Acetylcholinesterase (ache) is a 586-residue protein from Tetronarce californica. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P04058.
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The mean pLDDT of this model is 93.3 (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 | 90% |
| 70 to 90 | Confident: backbone generally right | 1% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 6% |
What pLDDT means and how to read it
Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions
Isoform H form is a homodimer; the asymmetric form is a disulfide-bonded oligomer composed of a collagenic subunit (Q) and a variable number of T catalytic subunits
Cell membrane, Synapse
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7AIS | X-ray | 1.75 Å | A/B=1-586 |
| 6G1U | X-ray | 1.79 Å | A/B=22-586 |
| 1EA5 | X-ray | 1.8 Å | A=22-558 |
| 6G1V | X-ray | 1.82 Å | A/B=22-586 |
| 7B38 | X-ray | 1.85 Å | A=25-556 |
| 6H14 | X-ray | 1.86 Å | A/B=22-586 |
| 7AIX | X-ray | 1.86 Å | A=1-586 |
| 6G1W | X-ray | 1.9 Å | A/B=22-586 |
| 7AIW | X-ray | 1.9 Å | A/B=1-586 |
| 2C5G | X-ray | 1.95 Å | A=22-558 |
| 2WFZ | X-ray | 1.95 Å | A=22-558 |
| 2WG2 | X-ray | 1.95 Å | A=22-558 |
| 6EUE | X-ray | 2.0 Å | A=24-556 |
| 7AIU | X-ray | 2.0 Å | A/B=1-586 |
| 1QID | X-ray | 2.05 Å | A=22-558 |
| 1W6R | X-ray | 2.05 Å | A=22-564 |
| 1E66 | X-ray | 2.1 Å | A=22-564 |
| 1GPK | X-ray | 2.1 Å | A=22-558 |
| 1QIE | X-ray | 2.1 Å | A=22-558 |
| 1QIF | X-ray | 2.1 Å | A=22-558 |
Showing 20 of 123 experimental structures (best resolution first).
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