P16104: Histone H2AX (H2AX)

Histone H2AX (H2AX) is a 143-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P16104.

Gene
H2AX
Organism
Homo sapiens
Length
143 residues
Mean pLDDT
86.3
Model
AF-P16104-F1 v6
Model created
1 Aug 2025
PDB structures
28

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Model confidence (pLDDT)

The mean pLDDT of this model is 86.3 (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 accurate72%
70 to 90Confident: backbone generally right4%
50 to 70Low: treat with caution17%
Below 50Very low: often disordered regions8%

What pLDDT means and how to read it

Function

Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by…

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 (Probable). Interacts with numerous proteins required for DNA damage signaling and repair when phosphorylated on Ser-140 (PubMed:12419185, PubMed:12607005, PubMed:15201865). These include MDC1,…

Subcellular location

Nucleus, Chromosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3U3ZX-ray1.5 ÅB=140-143
6ZWKX-ray1.55 ÅG/H/I/J/K/L=134-143
1YDPX-ray1.9 ÅP=78-86
3SHVX-ray2.1 ÅC/D=134-143
3SQDX-ray2.15 ÅC/D=134-143
6K1KX-ray2.2 ÅC/G=1-143
2AZMX-ray2.41 ÅC/D=134-143
2DYPX-ray2.5 ÅC=78-86
3SZMX-ray2.63 ÅI/J/K/L/M/N/O/P=134-143
6K1IX-ray2.75 ÅC/G=1-143
6K1JX-ray2.85 ÅC/G=1-143
9Q8XEM2.94 ÅC/G=1-143
9MLREM3.1 ÅC/G=1-143
2D31X-ray3.2 ÅC/F=78-86
9MMKEM3.2 ÅC/G=1-143
9MLNEM3.3 ÅC/G=1-143
7YQKEM3.38 ÅC/G=11-121
9Q80EM3.39 ÅC/G=1-143
9MMTEM3.4 ÅC/G=1-143
9MLSEM3.6 ÅC/G=1-143

Showing 20 of 28 experimental structures (best resolution first).

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