Cullin-3 (CUL3) is a 768-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13618.
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The mean pLDDT of this model is 90.2 (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 | 80% |
| 70 to 90 | Confident: backbone generally right | 13% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Core component of multiple cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:29695787). BCR complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins (PubMed:27565346). As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the BCR complex…
Forms neddylation-dependent homodimers. Component of multiple BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes formed of CUL3, RBX1 and a variable BTB domain-containing protein acting as both, adapter to cullin and substrate recognition subunit. The BCR complex may be active as a heterodimeric complex, in which NEDD8, covalently attached to one CUL3 molecule, binds to the C-terminus of…
Nucleus, Golgi apparatus, Cell projection, cilium, flagellum, Cytoplasm, cytoskeleton, spindle, Cytoplasm, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Cytoplasm, cytoskeleton, spindle pole
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6I2M | X-ray | 2.3 Å | B=23-388 |
| 4EOZ | X-ray | 2.4 Å | B/D=20-381 |
| 4AP2 | X-ray | 2.8 Å | B=1-388 |
| 8I79 | EM | 2.8 Å | B/C/E/H/J=22-388 |
| 4APF | X-ray | 3.1 Å | B=23-388 |
| 5NLB | X-ray | 3.45 Å | B=26-381 |
| 4HXI | X-ray | 3.51 Å | B=20-381 |
| 8U80 | EM | 3.6 Å | C1/C2/C3/C4/C5=1-381 |
| 8KHP | EM | 3.67 Å | C/D=1-768 |
| 8H3Q | EM | 3.76 Å | C=1-768 |
| 8K8T | EM | 3.8 Å | C/D=1-768 |
| 8U81 | EM | 3.82 Å | C1/C2/C3/C4/C5=1-381 |
| 8U82 | EM | 3.84 Å | C1/C2/C3/C4/C5=2-381 |
| 8U84 | EM | 3.88 Å | C1/C2/C3/C4/C5=1-381 |
| 9EGL | EM | 3.93 Å | J=1-768 |
| 8GQ6 | EM | 3.96 Å | C/F=1-768 |
| 8U83 | EM | 3.98 Å | C1/C2/C3/C4/C5=1-381 |
| 8K9I | EM | 4.2 Å | C=25-768 |
| 8H38 | EM | 4.25 Å | L=1-768 |
| 8H36 | EM | 4.6 Å | C/F=1-768 |
Showing 20 of 29 experimental structures (best resolution first).
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