Cullin-1 (CUL1) is a 776-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13616.
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The mean pLDDT of this model is 88.8 (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 | 21% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. SCF complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins (PubMed:22017875, PubMed:22017877, PubMed:27565346). In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. May contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (PubMed:38326650). The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the…
Component of multiple Cul1-RING E3 ubiquitin-protein ligase complexes commonly known as SCF (SKP1-CUL1-F-box) complexes, consisting of CUL1, SKP1, RBX1 and a variable F-box domain-containing protein as substrate-specific subunit (PubMed:10230406, PubMed:11961546, PubMed:15145941, PubMed:15531760, PubMed:16714087, PubMed:16797541, PubMed:17098746, PubMed:18203720, PubMed:20596027,…
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3TDU | X-ray | 1.5 Å | C/D=702-776 |
| 5V89 | X-ray | 1.55 Å | C=702-776 |
| 3TDZ | X-ray | 2.0 Å | C/D=702-776 |
| 8CAF | X-ray | 2.66 Å | E/H=698-776 |
| 7Z8R | EM | 2.7 Å | C=1-776 |
| 7Z8V | EM | 2.7 Å | C=1-776 |
| 8OR3 | EM | 2.9 Å | A=1-776 |
| 9QO4 | EM | 2.95 Å | I=1-776 |
| 1LDJ | X-ray | 3.0 Å | A=17-776 |
| 4F52 | X-ray | 3.0 Å | A/C=411-690 |
| 7Z8T | EM | 3.0 Å | C=1-776 |
| 9XZL | EM | 3.0 Å | C=1-776 |
| 9EFV | EM | 3.03 Å | J=1-776 |
| 1LDK | X-ray | 3.1 Å | A=15-410, B=411-776 |
| 1U6G | X-ray | 3.1 Å | A=1-776 |
| 7ZBZ | EM | 3.1 Å | C=1-776 |
| 8OR0 | EM | 3.1 Å | A=1-776 |
| 8UBT | EM | 3.1 Å | A=13-776 |
| 4P5O | X-ray | 3.11 Å | A/C=410-776 |
| 9XZJ | EM | 3.13 Å | C=1-776 |
Showing 20 of 48 experimental structures (best resolution first).
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