Q99N13: Histone deacetylase 9 (Hdac9)

Histone deacetylase 9 (Hdac9) is a 588-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q99N13.

Gene
Hdac9
Organism
Mus musculus
Length
588 residues
Mean pLDDT
58.1
Model
AF-Q99N13-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 58.1 (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 accurate15%
70 to 90Confident: backbone generally right11%
50 to 70Low: treat with caution25%
Below 50Very low: often disordered regions50%

What pLDDT means and how to read it

Function

Devoided of intrinsic deacetylase activity, promotes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) by recruiting HDAC1 and HDAC3. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Represses MEF2-dependent transcription, inhibits skeletal myogenesis and may be involved in heart development. Protects neurons from apoptosis, both by inhibiting JUN phosphorylation by MAPK10 and by repressing JUN transcription via HDAC1 recruitment to JUN promoter

Subunit structure

Homodimer. Interacts with ETV6 (By similarity). Interacts with MEF2, HDAC1, HDAC3, HDAC4, HDAC5, CTBP1 and MAPK10. The phosphorylated form interacts with 14-3-3. Interacts with FOXP3 in the absence of T-cell stimulation (By similarity)

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1TQEX-ray2.7 ÅX/Y=138-158

More AlphaFold highlights

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