Histone acetyltransferase KAT6A (KAT6A) is a 2004-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q92794.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 48.7 (very 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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 17% |
| 70 to 90 | Confident: backbone generally right | 10% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 70% |
What pLDDT means and how to read it
Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro) (PubMed:11742995, PubMed:11965546). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity (PubMed:11965546). May act as a transcriptional coactivator for RUNX1 and RUNX2 (PubMed:12771199). Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its transcriptional activity via association with PML (PubMed:23431171). May play a role in leukemogenic gene transcription (PubMed:39794553)
Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3 (PubMed:11965546). Interacts with RUNX1; phosphorylation of RUNX1 enhances the interaction (PubMed:11742995). Interacts with RUNX2 (PubMed:11965546). Interacts with p53/TP53 (PubMed:23431171). Interacts with PML (isoform PML-4) and this interaction positively regulates its…
Nucleus, Nucleus, nucleolus, Nucleus, nucleoplasm, Nucleus, PML body
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5B78 | X-ray | 1.4 Å | A=194-323 |
| 3V43 | X-ray | 1.47 Å | A=204-313 |
| 7Y43 | X-ray | 1.5 Å | A=1-85 |
| 5B77 | X-ray | 1.55 Å | A=194-323 |
| 4LK9 | X-ray | 1.6 Å | A=194-323 |
| 4LKA | X-ray | 1.61 Å | A=194-323 |
| 5B76 | X-ray | 1.65 Å | A=194-323 |
| 5B75 | X-ray | 1.7 Å | A=194-323 |
| 9DZN | X-ray | 1.72 Å | A=501-784 |
| 8H7A | X-ray | 1.92 Å | A/B/E/F=1-85 |
| 6LSB | X-ray | 2.0 Å | A=194-323 |
| 9ARR | X-ray | 2.1 Å | C=1005-1017 |
| 2OZU | X-ray | 2.3 Å | A=497-780 |
| 9ARO | X-ray | 2.3 Å | E/F/G/H=1005-1008 |
| 4LLB | X-ray | 2.5 Å | A/B=194-323 |
| 8DD5 | X-ray | 2.58 Å | A=501-784 |
| 9FKR | X-ray | 2.69 Å | A/B=509-778 |
| 2RC4 | X-ray | 3.0 Å | A=501-784 |
| 4LJN | X-ray | 3.0 Å | A=194-323 |
| 1M36 | NMR | A=533-563 |
Showing 20 of 21 experimental structures (best resolution first).
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.