O14929: Histone acetyltransferase type B catalytic subunit (HAT1)

Histone acetyltransferase type B catalytic subunit (HAT1) is a 419-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O14929.

Gene
HAT1
Organism
Homo sapiens
Length
419 residues
Mean pLDDT
92.8
Model
AF-O14929-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 92.8 (very high 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 accurate80%
70 to 90Confident: backbone generally right15%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Histone acetyltransferase that plays a role in different biological processes including cell cycle progression, glucose metabolism, histone production or DNA damage repair (PubMed:20953179, PubMed:23653357, PubMed:31278053, PubMed:32081014). Coordinates histone production and acetylation via H4 promoter binding (PubMed:31278053). Acetylates histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser extent, histone H2A at 'Lys-5' (H2AK5ac) (PubMed:11585814, PubMed:22615379). Drives H4 production by chromatin binding to support chromatin replication and acetylation. Since transcription of H4 genes is tightly coupled to S-phase, plays an important role in S-phase entry and…

Subunit structure

Catalytic subunit of the type B histone acetyltransferase (HAT) complex, composed of RBBP7 and HAT1. Interacts with histones H4 and H2A. The interaction is dependent of the ability of RBBP7 to bind to the N-terminus of histones. Component of the histone H3.1 and H3.3 complexes

Subcellular location

Nucleus matrix, Mitochondrion, Cytoplasm, Nucleus, Nucleus, nucleoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6VO5X-ray1.6 ÅA/B=20-341
2P0WX-ray1.9 ÅA/B=20-341
9MJGX-ray2.58 ÅA/B/C/D/E/F/G/H=20-341

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