Calmodulin-1 (Calm1) is a 149-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P0DP29.
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The mean pLDDT of this model is 85.0 (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 | 41% |
| 70 to 90 | Confident: backbone generally right | 49% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding (By similarity). Calcium-binding is required for the activation of calmodulin (By similarity). Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin-dependent protein kinase type II (CaMK2), and phosphatases (By similarity). Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (By similarity). Is a regulator of…
Homotetramer (By similarity). Component of the SIFI complex, which is a dimer of 2 heterotrimers, comprising two copies each of UBR4, KCMF1 and calmodulin (CALM1, CALM2 or CALM3) (By similarity). Component of the NALCN channelosome complex; within the complex interacts with NALCN (By similarity). Interacts with CEP97, CCP110, TTN/titin and SRY (By similarity). Interacts with MYO5A and RRAD…
Cytoplasm, cytoskeleton, spindle, Cytoplasm, cytoskeleton, spindle pole, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Cell projection, cilium, flagellum
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2PQ3 | X-ray | 1.3 Å | A=2-77 |
| 4J9Y | X-ray | 1.51 Å | R=1-149 |
| 1G4Y | X-ray | 1.6 Å | R=2-149 |
| 3B32 | X-ray | 1.6 Å | A=2-76 |
| 4G28 | X-ray | 1.63 Å | R=1-149 |
| 4G27 | X-ray | 1.65 Å | R=1-149 |
| 4J9Z | X-ray | 1.66 Å | R=1-149 |
| 3SG6 | X-ray | 1.7 Å | A=3-149 |
| 9M6G | X-ray | 1.7 Å | B=1-149 |
| 3EVU | X-ray | 1.75 Å | A=3-148 |
| 9KYS | X-ray | 1.76 Å | A/C=1-149 |
| 6MBA | X-ray | 1.8 Å | B=1-149 |
| 9M5Y | X-ray | 1.8 Å | B=1-149 |
| 9U9D | X-ray | 1.8 Å | A=3-149 |
| 3EK7 | X-ray | 1.85 Å | A=3-149 |
| 1UP5 | X-ray | 1.9 Å | A/B=2-149 |
| 2HQW | X-ray | 1.9 Å | A=2-149 |
| 3SG5 | X-ray | 1.9 Å | A=3-149 |
| 3SG7 | X-ray | 1.9 Å | A=3-149 |
| 3SJQ | X-ray | 1.9 Å | A/B=1-149 |
Showing 20 of 59 experimental structures (best resolution first).
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