Kelch-like ECH-associated protein 1 (Keap1) is a 624-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9Z2X8.
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The mean pLDDT of this model is 89.9 (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 | 84% |
| 70 to 90 | Confident: backbone generally right | 6% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 7% |
What pLDDT means and how to read it
Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that regulates the response to oxidative stress by targeting NFE2L2/NRF2 for ubiquitination (PubMed:12682069, PubMed:15282312, PubMed:15367669, PubMed:15581590, PubMed:9887101). KEAP1 acts as a key sensor of oxidative and electrophilic stress: in normal conditions, the BCR(KEAP1) complex mediates ubiquitination and degradation of NFE2L2/NRF2, a transcription factor regulating expression of many cytoprotective genes (PubMed:12193649, PubMed:14764894, PubMed:9887101). In response to oxidative stress, different electrophile metabolites trigger non-enzymatic covalent modifications of highly reactive cysteine…
Component of the BCR(KEAP1) E3 ubiquitin ligase complex, at least composed of 2 molecules of CUL3, 2 molecules of KEAP1, and RBX1 (PubMed:15282312, PubMed:16790436, PubMed:27697860). Interacts with NFE2L2/NRF2; the interaction is direct (PubMed:15282312, PubMed:15367669, PubMed:15581590, PubMed:16507366, PubMed:16581765, PubMed:16790436, PubMed:27697860). Forms a ternary complex with NFE2L2/NRF2…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9HWQ | X-ray | 1.14 Å | A=322-624 |
| 7OFE | X-ray | 1.19 Å | A=323-613 |
| 9F2Q | X-ray | 1.2 Å | A=322-624 |
| 6ZF4 | X-ray | 1.21 Å | A=322-624 |
| 7OFD | X-ray | 1.25 Å | A=322-624 |
| 6ZF3 | X-ray | 1.28 Å | A=322-624 |
| 6ZF5 | X-ray | 1.29 Å | A=322-624 |
| 8A46 | X-ray | 1.32 Å | A=322-624 |
| 8Q1R | X-ray | 1.33 Å | A=322-624 |
| 9F2P | X-ray | 1.36 Å | A=322-624 |
| 6ZF7 | X-ray | 1.37 Å | A=322-624 |
| 7OFF | X-ray | 1.37 Å | A=322-624 |
| 6ZEW | X-ray | 1.38 Å | A=322-624 |
| 6ZF6 | X-ray | 1.38 Å | A=322-624 |
| 8Q1Q | X-ray | 1.38 Å | A=322-624 |
| 9HWR | X-ray | 1.4 Å | A=322-624 |
| 9HWU | X-ray | 1.4 Å | A=322-624 |
| 9HWV | X-ray | 1.5 Å | A=322-624 |
| 3WN7 | X-ray | 1.57 Å | A/L=321-609 |
| 1X2J | X-ray | 1.6 Å | A=309-624 |
Showing 20 of 72 experimental structures (best resolution first).
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