Q8WUI4: Histone deacetylase 7 (HDAC7)

Histone deacetylase 7 (HDAC7) is a 952-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8WUI4.

Gene
HDAC7
Organism
Homo sapiens
Length
952 residues
Mean pLDDT
62.9
Model
AF-Q8WUI4-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 62.9 (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 accurate36%
70 to 90Confident: backbone generally right5%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions51%

What pLDDT means and how to read it

Function

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (By similarity). 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). Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C (By similarity). During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors (By similarity). May be involved in…

Subunit structure

Interacts with HDAC1, HDAC2, HDAC3, HDAC4, HDAC5, NCOR1, NCOR2, SIN3A, SIN3B, RBBP4, RBBP7, MTA1L1, SAP30 and MBD3 (PubMed:11466315). Interacts with KAT5 and EDNRA (PubMed:11262386, PubMed:12551922). Interacts with the 14-3-3 protein YWHAE, MEF2A, MEF2B and MEF2C. Interacts with ZMYND15 (By similarity). Interacts with KDM5B (PubMed:17373667). Interacts with PML (PubMed:22155184). Interacts with…

Subcellular location

Nucleus, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3C10X-ray2.0 ÅA/B/C=482-903
3C0YX-ray2.1 ÅA/B/C=482-903
3C0ZX-ray2.1 ÅA/B/C=482-903
8Q9QX-ray2.11 ÅX=83-97
3ZNRX-ray2.4 ÅA/B/C=482-903
3ZNSX-ray2.45 ÅA/B/C=482-903

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