Q9H7Z6: Histone acetyltransferase KAT8 (KAT8)

Histone acetyltransferase KAT8 (KAT8) is a 458-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9H7Z6.

Gene
KAT8
Organism
Homo sapiens
Length
458 residues
Mean pLDDT
81.7
Model
AF-Q9H7Z6-F1 v6
Model created
1 Aug 2025
PDB structures
43

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 81.7 (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 accurate53%
70 to 90Confident: backbone generally right23%
50 to 70Low: treat with caution13%
Below 50Very low: often disordered regions11%

What pLDDT means and how to read it

Function

Histone acetyltransferase that catalyzes histone H4 acetylation at 'Lys-5'- and 'Lys-8' (H4K5ac and H4K8ac) or 'Lys-16' (H4K16ac), depending on the context (PubMed:12397079, PubMed:16227571, PubMed:16543150, PubMed:20018852, PubMed:21217699, PubMed:22020126, PubMed:22547026, PubMed:31794431, PubMed:33837287). Catalytic component of the MSL histone acetyltransferase complex, a multiprotein complex that mediates the majority of histone H4 acetylation at 'Lys-16' (H4K16ac), an epigenetic mark that prevents chromatin compaction (PubMed:12397079, PubMed:16227571, PubMed:16543150, PubMed:21217699, PubMed:22020126, PubMed:22547026, PubMed:33657400, PubMed:33837287). H4K16ac constitutes the only…

Subunit structure

Component of a multisubunit histone acetyltransferase complex (MSL) at least composed of the MOF/KAT8, MSL1/hampin, MSL2L1 and MSL3L1 (PubMed:16227571, PubMed:16543150, PubMed:21217699, PubMed:22547026, PubMed:30224647, PubMed:33657400, PubMed:33837287). Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 (PubMed:16543150,…

Subcellular location

Nucleus, Chromosome, Mitochondrion

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9OOAX-ray1.39 ÅA=174-449
2PQ8X-ray1.45 ÅA=174-449
9OOFX-ray1.68 ÅA=174-449
6OINX-ray1.7 ÅA=176-448
6OIOX-ray1.7 ÅA=176-448
6OIQX-ray1.75 ÅA=176-448
6OWIX-ray1.75 ÅA=176-448
5WCIX-ray1.78 ÅA=174-449
6OIPX-ray1.8 ÅA=176-448
8W13X-ray1.81 ÅA=174-449
9OOJX-ray1.82 ÅA=174-449
9OOBX-ray1.83 ÅA=174-449
6BA2X-ray1.85 ÅA=174-449
6PDGX-ray1.92 ÅA=177-448
2GIVX-ray1.94 ÅA=174-449
6BA4X-ray1.95 ÅA=174-449
6PDCX-ray1.96 ÅA=177-448
6OWHX-ray2.0 ÅA=176-448
6OIRX-ray2.03 ÅA=176-448
4DNCX-ray2.05 ÅA/B=170-458

Showing 20 of 43 experimental structures (best resolution first).

More AlphaFold highlights

About this viewer

MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.