Gamma-secretase subunit PEN-2 (PSENEN) is a 101-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9NZ42.
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The mean pLDDT of this model is 92.6 (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 | 85% |
| 70 to 90 | Confident: backbone generally right | 13% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein) (PubMed:12522139, PubMed:12679784, PubMed:12740439, PubMed:12763021, PubMed:24941111, PubMed:30598546, PubMed:30630874). The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels (Probable). PSENEN modulates both endoproteolysis of presenilin and gamma-secretase activity (PubMed:12522139, PubMed:12679784, PubMed:12740439,…
The functional gamma-secretase complex is composed of at least four polypeptides: a presenilin homodimer (PSEN1 or PSEN2), nicastrin (NCSTN), APH1 (APH1A or APH1B) and PSENEN
Endoplasmic reticulum membrane, Golgi apparatus, Golgi stack membrane, Cell membrane, Membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8KCS | EM | 2.4 Å | D=1-101 |
| 6IYC | EM | 2.6 Å | D=1-101 |
| 7D8X | EM | 2.6 Å | D=2-101 |
| 8K8E | EM | 2.6 Å | D=1-101 |
| 8KCT | EM | 2.6 Å | D=1-101 |
| 6IDF | EM | 2.7 Å | D=1-101 |
| 8KCU | EM | 2.7 Å | D=1-101 |
| 8KCO | EM | 2.8 Å | D=1-101 |
| 7Y5T | EM | 2.9 Å | D=1-101 |
| 8X52 | EM | 2.9 Å | D=1-101 |
| 8X54 | EM | 2.9 Å | D=1-101 |
| 9K95 | EM | 2.9 Å | D=1-101 |
| 6LR4 | EM | 3.0 Å | D=2-101 |
| 7Y5X | EM | 3.0 Å | D=1-101 |
| 8KCP | EM | 3.0 Å | D=1-101 |
| 8X53 | EM | 3.0 Å | D=2-101 |
| 6LQG | EM | 3.1 Å | D=2-101 |
| 7C9I | EM | 3.1 Å | D=2-101 |
| 8OQY | EM | 3.3 Å | D=1-101 |
| 5A63 | EM | 3.4 Å | D=1-101 |
Showing 20 of 27 experimental structures (best resolution first).
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