Transcription initiation factor TFIID subunit 3 (TAF3) is a 929-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q5VWG9.
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The mean pLDDT of this model is 55.0 (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 | 9% |
| 70 to 90 | Confident: backbone generally right | 20% |
| 50 to 70 | Low: treat with caution | 13% |
| Below 50 | Very low: often disordered regions | 59% |
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). The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C (PubMed:33795473). TAF3 forms the TFIID-A module together with TAF5 and TBP…
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). Interacts with TAF10 via the histone fold (PubMed:11438666). Interacts with TAF13, TBP, SAP130 and GCN5L2 (PubMed:11438666). Interacts…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5WXH | X-ray | 1.3 Å | A/C=853-915 |
| 5WXG | X-ray | 1.7 Å | A=853-915 |
| 5XMY | X-ray | 1.7 Å | A/C=853-915 |
| 5C13 | X-ray | 2.1 Å | A/C/E/G=855-915 |
| 7EGF | EM | 3.16 Å | c=1-929 |
| 7EGB | EM | 3.3 Å | c=1-929 |
| 7EG9 | EM | 3.7 Å | c=1-929 |
| 7EGC | EM | 3.9 Å | c=1-929 |
| 7ENA | EM | 4.07 Å | Dc=1-929 |
| 7EGA | EM | 4.1 Å | c=1-929 |
| 7ENC | EM | 4.13 Å | Dc=1-929 |
| 8GXS | EM | 4.16 Å | Dc=1-929 |
| 7EDX | EM | 4.5 Å | c=1-929 |
| 8GXQ | EM | 5.04 Å | Dc=1-929 |
| 8WAK | EM | 5.47 Å | c=1-929 |
| 8WAP | EM | 5.85 Å | c=1-929 |
| 8WAN | EM | 6.07 Å | c=1-929 |
| 8WAS | EM | 6.13 Å | c=1-929 |
| 7EG7 | EM | 6.2 Å | c=1-929 |
| 8WAQ | EM | 6.29 Å | c=1-929 |
Showing 20 of 30 experimental structures (best resolution first).
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