Q92769: Histone deacetylase 2 (HDAC2)

Histone deacetylase 2 (HDAC2) is a 488-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q92769.

Gene
HDAC2
Organism
Homo sapiens
Length
488 residues
Mean pLDDT
85.6
Model
AF-Q92769-F1 v6
Model created
1 Aug 2025
PDB structures
48

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.6 (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 accurate75%
70 to 90Confident: backbone generally right4%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions14%

What pLDDT means and how to read it

Function

Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (PubMed:28497810). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (By similarity). Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR (PubMed:12724404). Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell…

Subunit structure

Part of the core histone deacetylase (HDAC) complex composed of HDAC1, HDAC2, RBBP4 and RBBP7, the core complex associates with SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex (PubMed:10904264). Component of the nucleosome remodeling and deacetylase (NuRD) repressor complex, composed of core proteins MTA1, MTA2, MTA3, RBBP4, RBBP7, HDAC1, HDAC2, MBD2, MBD3, and peripherally associated…

Subcellular location

Nucleus, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7KBGX-ray1.26 ÅA/B/C=1-376
6WBZX-ray1.32 ÅA/B/C=1-376
6WBWX-ray1.46 ÅA/B/C=1-376
7LTLX-ray1.49 ÅA/B/C=1-376
6XEBX-ray1.5 ÅA/B/C=1-376
7ZZPX-ray1.52 ÅA/B/C=1-488
6WHNX-ray1.54 ÅA/B/C=2-385
7MOTX-ray1.54 ÅA/B/C=1-376
7MOZX-ray1.54 ÅA/B/C=1-376
6XDMX-ray1.56 ÅA/B/C=1-376
7ZZTX-ray1.56 ÅA/B/C=1-488
4LY1X-ray1.57 ÅA/B/C=8-376
7LTKX-ray1.59 ÅA/B/C=1-376
9K0GX-ray1.62 ÅA/B/C=1-404
7JS8X-ray1.63 ÅA/B/C=1-376
5IWGX-ray1.66 ÅA/B/C=8-375
7MOXX-ray1.69 ÅA/B/C=1-376
6XECX-ray1.7 ÅA/B/C=1-376
7MOSX-ray1.7 ÅA/B/C=1-376
5IX0X-ray1.72 ÅA/B/C=7-375

Showing 20 of 48 experimental structures (best resolution first).

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