Transcription initiation factor TFIID subunit 1 (TAF1) is a 1893-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P21675.
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The mean pLDDT of this model is 61.8 (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 | 26% |
| 70 to 90 | Confident: backbone generally right | 18% |
| 50 to 70 | Low: treat with caution | 13% |
| Below 50 | Very low: often disordered regions | 43% |
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). TAF1 is the largest component and core scaffold of the TFIID complex, involved in nucleating complex assembly (PubMed:25412659, PubMed:27007846, PubMed:33795473). TAF1…
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, PubMed:7680771). Interacts with TAF7; the interaction is direct (PubMed:11592977, PubMed:25412659). TAF1, when part of the TFIID complex,…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5I29 | X-ray | 1.21 Å | A=1518-1659 |
| 7LB1 | X-ray | 1.35 Å | A=1394-1656 |
| 4YYM | X-ray | 1.5 Å | A/B=1518-1659 |
| 5I1Q | X-ray | 1.5 Å | A=1518-1659 |
| 7K27 | X-ray | 1.5 Å | A=1394-1656 |
| 7JJG | X-ray | 1.6 Å | A=1522-1656 |
| 7K03 | X-ray | 1.6 Å | A=1394-1656 |
| 7T36 | X-ray | 1.65 Å | A=1394-1656 |
| 7JSP | X-ray | 1.7 Å | A=1522-1656 |
| 7K3O | X-ray | 1.7 Å | A/B=1522-1656 |
| 7K42 | X-ray | 1.7 Å | A/B=1522-1656 |
| 7LB2 | X-ray | 1.7 Å | A=1394-1656 |
| 5MG2 | X-ray | 1.75 Å | A=1522-1656 |
| 4YYN | X-ray | 1.85 Å | A/B=1518-1659 |
| 7K6F | X-ray | 1.86 Å | A=1394-1656 |
| 3UV4 | X-ray | 1.89 Å | A/B=1522-1656 |
| 7T2I | X-ray | 1.89 Å | A=1394-1656 |
| 7LB3 | X-ray | 1.9 Å | A=1522-1656 |
| 7N42 | X-ray | 1.9 Å | A=1394-1656 |
| 3UV5 | X-ray | 2.03 Å | A=1394-1656 |
Showing 20 of 64 experimental structures (best resolution first).
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