Protein cereblon (CRBN) is a 442-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96SW2.
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The mean pLDDT of this model is 86.6 (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 | 72% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 9% |
What pLDDT means and how to read it
Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as MEIS2, ILF2, GLUL, IKZF1 and CSNK1A1 (PubMed:26990986, PubMed:33009960, PubMed:41565821). Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fibroblast growth factor FGF8 (PubMed:20223979, PubMed:24328678, PubMed:25043012, PubMed:25108355). Maintains presynaptic glutamate release and consequently cognitive functions, such as memory and learning, by negatively regulating large-conductance calcium-activated potassium (BK) channels in excitatory neurons…
Component of a DCX (DDB1-CUL4-X-box) protein ligase complex, at least composed of CRBN, CUL4A, DDB1 and RBX1 (PubMed:25043012, PubMed:41565821). Interacts (via Lon N-terminal domain) with DDB1 (via WD40 beta-propellers A and C); the interaction is direct (PubMed:25043012, PubMed:25108355, PubMed:41565821). Interacts with IKZF1 and IKZF3; the interaction is direct and requires the presence of…
Cytoplasm, Nucleus, Membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4M91 | X-ray | 1.1 Å | B=229-240 |
| 9CUO | X-ray | 1.6 Å | A/B/C/D/E/F=319-427 |
| 9OHQ | X-ray | 1.6 Å | A/C/E/G=319-426 |
| 9DOM | X-ray | 1.69 Å | A/C/E/G=319-426 |
| 7BQV | X-ray | 1.8 Å | A=318-426 |
| 9O91 | X-ray | 1.86 Å | A/C/E/G=318-426 |
| 7BQU | X-ray | 1.9 Å | A=318-426 |
| 9GAO | X-ray | 1.95 Å | A/C=41-187, A/C=249-426 |
| 9FJX | X-ray | 2.0 Å | B=40-442 |
| 8RQC | X-ray | 2.15 Å | A/D=41-187, A/D=249-426 |
| 8RQ8 | X-ray | 2.19 Å | A=41-187, A=249-426 |
| 9OHR | X-ray | 2.34 Å | A/C/E/G=319-426 |
| 9SFM | X-ray | 2.39 Å | B=46-427 |
| 8TNQ | EM | 2.41 Å | B=1-442 |
| 9ODR | X-ray | 2.42 Å | A/B/C/D=319-426 |
| 5FQD | X-ray | 2.45 Å | B/E=41-442 |
| 8OIZ | X-ray | 2.5 Å | B=40-442 |
| 8RQA | X-ray | 2.5 Å | A=41-187, A=249-426 |
| 8TNR | EM | 2.5 Å | B=1-442 |
| 9GY3 | X-ray | 2.5 Å | A/C=41-187, A/C=249-426 |
Showing 20 of 90 experimental structures (best resolution first).
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