P04911: Histone H2A.1 (HTA1)

Histone H2A.1 (HTA1) is a 132-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P04911.

Gene
HTA1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
132 residues
Mean pLDDT
89.4
Model
AF-P04911-F1 v6
Model created
1 Aug 2025
PDB structures
25

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Model confidence (pLDDT)

The mean pLDDT of this model is 89.4 (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 accurate78%
70 to 90Confident: backbone generally right5%
50 to 70Low: treat with caution16%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling

Subunit structure

The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA

Subcellular location

Nucleus, Chromosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4WNNX-ray1.8 ÅA/C/E/G=1-132
3T7KX-ray2.03 ÅC/D=125-132
7DLXX-ray2.4 ÅA/B/C/D/E/F/G/H=2-113
5BT1X-ray2.62 ÅC=1-132
9C9GEM2.91 ÅC/G=1-132
9C9SEM3.09 ÅC/G=1-132
1ID3X-ray3.1 ÅC/G=2-132
7K78EM3.1 ÅC/G=1-132
9C9TEM3.16 ÅC/G=1-132
7SSAEM3.2 ÅC/G=2-132
9OB1EM3.2 ÅC/G=1-132
7ON1EM3.35 Åc/g=1-132
8OW0EM3.4 Åc/g=1-132
8QYVEM3.5 ÅE=1-132
6GEJEM3.6 ÅE/F=1-132
6GENEM3.6 ÅE/F=1-132
8OW1EM3.7 Åc/g=1-132
8XGCEM3.7 ÅP=1-132
8QZ0EM3.8 ÅE=1-132
9CB7EM4.04 ÅC/G=1-132

Showing 20 of 25 experimental structures (best resolution first).

More AlphaFold highlights

About this viewer

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