Nuclear factor erythroid 2-related factor 2 (NFE2L2) is a 605-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q16236.
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The mean pLDDT of this model is 60.5 (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 | 21% |
| 70 to 90 | Confident: backbone generally right | 18% |
| 50 to 70 | Low: treat with caution | 13% |
| Below 50 | Very low: often disordered regions | 48% |
What pLDDT means and how to read it
Transcription factor that plays a key role in the response to oxidative stress: binds to antioxidant response (ARE) elements present in the promoter region of many cytoprotective genes, such as phase 2 detoxifying enzymes, and promotes their expression, thereby neutralizing reactive electrophiles (PubMed:11035812, PubMed:19489739, PubMed:29018201, PubMed:31398338). In normal conditions, ubiquitinated and degraded in the cytoplasm by the BCR(KEAP1) complex (PubMed:11035812, PubMed:15601839, PubMed:29018201). In response to oxidative stress, electrophile metabolites inhibit activity of the BCR(KEAP1) complex, promoting nuclear accumulation of NFE2L2/NRF2, heterodimerization with one of the…
Heterodimer; heterodimerizes with small Maf proteins (By similarity). Interacts (via the bZIP domain) with MAFG and MAFK; required for binding to antioxidant response elements (AREs) on DNA (By similarity). Interacts with KEAP1; the interaction is direct and promotes ubiquitination by the BCR(KEAP1) E3 ubiquitin ligase complex (PubMed:15601839, PubMed:16888629). Forms a ternary complex with…
Cytoplasm, cytosol, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2FLU | X-ray | 1.5 Å | P=69-84 |
| 9T8Y | X-ray | 1.79 Å | B=340-351 |
| 4IFL | X-ray | 1.8 Å | P=69-84 |
| 8HZ8 | X-ray | 1.81 Å | C=172-175 |
| 7K2A | X-ray | 1.9 Å | P=76-83 |
| 5WFV | X-ray | 1.91 Å | P=76-84 |
| 7K2K | X-ray | 1.98 Å | P=77-82 |
| 7K2E | X-ray | 2.03 Å | P=77-82 |
| 8EJR | X-ray | 2.08 Å | C=76-82 |
| 7K2C | X-ray | 2.11 Å | P=77-82 |
| 7K28 | X-ray | 2.15 Å | P=77-84 |
| 9T95 | X-ray | 2.15 Å | B=340-351 |
| 3ZGC | X-ray | 2.2 Å | C=76-82 |
| 7K29 | X-ray | 2.2 Å | P=76-84 |
| 7K2D | X-ray | 2.21 Å | P=77-82 |
| 7X5E | X-ray | 2.3 Å | B/F=452-560 |
| 7X5G | X-ray | 2.3 Å | B/F=452-560 |
| 7K2B | X-ray | 2.31 Å | P=77-83 |
| 6T7V | X-ray | 2.6 Å | I=76-84 |
| 7X5F | X-ray | 2.6 Å | B/F=452-560 |
Showing 20 of 23 experimental structures (best resolution first).
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