Chymotrypsinogen A is a 245-residue protein from Bos taurus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P00766.
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The mean pLDDT of this model is 93.6 (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 | 84% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
Secreted, extracellular space
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5R43 | X-ray | 1.0 Å | A=1-13, B=16-146, C=149-245 |
| 5R42 | X-ray | 1.05 Å | A=1-13, B=16-146, C=149-245 |
| 5R44 | X-ray | 1.05 Å | A=1-13, B=16-146, C=149-245 |
| 5R45 | X-ray | 1.05 Å | A=1-13, B=16-146, C=149-245 |
| 5R46 | X-ray | 1.05 Å | A=1-13, B=16-146, C=149-245 |
| 5R48 | X-ray | 1.05 Å | A=1-13, B=16-146, C=149-245 |
| 5R49 | X-ray | 1.05 Å | A=1-13, B=16-146, C=149-245 |
| 5R4B | X-ray | 1.05 Å | A=1-13, B=16-146, C=149-245 |
| 5R4D | X-ray | 1.05 Å | A=1-13, B=16-146, C=149-245 |
| 5R47 | X-ray | 1.1 Å | A=1-13, B=16-146, C=149-245 |
| 5R4C | X-ray | 1.15 Å | A=1-13, B=16-146, C=149-245 |
| 5R4A | X-ray | 1.2 Å | A=1-13, B=16-146, C=149-245 |
| 1YPH | X-ray | 1.34 Å | A/B=1-13, C/D=16-146, E/F=149-245 |
| 1GG6 | X-ray | 1.4 Å | A=1-10, B=16-146, C=149-245 |
| 1GGD | X-ray | 1.5 Å | A=1-10, B=16-146, C=149-245 |
| 2P8O | X-ray | 1.5 Å | A=1-13, B=16-146, C=149-245 |
| 1AB9 | X-ray | 1.6 Å | A=1-13, B=16-146, C=149-245 |
| 1GCT | X-ray | 1.6 Å | A=1-13, B=16-146, C=149-245 |
| 3GCT | X-ray | 1.6 Å | E=1-13, F=16-146, G=149-245 |
| 8GCH | X-ray | 1.6 Å | E=1-13, F=16-146, G=149-245 |
Showing 20 of 89 experimental structures (best resolution first).
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