Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PPP1CA) is a 330-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P62136.
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The mean pLDDT of this model is 91.3 (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 | 86% |
| 70 to 90 | Confident: backbone generally right | 2% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 10% |
What pLDDT means and how to read it
Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets (PubMed:28216226, PubMed:30158517, PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670, PubMed:39603239, PubMed:39603240). Protein phosphatase 1 (PP1) is essential for cell division, transcription elongation, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670, PubMed:39603239, PubMed:39603240). Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in…
PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting or regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen.…
Cytoplasm, Nucleus, Nucleus, nucleoplasm, Nucleus, nucleolus, Postsynaptic density
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6ZEG | X-ray | 1.09 Å | A/B=7-304 |
| 6ZEH | X-ray | 1.3 Å | A/B=7-304 |
| 6ZEI | X-ray | 1.39 Å | A/B=7-304 |
| 4MOV | X-ray | 1.45 Å | A/B=7-300 |
| 6DNO | X-ray | 1.45 Å | A=7-300 |
| 6OBR | X-ray | 1.5 Å | A/B=7-300 |
| 3E7A | X-ray | 1.63 Å | A/B=7-300 |
| 3E7B | X-ray | 1.7 Å | A/B=7-300 |
| 8SW6 | X-ray | 1.76 Å | A/B=7-300 |
| 6ZEJ | X-ray | 1.78 Å | A/D/F/I/L/O=7-304 |
| 6OBS | X-ray | 1.8 Å | A/B=7-300 |
| 7T0Y | X-ray | 1.8 Å | A/C=7-300 |
| 6OBQ | X-ray | 1.84 Å | A/B=7-300 |
| 3EGG | X-ray | 1.85 Å | A/B=7-330 |
| 6ZEE | X-ray | 1.9 Å | A/B/I/K/P/Q=7-300 |
| 6ZK6 | X-ray | 1.9 Å | A=1-330 |
| 6ZEF | X-ray | 1.94 Å | A/B=7-300 |
| 6OBU | X-ray | 1.95 Å | A/B=7-300 |
| 7TXH | X-ray | 1.95 Å | C/F=7-300 |
| 3EGH | X-ray | 2.0 Å | A/B=7-330 |
Showing 20 of 46 experimental structures (best resolution first).
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