Hypoxia-inducible factor 1-alpha (HIF1A) is a 826-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q16665.
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The mean pLDDT of this model is 60.8 (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 | 31% |
| 70 to 90 | Confident: backbone generally right | 8% |
| 50 to 70 | Low: treat with caution | 13% |
| Below 50 | Very low: often disordered regions | 48% |
What pLDDT means and how to read it
Functions as a master transcriptional regulator of the adaptive response to hypoxia (PubMed:11292861, PubMed:11566883, PubMed:15465032, PubMed:16973622, PubMed:17610843, PubMed:18658046, PubMed:20624928, PubMed:22009797, PubMed:30125331, PubMed:9887100). Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia (PubMed:11292861, PubMed:11566883, PubMed:15465032, PubMed:16973622, PubMed:17610843, PubMed:20624928, PubMed:22009797, PubMed:30125331,…
Interacts with the ARNT; forms a heterodimer that binds core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (PubMed:10944113, PubMed:20699359). Interacts with COPS5; the interaction increases the transcriptional activity of HIF1A through increased stability (By similarity). Interacts with EP300 (via TAZ-type 1 domains); the interaction is stimulated…
Cytoplasm, Nucleus, Nucleus speckle
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4H6J | X-ray | 1.52 Å | A=238-348 |
| 4AJY | X-ray | 1.73 Å | H=559-577 |
| 6GMR | X-ray | 1.75 Å | H=560-577 |
| 8HE0 | X-ray | 1.8 Å | B=717-757 |
| 5L9V | X-ray | 1.83 Å | C/D=395-413 |
| 6GFX | X-ray | 1.83 Å | D=560-577 |
| 1LM8 | X-ray | 1.85 Å | H=556-575 |
| 8HE3 | X-ray | 1.9 Å | B=749-757 |
| 5L9B | X-ray | 1.95 Å | C/D=556-574 |
| 1LQB | X-ray | 2.0 Å | D=549-582 |
| 3HQR | X-ray | 2.0 Å | S=558-574 |
| 7QGS | X-ray | 2.0 Å | B=794-826 |
| 7LVS | X-ray | 2.02 Å | F=796-826 |
| 5JWP | X-ray | 2.1 Å | B=788-806 |
| 5LAS | X-ray | 2.1 Å | C/D=395-413 |
| 1H2K | X-ray | 2.15 Å | S=786-826 |
| 1H2L | X-ray | 2.25 Å | S=786-826 |
| 6YW3 | X-ray | 2.28 Å | S=556-574 |
| 2ILM | X-ray | 2.3 Å | S=786-826 |
| 3HQU | X-ray | 2.3 Å | S=558-574 |
Showing 20 of 25 experimental structures (best resolution first).
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