Egl nine homolog 1 (EGLN1) is a 426-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9GZT9.
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The mean pLDDT of this model is 71.9 (confident 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 | 47% |
| 70 to 90 | Confident: backbone generally right | 11% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 35% |
What pLDDT means and how to read it
Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B,…
Monomer. Interacts with ING4; the interaction inhibits the hydroxylation of HIF alpha proteins. Interacts with PTGES3 (via PXLE motif); thereby recruiting EGLN1 to the HSP90 pathway to facilitate HIF alpha proteins hydroxylation. Interacts with LIMD1. Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, ELOB and CUL2. Interacts with EPAS1. Interacts with CBFA2T3 (PubMed:25974097). Interacts…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7Q5V | X-ray | 1.17 Å | A=181-407 |
| 7Q5X | X-ray | 1.21 Å | A=181-407 |
| 8Q64 | X-ray | 1.36 Å | A=181-407 |
| 8Q6E | X-ray | 1.37 Å | A=181-407 |
| 8RV1 | X-ray | 1.39 Å | A=181-407 |
| 6QGV | X-ray | 1.4 Å | A=181-407 |
| 8Q6D | X-ray | 1.4 Å | A=181-407 |
| 6YW1 | X-ray | 1.46 Å | A=181-407 |
| 8Q5S | X-ray | 1.49 Å | A=181-407 |
| 4BQY | X-ray | 1.53 Å | A=181-426 |
| 6YW4 | X-ray | 1.53 Å | A=181-407 |
| 6NMQ | X-ray | 1.58 Å | A=180-392 |
| 2HBT | X-ray | 1.6 Å | A=188-426 |
| 8RUT | X-ray | 1.62 Å | A=181-407 |
| 8RUV | X-ray | 1.66 Å | A=181-407 |
| 2G19 | X-ray | 1.7 Å | A=181-417 |
| 3OUI | X-ray | 1.7 Å | A=181-392 |
| 5LB6 | X-ray | 1.7 Å | A=181-426 |
| 5LBB | X-ray | 1.7 Å | A=181-426 |
| 4UWD | X-ray | 1.72 Å | A=181-426 |
Showing 20 of 64 experimental structures (best resolution first).
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