O00459: Phosphatidylinositol 3-kinase regulatory subunit beta (PIK3R2)

Phosphatidylinositol 3-kinase regulatory subunit beta (PIK3R2) is a 728-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O00459.

Gene
PIK3R2
Organism
Homo sapiens
Length
728 residues
Mean pLDDT
81.6
Model
AF-O00459-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.6 (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 accurate41%
70 to 90Confident: backbone generally right42%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions12%

What pLDDT means and how to read it

Function

Regulatory subunit of phosphoinositide-3-kinase (PI3K), a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Indirectly regulates autophagy (PubMed:23604317). Promotes nuclear translocation of XBP1 isoform…

Subunit structure

Heterodimer of a regulatory subunit PIK3R2 and a p110 catalytic subunit (PIK3CA, PIK3CB or PIK3CD) (PubMed:23604317). Interacts with AXL (PubMed:9178760). Interacts with FLT1 (tyrosine-phosphorylated) and FLT4 (tyrosine-phosphorylated) (PubMed:15102829, PubMed:9600074). Interacts with NYAP1, NYAP2 and MYO16 (By similarity). Interacts with FBXL2; PIK3R2 is a substrate of the SCF(FBXL2) complex…

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7RNUX-ray1.45 ÅA/C/E/G=318-428
3O5ZX-ray2.01 ÅA/B=1-85
2XS6X-ray2.09 ÅA=108-298
6OX7X-ray2.75 ÅC/D=435-597
6U28X-ray2.95 ÅC/D=435-597
7RCHX-ray3.1 ÅC/D=435-597
3MTTX-ray3.3 ÅA=433-610
2KT1NMRA=1-80

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