Q6P1X5: Transcription initiation factor TFIID subunit 2 (TAF2)

Transcription initiation factor TFIID subunit 2 (TAF2) is a 1199-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q6P1X5.

Gene
TAF2
Organism
Homo sapiens
Length
1199 residues
Mean pLDDT
73.6
Model
AF-Q6P1X5-F1 v6
Model created
1 Aug 2025
PDB structures
28

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Model confidence (pLDDT)

The mean pLDDT of this model is 73.6 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate21%
70 to 90Confident: backbone generally right53%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions20%

What pLDDT means and how to read it

Function

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, PubMed:9418870, PubMed:9774672). TAF2 forms a promoter DNA binding subcomplex of TFIID, together with TAF7 and TAF1 (PubMed:33795473, PubMed:9774672)

Subunit structure

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:9774672). Interacts with TAF2C1 (PubMed:9418870). Component of the TFTC-HAT complex (PubMed:12601814)

Subcellular location

Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7EGHEM3.04 ÅB=1-1199
7EGBEM3.3 ÅB=1-1199
7EG9EM3.7 ÅB=1-1199
7EGCEM3.9 ÅB=1-1199
7ENAEM4.07 ÅDB=1-1199
7EGAEM4.1 ÅB=1-1199
7ENCEM4.13 ÅDB=1-1199
8GXSEM4.16 ÅDB=1-1199
6MZCEM4.5 ÅB=1-1199
7EDXEM4.5 ÅB=1-1199
8GXQEM5.04 ÅDB=1-1199
8WAKEM5.47 ÅB=1-1199
8WAPEM5.85 ÅB=1-1199
8WANEM6.07 ÅB=1-1199
8WASEM6.13 ÅB=1-1199
7EG7EM6.2 ÅB=1-1199
8WAQEM6.29 ÅB=1-1199
8WAOEM6.4 ÅB=1-1199
7EGDEM6.75 ÅB=1-1199
8WAREM7.2 ÅB=1-1199

Showing 20 of 28 experimental structures (best resolution first).

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