Q05021: Transcription initiation factor TFIID subunit 7 (TAF7)

Transcription initiation factor TFIID subunit 7 (TAF7) is a 590-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q05021.

Gene
TAF7
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
590 residues
Mean pLDDT
69.0
Model
AF-Q05021-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 69.0 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate44%
70 to 90Confident: backbone generally right8%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions40%

What pLDDT means and how to read it

Function

Functions as a component 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 pre-initiation 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. TAF7 is responsible for the recruitment of BDF1 to TATA element containing promoters

Subunit structure

TAF7 interacts with BDF1. 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

Subcellular location

Nucleus

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
4OY2X-ray2.9 ÅB/D/F=86-320

More AlphaFold highlights

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