Endothelial PAS domain-containing protein 1 (EPAS1) is a 870-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q99814.
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The mean pLDDT of this model is 58.6 (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 | 29% |
| 70 to 90 | Confident: backbone generally right | 6% |
| 50 to 70 | Low: treat with caution | 12% |
| Below 50 | Very low: often disordered regions | 53% |
What pLDDT means and how to read it
Transcription factor involved in the induction of oxygen regulated genes. Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (By similarity). Regulates the vascular endothelial growth factor (VEGF) expression and seems to be implicated in the development of blood vessels and the tubular system of lung. May also play a role in the formation of the endothelium that gives rise to the blood brain barrier. Potent activator of the Tie-2 tyrosine kinase expression. Activation requires recruitment of transcriptional coactivators such as CREBBP and probably EP300. Interaction with redox regulatory protein…
Interacts with HIF3A (By similarity). Efficient DNA binding requires dimerization with another bHLH-PAS protein. Heterodimerizes with ARNT; heterodimer binds to the hypoxia response element (HRE) of target gene promoters (PubMed:16181639). Interacts with CREBBP (By similarity). Interacts with EGLN1. Interacts with VHL (PubMed:19208626)
Nucleus, Nucleus speckle
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3F1P | X-ray | 1.17 Å | A=239-350 |
| 7Q5V | X-ray | 1.17 Å | B=523-542 |
| 7Q5X | X-ray | 1.21 Å | B=523-542 |
| 8Q64 | X-ray | 1.36 Å | B=523-542 |
| 8Q6E | X-ray | 1.37 Å | B=523-542 |
| 8RV1 | X-ray | 1.39 Å | B=523-542 |
| 8Q6D | X-ray | 1.4 Å | B=523-542 |
| 3F1N | X-ray | 1.48 Å | A=239-350 |
| 8Q5S | X-ray | 1.49 Å | B=523-542 |
| 3H82 | X-ray | 1.5 Å | A=239-350 |
| 4GHI | X-ray | 1.5 Å | A=239-350 |
| 6D0C | X-ray | 1.5 Å | A=239-350 |
| 6X21 | X-ray | 1.54 Å | A=239-348 |
| 9I64 | X-ray | 1.56 Å | A=240-350 |
| 3F1O | X-ray | 1.6 Å | A=239-350 |
| 6CZW | X-ray | 1.6 Å | A=239-350 |
| 6D0B | X-ray | 1.6 Å | A=239-350 |
| 8RUT | X-ray | 1.62 Å | B=523-542 |
| 3H7W | X-ray | 1.65 Å | A=239-350 |
| 8RUV | X-ray | 1.66 Å | B=524-542 |
Showing 20 of 43 experimental structures (best resolution first).
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