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.
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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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 6% |
| 70 to 90 | Confident: backbone generally right | 30% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 58% |
What pLDDT means and how to read it
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…
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…
Nucleus, Chromosome, telomere, Nucleus, PML body
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3QL9 | X-ray | 0.93 Å | A=167-289 |
| 6G0O | X-ray | 1.4 Å | B=1027-1037 |
| 5GRQ | X-ray | 1.58 Å | C/D=1256-1285 |
| 3QLA | X-ray | 1.6 Å | A/D=167-289 |
| 3QLN | X-ray | 1.9 Å | A/B=167-289 |
| 5Y18 | X-ray | 2.2 Å | B=1268-1289 |
| 3QLC | X-ray | 2.5 Å | A/B=167-289 |
| 4W5A | X-ray | 2.6 Å | A/B/E=167-289 |
| 5Y6O | X-ray | 3.1 Å | A/B/C/D/E/F/G/H/I=1265-1288 |
| 2JM1 | NMR | A=159-296 | |
| 2LBM | NMR | A=159-296 | |
| 2LD1 | NMR | A=159-296 |
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