Calcium/calmodulin-dependent protein kinase type II subunit alpha (CAMK2A) is a 478-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UQM7.
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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 | 62% |
| 70 to 90 | Confident: backbone generally right | 25% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 8% |
What pLDDT means and how to read it
Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in various processes, such as synaptic plasticity, neurotransmitter release and long-term potentiation (PubMed:14722083). Member of the NMDAR signaling complex in excitatory synapses, it regulates NMDAR-dependent potentiation of the AMPAR and therefore excitatory synaptic transmission (By similarity). Regulates dendritic spine development (PubMed:28130356). Also regulates the migration of developing neurons (PubMed:29100089). Phosphorylates the transcription factor FOXO3 to activate its transcriptional activity (PubMed:23805378). Phosphorylates…
There are 4 genes encoding calcium/calmodulin-dependent protein kinase type II chains: CAMK2A, CAMK2B, CAMK2G and CAMK2D. The corresponding proteins assemble into homo- or heteromultimeric holoenzymes composed of 12 subunits with two hexameric rings stacked one on top of the other (PubMed:14722083, PubMed:29784083). Interacts with BAALC. Interacts with MPDZ. Interacts with SYN1. Interacts with…
Synapse, Postsynaptic density, Cell projection, dendritic spine, Cell projection, dendrite
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6X5G | X-ray | 1.85 Å | A=7-274 |
| 7UJR | X-ray | 1.95 Å | A=7-274 |
| 6OF8 | X-ray | 2.1 Å | A/B/C/D/E/F/G=345-475 |
| 7UJT | X-ray | 2.1 Å | A=7-274 |
| 9EOY | X-ray | 2.1 Å | A/B/C/D/E/F/G=345-475 |
| 6X5Q | X-ray | 2.14 Å | A=7-274 |
| 7REC | X-ray | 2.2 Å | A/B/C/D/E/F/G=345-475 |
| 7UJQ | X-ray | 2.25 Å | A/B=7-274 |
| 2VZ6 | X-ray | 2.3 Å | A/B=9-302 |
| 7KL0 | X-ray | 2.4 Å | A/B=7-274 |
| 7KL1 | X-ray | 2.4 Å | A/B=7-274 |
| 6VZK | X-ray | 2.55 Å | A=7-274 |
| 7KL2 | X-ray | 2.56 Å | A=7-274 |
| 7UJP | X-ray | 2.56 Å | A/B=7-274 |
| 7UIS | X-ray | 2.58 Å | A=7-274 |
| 5IG3 | X-ray | 2.75 Å | A/B/C/D/E/F=345-475 |
| 7UJS | X-ray | 2.75 Å | A=7-274 |
| 7UIR | X-ray | 3.1 Å | A/B=7-274 |
| 7UIQ | X-ray | 3.11 Å | A/B=7-274 |
| 3SOA | X-ray | 3.55 Å | A=1-474 |
Showing 20 of 22 experimental structures (best resolution first).
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