Catenin beta-1 (CTNNB1) is a 781-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P35222.
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The mean pLDDT of this model is 81.1 (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 | 63% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 19% |
What pLDDT means and how to read it
Key downstream component of the canonical Wnt signaling pathway (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for…
Two separate complex-associated pools are found in the cytoplasm. The majority is present as component of an E-cadherin:catenin adhesion complex composed of at least E-cadherin/CDH1 and beta-catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in…
Cytoplasm, Nucleus, Cytoplasm, cytoskeleton, Cell junction, adherens junction, Cell junction, Cell membrane, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Cytoplasm, cytoskeleton, spindle pole, Synapse, Cytoplasm, cytoskeleton, cilium basal body
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3FQN | X-ray | 1.65 Å | C=30-39 |
| 3FQR | X-ray | 1.7 Å | C=30-39 |
| 7AFW | X-ray | 1.81 Å | A=141-305 |
| 1JDH | X-ray | 1.9 Å | A=135-663 |
| 8RU3 | X-ray | 2.0 Å | A=134-665 |
| 9I8K | X-ray | 2.0 Å | A/B=150-663 |
| 9I8X | X-ray | 2.0 Å | A=134-671 |
| 6M90 | X-ray | 2.05 Å | C=17-48 |
| 1G3J | X-ray | 2.1 Å | A/C=133-664 |
| 1T08 | X-ray | 2.1 Å | A=146-664 |
| 3DIW | X-ray | 2.1 Å | C/D=772-781 |
| 8RU4 | X-ray | 2.13 Å | A/B=145-665 |
| 1QZ7 | X-ray | 2.2 Å | A=133-665 |
| 2Z6H | X-ray | 2.2 Å | A=138-781 |
| 3SL9 | X-ray | 2.2 Å | A/B/E/G=141-305 |
| 6O9B | X-ray | 2.2 Å | C=41-49 |
| 6WLX | X-ray | 2.2 Å | B=671-677 |
| 9I8W | X-ray | 2.2 Å | A=134-671 |
| 8Z0U | X-ray | 2.21 Å | A=138-686 |
| 8VME | X-ray | 2.3 Å | C=35-61 |
Showing 20 of 50 experimental structures (best resolution first).
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