Aryl hydrocarbon receptor nuclear translocator (ARNT) is a 789-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P27540.
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The mean pLDDT of this model is 55.5 (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 | 19% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 59% |
What pLDDT means and how to read it
Transcription factor that functions as an obligate heterodimerization partner for several basic helix-loop-helix PER-ARNT-SIM (bHLH-PAS) proteins. Forms heterodimers with the aryl hydrocarbon receptor (AHR) to mediate the transcriptional response to xenobiotics by binding xenobiotic response elements (XREs) or dioxin response elements (DREs) in target gene promoters (PubMed:28396409, PubMed:34521881). Also heterodimerizes with hypoxia-inducible factor alpha subunits (HIF1A, EPAS1, NPAS1 or NPAS3) to form hypoxia-inducible transcription factors that bind hypoxia response elements (HREs) and activate genes involved in cellular and systemic responses to hypoxia, including angiogenesis,…
Monomer. Homodimer only upon binding to a DNA (By similarity). Efficient DNA binding requires dimerization with another bHLH-PAS protein. Interacts with TACC3 (By similarity). Interacts with HIF1A, EPAS1, NPAS1 and NPAS3; forms a heterodimer that binds core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (By similarity) (PubMed:16181639,…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3F1P | X-ray | 1.17 Å | B=356-470 |
| 3F1N | X-ray | 1.48 Å | B=356-470 |
| 2B02 | X-ray | 1.5 Å | A=354-470 |
| 3H82 | X-ray | 1.5 Å | B=356-470 |
| 4GHI | X-ray | 1.5 Å | B=356-470 |
| 6D0C | X-ray | 1.5 Å | B=356-470 |
| 4H6J | X-ray | 1.52 Å | B=357-470 |
| 6X21 | X-ray | 1.54 Å | B=356-467 |
| 9I64 | X-ray | 1.56 Å | B=355-470 |
| 3F1O | X-ray | 1.6 Å | B=356-470 |
| 4EQ1 | X-ray | 1.6 Å | A/B=357-464 |
| 6CZW | X-ray | 1.6 Å | B=356-470 |
| 6D0B | X-ray | 1.6 Å | B=356-470 |
| 3H7W | X-ray | 1.65 Å | B=356-470 |
| 4XT2 | X-ray | 1.7 Å | B/D=356-470 |
| 8CK3 | X-ray | 1.71 Å | B=356-470 |
| 4GS9 | X-ray | 1.72 Å | B=356-470 |
| 5TBM | X-ray | 1.85 Å | B=354-467 |
| 6D09 | X-ray | 1.85 Å | B=356-470 |
| 5UFP | X-ray | 1.9 Å | B=356-467 |
Showing 20 of 43 experimental structures (best resolution first).
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