P02299: Histone H3 (His3)

Histone H3 (His3) is a 136-residue protein from Drosophila melanogaster. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P02299.

Gene
His3
Organism
Drosophila melanogaster
Length
136 residues
Mean pLDDT
86.4
Model
AF-P02299-F1 v6
Model created
1 Aug 2025
PDB structures
31

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Model confidence (pLDDT)

The mean pLDDT of this model is 86.4 (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 accurate68%
70 to 90Confident: backbone generally right5%
50 to 70Low: treat with caution25%
Below 50Very low: often disordered regions2%

What pLDDT means and how to read it

Function

Core component of nucleosome. 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. Involved in recruitment of Parp1 to chromatin and regulates its activity; inhibits DNA-dependent activation of Parp1 but contributes to nucleosome-dependent activation of Parp1 (PubMed:17827147)

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. Interacts (via N-terminus di- or tri-methylated on Lys-10 (H3K9me2/3)) with rhi (via Chromo domain); this interaction is direct (PubMed:24906153, PubMed:25085419). Interacts with Nasp…

Subcellular location

Nucleus, Chromosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6AT0X-ray1.28 ÅP=6-11
6MHAX-ray1.5 ÅB=6-11
6ASZX-ray1.52 ÅP=6-11
7VRFX-ray1.7 ÅC/D=5-15
4U68X-ray1.8 ÅD/E/F=5-15
1KNAX-ray2.1 ÅP=2-17
9ZQBEM2.1 ÅE/F=1-136
2NQBX-ray2.3 ÅA/E=2-136
9ZQCEM2.37 ÅE/F=1-136
1KNEX-ray2.4 ÅP=2-17
2PYOX-ray2.43 ÅA/E=2-136
4QUFX-ray2.5 ÅP/Q/R/T/U/V=2-16
8UX1EM2.5 ÅA/E=1-136
2YBAX-ray2.55 ÅC/D=2-20
4UUZX-ray2.9 ÅA=1-136
8PP7EM2.91 ÅA/E=2-136
6DZTEM2.99 ÅA/E=1-136
8PP6EM3.18 ÅA/E=2-136
9ZQAEM3.28 ÅE/F=1-136
9MU4EM3.29 Åa/e=37-136

Showing 20 of 31 experimental structures (best resolution first).

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