Phosphatidylinositol 3-kinase catalytic subunit type 3 (PIK3C3) is a 887-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8NEB9.
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The mean pLDDT of this model is 83.4 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 52% |
| 70 to 90 | Confident: backbone generally right | 33% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 8% |
What pLDDT means and how to read it
Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis (PubMed:14617358, PubMed:33637724, PubMed:7628435, PubMed:33993848). As part of PI3KC3-C1, promotes endoplasmic reticulum membrane curvature formation prior to vesicle budding (PubMed:32690950). Involved in regulation of degradative endocytic trafficking and required for the abscission step in cytokinesis, probably in the context of PI3KC3-C2 (PubMed:20208530, PubMed:20643123).…
Component of the PI3K (PI3KC3/PI3K-III/class III phosphatidylinositol 3-kinase) complex the core of which is composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4 and BECN1 associating with additional regulatory/auxiliary subunits to form alternative complex forms. Alternative complex forms containing a fourth regulatory subunit in a mutually exclusive manner are: the PI3K…
Midbody, Late endosome, Cytoplasmic vesicle, autophagosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6HOG | X-ray | 1.26 Å | A=244-258 |
| 7RSP | X-ray | 1.67 Å | A/B=282-879 |
| 7RSV | X-ray | 1.78 Å | A/B=282-879 |
| 7RSJ | X-ray | 1.88 Å | A=282-879 |
| 4UWH | X-ray | 1.93 Å | A=282-879 |
| 9NIN | X-ray | 2.01 Å | A=290-871 |
| 8RXR | X-ray | 2.06 Å | A/B=282-879 |
| 9ORM | X-ray | 2.06 Å | A=290-871 |
| 6I3U | X-ray | 2.09 Å | A=268-879 |
| 9ZF4 | X-ray | 2.09 Å | A=290-871 |
| 9DKP | X-ray | 2.16 Å | B=290-871 |
| 3LS8 | X-ray | 2.25 Å | A/B=268-879 |
| 6HOH | X-ray | 2.25 Å | A/B/C/D=244-258 |
| 9E4V | X-ray | 2.36 Å | B=290-871 |
| 11YC | X-ray | 2.41 Å | B=290-871 |
| 11MM | X-ray | 2.69 Å | A=290-871 |
| 4UWG | X-ray | 2.7 Å | A=282-879 |
| 5ANL | X-ray | 2.7 Å | A=282-879 |
| 5ENN | X-ray | 2.7 Å | A/B=293-887 |
| 9MHF | EM | 2.73 Å | B=1-887 |
Showing 20 of 34 experimental structures (best resolution first).
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