P0DP31: Calmodulin-3 (Calm3)

Calmodulin-3 (Calm3) is a 149-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P0DP31.

Gene
Calm3
Organism
Rattus norvegicus
Length
149 residues
Mean pLDDT
84.8
Model
AF-P0DP31-F1 v6
Model created
1 Aug 2025
PDB structures
17

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Model confidence (pLDDT)

The mean pLDDT of this model is 84.8 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate40%
70 to 90Confident: backbone generally right50%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions3%

What pLDDT means and how to read it

Function

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. Calcium-binding is required for the activation of calmodulin. 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. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis

Subunit structure

Interacts with CEP97, CCP110, TTN/titin and SRY (By similarity). Interacts with MYO5A and RRAD (PubMed:18056528). Interacts with USP6; the interaction is calcium dependent (By similarity). Interacts with CDK5RAP2 (By similarity). Interacts with SCN5A (By similarity). Interacts with RYR1 (By similarity). Interacts with FCHO1 (By similarity). Interacts with MIP in a 1:2 stoichiometry; the…

Subcellular location

Cytoplasm, cytoskeleton, spindle, Cytoplasm, cytoskeleton, spindle pole

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
3SG6X-ray1.7 ÅA=3-149
3EVUX-ray1.75 ÅA=3-148
3EK7X-ray1.85 ÅA=3-149
1UP5X-ray1.9 ÅA/B=2-149
3SG5X-ray1.9 ÅA=3-149
3SG7X-ray1.9 ÅA=3-149
3EKHX-ray2.0 ÅA=3-149
3SG2X-ray2.0 ÅA=3-149
3SG3X-ray2.1 ÅA=3-149
4I2YX-ray2.2 ÅA/B=3-149
3SG4X-ray2.4 ÅA=3-149
3WLCX-ray2.49 ÅA=3-149
3EVVX-ray2.6 ÅA=46-149
3EK4X-ray2.65 ÅA=3-149
3WLDX-ray2.7 ÅA=3-149
3EK8X-ray2.8 ÅA=3-149
3EKJX-ray2.8 ÅA=3-149

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