Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha… (PPP2R1A) is a 589-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P30153.
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The mean pLDDT of this model is 94.9 (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 | 92% |
| 70 to 90 | Confident: backbone generally right | 7% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit (PubMed:15525651, PubMed:16580887, PubMed:33243860, PubMed:33633399, PubMed:34004147, PubMed:8694763). Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT (PubMed:15525651). Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis (PubMed:16580887). Together with RACK1 adapter, mediates dephosphorylation of AKT1 at 'Ser-473', preventing AKT1 activation and AKT-mTOR signaling pathway (By similarity). Dephosphorylation of AKT1 is essential for…
PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits (PubMed:38123684). Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and…
Cytoplasm, Nucleus, Chromosome, Chromosome, centromere, Lateral cell membrane, Cell projection, dendrite
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1B3U | X-ray | 2.3 Å | A/B=2-589 |
| 4I5L | X-ray | 2.43 Å | A/D=6-589 |
| 8TWE | EM | 2.55 Å | A=9-589 |
| 2IE4 | X-ray | 2.6 Å | A=1-589 |
| 9C6B | EM | 2.6 Å | A=9-589 |
| 8TWI | EM | 2.69 Å | A=9-589 |
| 8U1X | EM | 2.7 Å | A=1-589 |
| 9C7T | EM | 2.7 Å | A=9-589 |
| 8TTB | EM | 2.77 Å | A=9-589 |
| 2IE3 | X-ray | 2.8 Å | A=1-589 |
| 3C5W | X-ray | 2.8 Å | A=364-589 |
| 4I5N | X-ray | 2.8 Å | A/D=6-589 |
| 8SO0 | EM | 2.8 Å | A=9-589 |
| 4LAC | X-ray | 2.82 Å | A=366-589 |
| 3DW8 | X-ray | 2.85 Å | A/D=9-589 |
| 3K7V | X-ray | 2.85 Å | A=1-589 |
| 3K7W | X-ray | 2.96 Å | A=1-589 |
| 8RC4 | EM | 3.1 Å | p=1-589 |
| 8UWB | X-ray | 3.15 Å | C/F=439-505 |
| 9MZW | EM | 3.16 Å | A=9-589 |
Showing 20 of 41 experimental structures (best resolution first).
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