Cullin-2 (CUL2) is a 745-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13617.
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The mean pLDDT of this model is 85.8 (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 | 39% |
| 70 to 90 | Confident: backbone generally right | 53% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
Core component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins (PubMed:11384984, PubMed:26138980, PubMed:29775578, PubMed:29779948, PubMed:37844242, PubMed:38326650). CUL2 serves as a rigid scaffold in the complex and may contribute to catalysis through positioning of the substrate and the E2 ubiquitin-conjugating enzyme (PubMed:10973499, PubMed:11384984, PubMed:12609982, PubMed:24076655, PubMed:9122164, PubMed:37844242, PubMed:38326650). The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the…
Component of multiple Cul2-RING (CRL2) E3 ubiquitin-protein ligase complexes consisting of CUL2, Elongin BC (ELOB and ELOC), RBX1 and a variable substrate-specific adapter; this complex is also known as ECS (Elongin BC-CUL2/5-SOCS-box protein) complex and may consist of CUL2 or CUL5 (PubMed:10973499, PubMed:11384984, PubMed:26138980, PubMed:29775578, PubMed:29779948, PubMed:9122164,…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7PLO | EM | 2.8 Å | S=1-745 |
| 9EFQ | EM | 2.96 Å | J=1-745 |
| 4WQO | X-ray | 3.2 Å | D=1-163 |
| 8JAU | EM | 3.22 Å | E/I=2-745 |
| 8JAQ | EM | 3.26 Å | E/I/L/U=2-745 |
| 8WQF | EM | 3.27 Å | A/B=2-745 |
| 9UA3 | EM | 3.28 Å | B/F=2-745 |
| 8JAL | EM | 3.3 Å | E/I=2-745 |
| 8JAR | EM | 3.3 Å | E/I=2-745 |
| 8WQB | EM | 3.37 Å | A/B=2-745 |
| 8WQE | EM | 3.38 Å | A/C=2-745 |
| 8WQA | EM | 3.39 Å | A/C=2-745 |
| 8JAV | EM | 3.44 Å | E/I/L/U=2-745 |
| 8R5H | EM | 3.44 Å | A=1-745 |
| 8WQH | EM | 3.44 Å | A/C=2-745 |
| 8QU8 | EM | 3.5 Å | D=2-745 |
| 8JAS | EM | 3.54 Å | E/I/L/U=2-745 |
| 8WQC | EM | 3.54 Å | C/E=2-745 |
| 9J77 | EM | 3.56 Å | A/B=2-744 |
| 8JE2 | EM | 3.63 Å | A=1-745 |
Showing 20 of 42 experimental structures (best resolution first).
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