Plasminogen (PLG) is a 810-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P00747.
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The mean pLDDT of this model is 82.8 (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 | 45% |
| 70 to 90 | Confident: backbone generally right | 39% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 9% |
What pLDDT means and how to read it
Protease which primary function is to degrade fibrin, the main component of blood clots (PubMed:6094526, PubMed:6919539). Also cleaves other components of blood clots like thrombospondin-1/THBS1 and von Willebrand factor (VWF) (PubMed:24449821, PubMed:7679575). Can also directly and/or through the activation of other proteases degrade the various components of the extracellular matrix including collagen, fibronectin and laminin (PubMed:14699093, PubMed:28849762, PubMed:9171346). Thereby, regulates a variety of biological processes including embryonic development, tissue remodeling, and inflammation (PubMed:9171346). In ovulation, weakens the walls of the Graafian follicle (By similarity).…
The active form of plasmin is a two-chain monomeric protein, not oligomerized, consisting of a heavy chain (A) and a light chain (B) that are covalently linked by disulfide bonds. Interacts with CSPG4; enhances the activation of plasminogen by urokinase-type (PLAU) plasminogen activator (PubMed:10889192). Interacts with AMOT (PubMed:16043488). Interacts (via the Kringle domains) with HRG; the…
Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5UGG | X-ray | 1.2 Å | A=562-810 |
| 6D3Y | X-ray | 1.32 Å | A=564-810 |
| 5UGD | X-ray | 1.38 Å | A=562-810 |
| 6D40 | X-ray | 1.43 Å | A=563-810 |
| 8F7U | X-ray | 1.47 Å | A/B=561-810 |
| 7UAH | X-ray | 1.57 Å | A/B=561-810 |
| 8F7V | X-ray | 1.65 Å | A/B=561-810 |
| 5HPG | X-ray | 1.66 Å | A/B=480-563 |
| 1KRN | X-ray | 1.67 Å | A=374-461 |
| 6OG4 | X-ray | 1.7 Å | A/B=183-264 |
| 1KI0 | X-ray | 1.75 Å | A=100-352 |
| 4CIK | X-ray | 1.78 Å | A=101-181 |
| 6D3X | X-ray | 1.8 Å | A/B=565-810 |
| 7THS | X-ray | 1.8 Å | A/B=561-810 |
| 1PK4 | X-ray | 1.9 Å | A=376-454 |
| 7E50 | X-ray | 1.95 Å | B=564-810 |
| 1DDJ | X-ray | 2.0 Å | A/B/C/D=564-810 |
| 1QRZ | X-ray | 2.0 Å | A/B/C/D=565-810 |
| 6D3Z | X-ray | 2.0 Å | A=565-810 |
| 4DCB | X-ray | 2.03 Å | F=576-585 |
Showing 20 of 49 experimental structures (best resolution first).
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