Q9HAW0: Transcription factor IIIB 50 kDa subunit (BRF2)

Transcription factor IIIB 50 kDa subunit (BRF2) is a 419-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9HAW0.

Gene
BRF2
Organism
Homo sapiens
Length
419 residues
Mean pLDDT
84.3
Model
AF-Q9HAW0-F1 v6
Model created
1 Aug 2025
PDB structures
22

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Model confidence (pLDDT)

The mean pLDDT of this model is 84.3 (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 accurate67%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions13%

What pLDDT means and how to read it

Function

General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites (PubMed:11040218, PubMed:11121026, PubMed:11564744, PubMed:26638071). Contributes to the regulation of gene expression; functions as activator in the absence of oxidative stress (PubMed:26638071). Down-regulates expression of target genes in response to oxidative stress (PubMed:26638071). Overexpression protects cells against apoptosis in response to oxidative stress (PubMed:26638071)

Subunit structure

Component of TFIIIB complexes. The TFIIIB complex has two activities, alpha and beta. The TFIIIB-alpha activity complex is composed of TBP, BDP1, and a complex containing both BRF2 and at least four stably associated proteins; this complex inhibits the transcription by pol III via its phosphorylation by CK2; YY1 facilitates the TFIIIB-alpha complex formation. Interacts with TBP; this interaction…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4ROCX-ray1.9 ÅA=62-419
4ROEX-ray2.2 ÅA=62-419
4RODX-ray2.7 ÅA=62-419
5N9GX-ray2.7 ÅA/F=62-419
9K39EM2.8 ÅV=1-419
9K36EM2.9 ÅV=1-419
9K2GEM3.0 ÅV=1-419
9K3UEM3.0 ÅV=1-419
9K38EM3.1 ÅV=1-419
9FSOEM3.28 ÅS=1-419
9LXNEM3.3 ÅV=1-419
9FSPEM3.39 ÅS=1-419
8IUHEM3.4 ÅV=1-419
9K3VEM3.5 ÅV=1-419
9LKTEM3.5 ÅV=1-419
9FSQEM3.51 ÅS=1-419
9LXOEM3.6 ÅV=1-419
9FSREM3.76 ÅS=1-419
8ITYEM3.9 ÅV=1-419
8IUEEM4.1 ÅV=1-419

Showing 20 of 22 experimental structures (best resolution first).

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