P46100: Transcriptional regulator ATRX (ATRX)

Transcriptional regulator ATRX (ATRX) is a 2492-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P46100.

Gene
ATRX
Organism
Homo sapiens
Length
2492 residues
Mean pLDDT
51.8
Model
AF-P46100-F1 v6
Model created
1 Aug 2025
PDB structures
12

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Model confidence (pLDDT)

The mean pLDDT of this model is 51.8 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate6%
70 to 90Confident: backbone generally right30%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions58%

What pLDDT means and how to read it

Function

Involved in transcriptional regulation and chromatin remodeling. Facilitates DNA replication in multiple cellular environments and is required for efficient replication of a subset of genomic loci. Binds to DNA tandem repeat sequences in both telomeres and euchromatin and in vitro binds DNA quadruplex structures. May help stabilizing G-rich regions into regular chromatin structures by remodeling G4 DNA and incorporating H3.3-containing nucleosomes. Catalytic component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and…

Subunit structure

Interacts with DAXX to form the chromatin remodeling complex ATRX:DAXX. Probably binds EZH2. Binds annexin V in a calcium and phosphatidylcholine/phosphatidylserine-dependent manner. Interacts directly with CBX5 via the PxVxL motif. Interacts with RAD50, MRE11 and NBN; indicative for an association with the MRN complex. Interacts with histone MACROH2A1. Interacts with histone H3 peptides…

Subcellular location

Nucleus, Chromosome, telomere, Nucleus, PML body

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3QL9X-ray0.93 ÅA=167-289
6G0OX-ray1.4 ÅB=1027-1037
5GRQX-ray1.58 ÅC/D=1256-1285
3QLAX-ray1.6 ÅA/D=167-289
3QLNX-ray1.9 ÅA/B=167-289
5Y18X-ray2.2 ÅB=1268-1289
3QLCX-ray2.5 ÅA/B=167-289
4W5AX-ray2.6 ÅA/B/E=167-289
5Y6OX-ray3.1 ÅA/B/C/D/E/F/G/H/I=1265-1288
2JM1NMRA=159-296
2LBMNMRA=159-296
2LD1NMRA=159-296

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