Q9FH40: Transcription initiation factor TFIID subunit 14b (TAF14B)

Transcription initiation factor TFIID subunit 14b (TAF14B) is a 268-residue protein from Arabidopsis thaliana. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9FH40.

Gene
TAF14B
Organism
Arabidopsis thaliana
Length
268 residues
Mean pLDDT
77.0
Model
AF-Q9FH40-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 77.0 (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 accurate43%
70 to 90Confident: backbone generally right26%
50 to 70Low: treat with caution15%
Below 50Very low: often disordered regions16%

What pLDDT means and how to read it

Function

Negative regulator of flowering controlling the H4K5 acetylation levels in the FLC and FT chromatin. Positively regulates FLC expression. Component of the transcription factor IID (TFIID) complex that is essential for mediating regulation of RNA polymerase transcription. Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of a NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4 and H2A

Subunit structure

Component of the TFIID complex. TFIID is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs) whose MWs range from 14-217 kDa. Interacts with TAF1, TAF4B and TAF12B. Component of the SWR1 chromatin-remodeling complex. Interacts with FLX, a component of the transcription activator complex FRI-C (PubMed:17340043, PubMed:21282526). Interacts with SWC4, and with EAF1A…

Subcellular location

Cytoplasm, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8JG4X-ray2.3 ÅA/B=38-210

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