Subtilisin Carlsberg (subC) is a 379-residue protein from Bacillus licheniformis. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P00780.
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The mean pLDDT of this model is 91.2 (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 | 86% |
| 70 to 90 | Confident: backbone generally right | 3% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 9% |
What pLDDT means and how to read it
Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides (PubMed:11109488, Ref.4). Shows high specificity for aromatic and hydrophobic amino acids in the P1 substrate position (PubMed:11109488). May play an important role in the degradation of feather keratin (PubMed:11109488)
Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1R0R | X-ray | 1.1 Å | E=106-379 |
| 1CSE | X-ray | 1.2 Å | E=106-379 |
| 3UNX | X-ray | 1.26 Å | A=106-379 |
| 6DWQ | X-ray | 1.27 Å | A=106-379 |
| 1YU6 | X-ray | 1.55 Å | A/B=105-379 |
| 2SEC | X-ray | 1.8 Å | E=106-379 |
| 1SCN | X-ray | 1.9 Å | E=106-379 |
| 1AVT | X-ray | 2.0 Å | A=106-379 |
| 1SCA | X-ray | 2.0 Å | A=106-379 |
| 1SEL | X-ray | 2.0 Å | A/B=106-379 |
| 1VSB | X-ray | 2.1 Å | A=106-379 |
| 1BE6 | X-ray | 2.15 Å | A=106-379 |
| 1C3L | X-ray | 2.16 Å | A=106-379 |
| 1BE8 | X-ray | 2.2 Å | A=106-379 |
| 1BFU | X-ray | 2.2 Å | A=106-379 |
| 2WUW | X-ray | 2.23 Å | E=106-379 |
| 2WUV | X-ray | 2.24 Å | A=106-379 |
| 4C3V | X-ray | 2.26 Å | A=106-379 |
| 4C3U | X-ray | 2.29 Å | A=106-379 |
| 1BFK | X-ray | 2.3 Å | A=106-379 |
Showing 20 of 27 experimental structures (best resolution first).
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