Kelch-like ECH-associated protein 1 (KEAP1) is a 624-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q14145.
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The mean pLDDT of this model is 90.1 (very high 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 | 82% |
| 70 to 90 | Confident: backbone generally right | 9% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 6% |
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:14585973, PubMed:15379550, PubMed:15572695, PubMed:15601839, PubMed:15983046, PubMed:37339955). 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:15601839, PubMed:16006525). 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:15572695, PubMed:15601839, PubMed:15983046, PubMed:17127771, PubMed:18251510, PubMed:24896564). Interacts with NFE2L2/NRF2; the interaction is direct (PubMed:15379550, PubMed:15601839, PubMed:16006525, PubMed:16888629, PubMed:18387606). Forms a ternary complex…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8XGK | X-ray | 1.32 Å | A=310-624 |
| 1ZGK | X-ray | 1.35 Å | A=321-609 |
| 6TYM | X-ray | 1.42 Å | A=321-609 |
| 8XGV | X-ray | 1.42 Å | A=310-624 |
| 9KVW | X-ray | 1.44 Å | A=322-609 |
| 8IXS | X-ray | 1.48 Å | A=310-624 |
| 2FLU | X-ray | 1.5 Å | X=321-609 |
| 8IVR | X-ray | 1.5 Å | A=310-624 |
| 9R1Z | X-ray | 1.5 Å | A=325-609 |
| 6LRZ | X-ray | 1.54 Å | A=311-616 |
| 8PKW | X-ray | 1.54 Å | A/B=312-623 |
| 8PKV | X-ray | 1.55 Å | A/B=312-623 |
| 9M24 | X-ray | 1.57 Å | A=321-609 |
| 6V6Z | X-ray | 1.6 Å | A/B/C/D=321-609 |
| 9R1C | X-ray | 1.69 Å | A=321-609 |
| 9IH9 | X-ray | 1.7 Å | A/B/C=321-609 |
| 9VD2 | X-ray | 1.7 Å | A=321-609 |
| 8PKU | X-ray | 1.73 Å | A/B=312-623 |
| 6HWS | X-ray | 1.75 Å | A=321-609 |
| 8PKX | X-ray | 1.79 Å | A/B=312-623 |
Showing 20 of 122 experimental structures (best resolution first).
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