Q15257: Serine/threonine-protein phosphatase 2A activator (PTPA)

Serine/threonine-protein phosphatase 2A activator (PTPA) is a 358-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15257.

Gene
PTPA
Organism
Homo sapiens
Length
358 residues
Mean pLDDT
87.2
Model
AF-Q15257-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 87.2 (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 accurate77%
70 to 90Confident: backbone generally right6%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions15%

What pLDDT means and how to read it

Function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A) (PubMed:16916641, PubMed:36073231). Modulates PP2A activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase (PubMed:16916641). Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg(2+) (By similarity). Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence…

Subunit structure

Associates with PP2A heterodimeric core enzyme PP2A(D), composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A) (PubMed:16916641). Interacts with the catalytic subunit PPP2CA (via C-terminus) (PubMed:25003389). Interacts with PPP2CB (By similarity)

Subcellular location

Cytoplasm, Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2IXMX-ray1.5 ÅA=20-357
2G62X-ray1.6 ÅA=22-358
4NY3X-ray1.8 ÅA/B=22-358
2HV6X-ray1.9 ÅA/B=1-358
2HV7X-ray2.5 ÅA/B/C/D/E/F/G/H=1-358
4LACX-ray2.82 ÅB=19-358

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