Transmembrane protease serine 2 (TMPRSS2) is a 492-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O15393.
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The mean pLDDT of this model is 79.4 (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 | 50% |
| 70 to 90 | Confident: backbone generally right | 27% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 17% |
What pLDDT means and how to read it
Plasma membrane-anchored serine protease that cleaves at arginine residues (PubMed:32703818, PubMed:35676539, PubMed:37990007, PubMed:38964328). Participates in proteolytic cascades of relevance for the normal physiologic function of the prostate (PubMed:25122198). Androgen-induced TMPRSS2 activates several substrates that include pro-hepatocyte growth factor/HGF, the protease activated receptor-2/F2RL1 or matriptase/ST14 leading to extracellular matrix disruption and metastasis of prostate cancer cells (PubMed:15537383, PubMed:25122198, PubMed:26018085). In addition, activates trigeminal neurons and contribute to both spontaneous pain and mechanical allodynia (By similarity)
The catalytically active form interacts with ACE2
Cell membrane, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8V04 | X-ray | 1.58 Å | A=148-255, B=256-492 |
| 8S0L | X-ray | 1.8 Å | A=107-492 |
| 9JD1 | X-ray | 1.9 Å | C=109-254, D=256-492 |
| 7MEQ | X-ray | 1.95 Å | A=109-492 |
| 9JD0 | X-ray | 2.0 Å | A/B=109-254, C/D=256-492 |
| 9U8G | X-ray | 2.0 Å | A/C=109-254, B/D=256-492 |
| 9E83 | X-ray | 2.07 Å | A=148-255, B=256-492 |
| 8V1F | X-ray | 2.19 Å | A/C=148-255, B/D=256-492 |
| 8S0N | X-ray | 2.3 Å | A/C=107-492 |
| 7Y0E | X-ray | 2.39 Å | A/B=109-254, C/D=256-492 |
| 8HD8 | X-ray | 2.4 Å | A/B=109-254, C/D=256-492 |
| 9IZN | X-ray | 2.4 Å | B=109-492 |
| 7XYD | X-ray | 2.58 Å | A/B=109-254, C/D=256-492 |
| 7Y0F | X-ray | 2.6 Å | A/B=109-254, C/D=256-492 |
| 8Y1D | EM | 2.7 Å | D/E=109-492 |
| 8Y1E | EM | 2.7 Å | D/E/F=109-492 |
| 9JCX | X-ray | 2.75 Å | A=109-254, C=256-492 |
| 8VGT | EM | 2.9 Å | B=109-492 |
| 8JI0 | EM | 3.0 Å | B=106-492 |
| 8Y8B | EM | 3.01 Å | C/T=109-492 |
Showing 20 of 31 experimental structures (best resolution first).
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