Cerebral cavernous malformations 2 protein (CCM2) is a 444-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9BSQ5.
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The mean pLDDT of this model is 66.5 (low 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 | 23% |
| 70 to 90 | Confident: backbone generally right | 28% |
| 50 to 70 | Low: treat with caution | 15% |
| Below 50 | Very low: often disordered regions | 34% |
What pLDDT means and how to read it
Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May act through the stabilization of endothelial cell junctions (By similarity). May function as a scaffold protein for MAP2K3-MAP3K3 signaling. Seems to play a major role in the modulation of MAP3K3-dependent p38 activation induced by hyperosmotic shock (By similarity)
Part of a complex with MAP2K3, MAP3K3 and RAC1. Binds RAC1 directly and independently of its nucleotide-bound state (By similarity). Interacts with HEG1 and KRIT1; KRIT1 greatly facilitates the interaction with HEG1 (By similarity). Interacts with PDCD10
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4FQN | X-ray | 1.9 Å | A/B/C/D=283-379 |
| 4YKD | X-ray | 1.93 Å | A=290-376 |
| 4YL6 | X-ray | 2.1 Å | A=290-376 |
| 4Y5O | X-ray | 2.35 Å | A=283-379 |
| 4YKC | X-ray | 2.7 Å | A=290-444 |
| 4WJ7 | X-ray | 2.75 Å | A/B/C/D=51-228 |
| 4TVQ | X-ray | 2.8 Å | E=224-239 |
| 9PVG | X-ray | 3.0 Å | A/B/C/D=51-228 |
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