Q9ESU6: Bromodomain-containing protein 4 (Brd4)

Bromodomain-containing protein 4 (Brd4) is a 1400-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9ESU6.

Gene
Brd4
Organism
Mus musculus
Length
1400 residues
Mean pLDDT
55.0
Model
AF-Q9ESU6-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 55.0 (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 accurate17%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions61%

What pLDDT means and how to read it

Function

Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation (PubMed:10938129, PubMed:29379197). Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure (PubMed:10938129). During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters. Also recruits P-TEFb complex to distal enhancers, so called…

Subunit structure

Binds acetylated histone H4. Interacts with p53/TP53; the interaction is direct (By similarity). Interacts (via CTD region) with CDK9 and CCNT1, acting as an associated component of P-TEFb complex (PubMed:16109376). Interacts with RELA (when acetylated at 'Lys-310'). Interacts (via NET domain) with NSD3, CHD4, BICRA and ATAD5. The interaction with BICRA bridges BRD4 to the GBAF complex.…

Subcellular location

Nucleus, Chromosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3JVLX-ray1.2 ÅA=349-464
3JVMX-ray1.2 ÅA=349-464
3JVJX-ray1.55 ÅA=42-168
3MULX-ray1.65 ÅA=42-168
3MUKX-ray1.75 ÅA=42-168
2DWWX-ray1.8 ÅA=347-460
3JVKX-ray1.8 ÅA=42-168
2JNSNMRA=601-683

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