Transcription initiation factor TFIID subunit 7 (TAF7) is a 349-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15545.
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The mean pLDDT of this model is 76.1 (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 | 46% |
| 70 to 90 | Confident: backbone generally right | 20% |
| 50 to 70 | Low: treat with caution | 17% |
| Below 50 | Very low: often disordered regions | 18% |
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:10438527, PubMed:33795473). TAF7 forms a promoter DNA binding subcomplex of TFIID, together with TAF1 and TAF2 (PubMed:33795473). Part of a TFIID complex containing TAF10 (TFIID…
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:10438527, PubMed:27007846, PubMed:33795473). Part of a TFIID-containing RNA polymerase II pre-initiation complex that is composed of TBP and at…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4RGW | X-ray | 2.3 Å | B=1-349 |
| 7EGH | EM | 3.04 Å | G=1-349 |
| 7EGB | EM | 3.3 Å | G=1-349 |
| 7EG9 | EM | 3.7 Å | G=1-349 |
| 7EGC | EM | 3.9 Å | G=1-349 |
| 7ENA | EM | 4.07 Å | DG=1-349 |
| 7EGA | EM | 4.1 Å | G=1-349 |
| 7ENC | EM | 4.13 Å | DG=1-349 |
| 8GXS | EM | 4.16 Å | DG=1-349 |
| 7EDX | EM | 4.5 Å | G=1-349 |
| 8GXQ | EM | 5.04 Å | DG=1-349 |
| 8WAK | EM | 5.47 Å | G=1-349 |
| 8WAP | EM | 5.85 Å | G=1-349 |
| 8WAN | EM | 6.07 Å | G=1-349 |
| 8WAS | EM | 6.13 Å | G=1-349 |
| 7EG7 | EM | 6.2 Å | G=1-349 |
| 8WAQ | EM | 6.29 Å | G=1-349 |
| 8WAO | EM | 6.4 Å | G=1-349 |
| 7EGD | EM | 6.75 Å | G=1-349 |
| 8WAR | EM | 7.2 Å | G=1-349 |
Showing 20 of 28 experimental structures (best resolution first).
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