Procathepsin L (CTSL) is a 333-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P07711.
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The mean pLDDT of this model is 93.5 (very high 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 | 88% |
| 70 to 90 | Confident: backbone generally right | 6% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (By similarity). In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter (By similarity). In thymus, regulates CD4(+) T cell positive selection by generating the major histocompatibility…
Dimer of a heavy and a light chain linked by disulfide bonds. Interacts with Long isoform of CD74/Ii chain; the interaction stabilizes the conformation of mature CTSL
Lysosome, Apical cell membrane, Cytoplasmic vesicle, secretory vesicle, chromaffin granule, Secreted, extracellular space, Secreted, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2XU3 | X-ray | 0.9 Å | A=114-333 |
| 5MAE | X-ray | 1.0 Å | A=114-333 |
| 5MAJ | X-ray | 1.0 Å | A=114-333 |
| 2XU4 | X-ray | 1.12 Å | A=114-333 |
| 5MQY | X-ray | 1.13 Å | A=114-333 |
| 2YJC | X-ray | 1.14 Å | A=114-333 |
| 2YJ2 | X-ray | 1.15 Å | A=114-333 |
| 3HHA | X-ray | 1.27 Å | A/B/C/D=114-333 |
| 2YJ8 | X-ray | 1.3 Å | A=114-333 |
| 2YJ9 | X-ray | 1.35 Å | A=114-333 |
| 7Z58 | X-ray | 1.35 Å | A/B/C/D=114-333 |
| 6EZP | X-ray | 1.37 Å | A=114-333 |
| 2YJB | X-ray | 1.4 Å | A=114-333 |
| 8A4W | X-ray | 1.4 Å | A/B/C/D=114-333 |
| 8UAC | X-ray | 1.4 Å | A/B=114-333 |
| 5I4H | X-ray | 1.42 Å | A=113-218, B=222-333 |
| 5F02 | X-ray | 1.43 Å | A=114-333 |
| 2XU1 | X-ray | 1.45 Å | A/B/C/D=114-333 |
| 6JD8 | X-ray | 1.46 Å | A=18-333 |
| 2VHS | X-ray | 1.5 Å | A/B/C/D=114-333 |
Showing 20 of 64 experimental structures (best resolution first).
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