cAMP-dependent protein kinase catalytic subunit alpha (Prkaca) is a 351-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P05132.
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The mean pLDDT of this model is 95.4 (very high 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 | 94% |
| 70 to 90 | Confident: backbone generally right | 3% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
Phosphorylates a large number of substrates in the cytoplasm and the nucleus (By similarity). Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, histone H1.4 (H1-4), PSMC5/RPT6, PJA2, RYR2, RORA, SLC6A6, SOX9, UHRF1 and VASP (PubMed:10805756, PubMed:19223768). Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis (By similarity). RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts (By similarity). Involved in chondrogenesis by mediating…
A number of inactive tetrameric holoenzymes are produced by the combination of homo- or heterodimers of the different regulatory subunits associated with two catalytic subunits. Protein kinase A holoenzyme is comprised of two catalytic (C) and two regulatory (R) subunits which keep the enzyme in an inhibited state before activation by cyclic-AMP. cAMP causes the dissociation of the inactive…
Cytoplasm, Cell membrane, Nucleus, Mitochondrion, Membrane, Cell projection, cilium, flagellum, Cytoplasmic vesicle, secretory vesicle, acrosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1RDQ | X-ray | 1.26 Å | E=2-351 |
| 4DFX | X-ray | 1.35 Å | E=2-351 |
| 4HPU | X-ray | 1.55 Å | E=2-351 |
| 4IAI | X-ray | 1.55 Å | A=2-351 |
| 3FJQ | X-ray | 1.6 Å | E=2-351 |
| 4IAK | X-ray | 1.6 Å | A=2-351 |
| 3IDB | X-ray | 1.62 Å | A=2-351 |
| 4IB1 | X-ray | 1.63 Å | A=2-351 |
| 7V0G | X-ray | 1.63 Å | E=2-351 |
| 3QAL | X-ray | 1.7 Å | E=2-351 |
| 3X2W | X-ray | 1.7 Å | A=1-351 |
| 4O22 | X-ray | 1.7 Å | A=16-351 |
| 3X2V | X-ray | 1.77 Å | A=1-351 |
| 4DG3 | X-ray | 1.8 Å | E=1-351 |
| 4DH7 | X-ray | 1.8 Å | A=2-351 |
| 4XW4 | X-ray | 1.82 Å | A=15-351 |
| 4IAZ | X-ray | 1.85 Å | A=2-351 |
| 6MM7 | X-ray | 1.85 Å | A/D=16-351 |
| 6MM8 | X-ray | 1.85 Å | C=16-351 |
| 4IB0 | X-ray | 1.87 Å | A=2-351 |
Showing 20 of 85 experimental structures (best resolution first).
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