Urokinase-type plasminogen activator (PLAU) is a 431-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P00749.
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The mean pLDDT of this model is 82.1 (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 | 54% |
| 70 to 90 | Confident: backbone generally right | 26% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 12% |
What pLDDT means and how to read it
Serine protease that cleaves the inactive precursor plasminogen at a specific Arg-Val peptide bond, converting it into active plasmin (PubMed:1969415, PubMed:2521625, PubMed:4270330). Secreted as an inactive zymogen, it is recruited and activated at the cell surface through interaction with the urokinase plasminogen activator receptor (uPAR). Cell-surface activation enables localized, plasmin-dependent pericellular proteolysis, regulating extracellular matrix degradation in cell migration and tissue remodeling (PubMed:1829461, PubMed:2521625, PubMed:28849762). Also contributes to fibrinolysis and blood clot clearance by promoting plasmin generation (By similarity)
Found in high and low molecular mass forms. Each consists of two chains, A and B. The high molecular mass form contains a long chain A which is cleaved to yield a short chain A. Forms heterodimer with SERPINA5. Binds LRP1B; binding is followed by internalization and degradation. Interacts with MRC2. Interacts with PLAUR. In complex with SERPINE1, interacts with PLAUR/uPAR (PubMed:15053742).…
Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5YC6 | X-ray | 1.18 Å | U=179-424 |
| 4ZKO | X-ray | 1.29 Å | U=179-425 |
| 4ZKN | X-ray | 1.36 Å | U=179-425 |
| 4ZKR | X-ray | 1.36 Å | U=179-425 |
| 6XVD | X-ray | 1.4 Å | U=179-431 |
| 2O8T | X-ray | 1.45 Å | A=179-431 |
| 3MHW | X-ray | 1.45 Å | U=179-425 |
| 5Z1C | X-ray | 1.45 Å | U=179-423 |
| 5WXF | X-ray | 1.46 Å | U=179-431 |
| 4MNW | X-ray | 1.49 Å | A=179-423 |
| 1GJ7 | X-ray | 1.5 Å | A=156-178, B=179-431 |
| 4XSK | X-ray | 1.5 Å | U=179-424 |
| 4GLY | X-ray | 1.52 Å | A=179-423 |
| 4JK5 | X-ray | 1.55 Å | A=179-423 |
| 1GJA | X-ray | 1.56 Å | A=156-178, B=179-431 |
| 3OX7 | X-ray | 1.58 Å | U=179-431 |
| 1OWE | X-ray | 1.6 Å | A=179-423 |
| 4FU9 | X-ray | 1.6 Å | A=179-424 |
| 4FUH | X-ray | 1.6 Å | A=179-424 |
| 4X1P | X-ray | 1.6 Å | U=179-425 |
Showing 20 of 156 experimental structures (best resolution first).
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