Urokinase plasminogen activator surface receptor (PLAUR) is a 335-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q03405.
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The mean pLDDT of this model is 81.4 (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 | 61% |
| 70 to 90 | Confident: backbone generally right | 15% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 18% |
What pLDDT means and how to read it
GPI-anchored receptor that recruits and activates the urokinase-type plasminogen activator (uPA) at the cell surface. Activated uPA converts plasminogen into plasmin, initiating extracellular matrix degradation and remodeling (PubMed:1689240, PubMed:15677461). Also binds the extracellular matrix protein vitronectin, promoting cell-matrix adhesion and indirectly integrin signaling (PubMed:17548516, PubMed:25168639, PubMed:28849762). This dual interaction coordinates dynamic changes in cell migration, proliferation, and tissue remodeling (PubMed:28849762)
Monomer (Probable). Interacts with MRC2. Interacts (via the UPAR/Ly6 domains) with SRPX2. Interacts with FAP (seprase); the interaction occurs at the cell surface of invadopodia membrane. Interacts with SORL1 (via N-terminal ectodomain); this interaction decreases PLAUR internalization (PubMed:14764453, PubMed:23486467). The ternary complex composed of PLAUR-PLAU-SERPINE1 also interacts with…
Cell membrane, Cell projection, invadopodium membrane, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2FD6 | X-ray | 1.9 Å | U=23-297 |
| 3U74 | X-ray | 2.39 Å | U=23-305 |
| 3BT2 | X-ray | 2.5 Å | U=23-303 |
| 1YWH | X-ray | 2.7 Å | A/C/E/G/I/K/M/O=23-335 |
| 2I9B | X-ray | 2.8 Å | E/F/G/H=23-299 |
| 3BT1 | X-ray | 2.8 Å | U=23-303 |
| 7V63 | X-ray | 2.91 Å | A/B=23-299 |
| 9YC5 | EM | 2.94 Å | A=23-305 |
| 7E17 | X-ray | 2.96 Å | A/B=23-299 |
| 4QTI | X-ray | 3.0 Å | U=23-305 |
| 3U73 | X-ray | 3.19 Å | U=23-305 |
| 4K24 | X-ray | 4.5 Å | U=23-303 |
| 9YC6 | EM | 4.8 Å | U=23-305 |
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