Sentrin-specific protease 2 (SENP2) is a 589-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9HC62.
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The mean pLDDT of this model is 62.1 (low 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 | 37% |
| 70 to 90 | Confident: backbone generally right | 4% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 51% |
What pLDDT means and how to read it
Protease that catalyzes two essential functions in the SUMO pathway (PubMed:11896061, PubMed:12192048, PubMed:15296745, PubMed:20194620, PubMed:21965678). The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins (PubMed:15296745). The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein (PubMed:15296745, PubMed:20194620, PubMed:21965678). May down-regulate CTNNB1 levels…
Binds to SUMO2 and SUMO3 (PubMed:15296745). Interacts with the C-terminal domain of NUP153 via its N-terminus (PubMed:11896061, PubMed:12192048). Interacts with MTA1 (PubMed:21965678)
Nucleus, nuclear pore complex, Nucleus membrane, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3ZO5 | X-ray | 2.15 Å | A=363-589 |
| 1TH0 | X-ray | 2.2 Å | A/B=364-589 |
| 2IO0 | X-ray | 2.3 Å | A=364-589 |
| 2IO1 | X-ray | 2.6 Å | A/C/E=364-589 |
| 1TGZ | X-ray | 2.8 Å | A=364-589 |
| 2IO2 | X-ray | 2.9 Å | A=364-589 |
| 5AEK | X-ray | 3.0 Å | A/C/E/G/I/K/M/O/Q/S/U/W=366-589 |
| 2IO3 | X-ray | 3.2 Å | A=364-589 |
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