |
| 8CEN | EM | 3.0 Å | O=1-240 |
| 7ML4 | EM | 3.1 Å | O=1-240 |
| 7ZS9 | EM | 3.1 Å | O=1-240 |
| 7O4I | EM | 3.2 Å | O=1-240 |
| 7O75 | EM | 3.2 Å | O=1-240 |
| 7ML2 | EM | 3.4 Å | O=1-240 |
Showing 20 of 56 experimental structures (best resolution first).
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