Transcription initiation factor TFIID subunit 4 (TAF4) is a 1085-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O00268.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 52.8 (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 | 14% |
| 70 to 90 | Confident: backbone generally right | 15% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 63% |
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:10594036, PubMed:33795473, PubMed:8942982). TAF4 may maintain an association between the TFIID and TFIIA complexes, while bound to the promoter, together with TBP, during PIC…
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:10594036, PubMed:33795473). Component of the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TADA3L, SUPT3H, TAF2, TAF4, TAF5, GCN5L2/GCN5,…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2P6V | X-ray | 2.0 Å | A=575-688 |
| 1H3O | X-ray | 2.3 Å | A/C=872-945 |
| 7EGG | EM | 2.77 Å | D=1-1085 |
| 7EGF | EM | 3.16 Å | d=1-1085 |
| 7EGB | EM | 3.3 Å | D/d=1-1085 |
| 7EG9 | EM | 3.7 Å | D/d=1-1085 |
| 7EGC | EM | 3.9 Å | D/d=1-1085 |
| 7ENA | EM | 4.07 Å | DD/Dd=1-1085 |
| 7EGA | EM | 4.1 Å | D/d=1-1085 |
| 7ENC | EM | 4.13 Å | DD/Dd=1-1085 |
| 8GXS | EM | 4.16 Å | DD/Dd=1-1085 |
| 6MZC | EM | 4.5 Å | E=1-1085 |
| 7EDX | EM | 4.5 Å | D/d=1-1085 |
| 8GXQ | EM | 5.04 Å | DD/Dd=1-1085 |
| 8WAK | EM | 5.47 Å | D/d=1-1085 |
| 8WAP | EM | 5.85 Å | D/d=1-1085 |
| 8WAN | EM | 6.07 Å | D/d=1-1085 |
| 8WAS | EM | 6.13 Å | D/d=1-1085 |
| 7EG7 | EM | 6.2 Å | D/d=1-1085 |
| 8WAQ | EM | 6.29 Å | D/d=1-1085 |
Showing 20 of 31 experimental structures (best resolution first).
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.