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.
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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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 75% |
| 70 to 90 | Confident: backbone generally right | 4% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 14% |
What pLDDT means and how to read it
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…
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…
Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7KBG | X-ray | 1.26 Å | A/B/C=1-376 |
| 6WBZ | X-ray | 1.32 Å | A/B/C=1-376 |
| 6WBW | X-ray | 1.46 Å | A/B/C=1-376 |
| 7LTL | X-ray | 1.49 Å | A/B/C=1-376 |
| 6XEB | X-ray | 1.5 Å | A/B/C=1-376 |
| 7ZZP | X-ray | 1.52 Å | A/B/C=1-488 |
| 6WHN | X-ray | 1.54 Å | A/B/C=2-385 |
| 7MOT | X-ray | 1.54 Å | A/B/C=1-376 |
| 7MOZ | X-ray | 1.54 Å | A/B/C=1-376 |
| 6XDM | X-ray | 1.56 Å | A/B/C=1-376 |
| 7ZZT | X-ray | 1.56 Å | A/B/C=1-488 |
| 4LY1 | X-ray | 1.57 Å | A/B/C=8-376 |
| 7LTK | X-ray | 1.59 Å | A/B/C=1-376 |
| 9K0G | X-ray | 1.62 Å | A/B/C=1-404 |
| 7JS8 | X-ray | 1.63 Å | A/B/C=1-376 |
| 5IWG | X-ray | 1.66 Å | A/B/C=8-375 |
| 7MOX | X-ray | 1.69 Å | A/B/C=1-376 |
| 6XEC | X-ray | 1.7 Å | A/B/C=1-376 |
| 7MOS | X-ray | 1.7 Å | A/B/C=1-376 |
| 5IX0 | X-ray | 1.72 Å | A/B/C=7-375 |
Showing 20 of 48 experimental structures (best resolution first).
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