Angiotensin-converting enzyme (ACE) is a 1306-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P12821.
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The mean pLDDT of this model is 90.9 (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 | 81% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity (PubMed:15615692, PubMed:20826823, PubMed:2558109, PubMed:4322742, PubMed:7523412, PubMed:7683654). Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates (PubMed:10913258, PubMed:1320019, PubMed:1851160, PubMed:19773553, PubMed:7683654, PubMed:7876104). Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium…
Monomer and homodimer; homodimerizes following binding to an inhibitor (PubMed:16476786). Interacts with calmodulin (CALM1, CALM2 or CALM3); interaction takes place in the cytoplasmic region and regulates phosphorylation and proteolytic cleavage (By similarity)
Cell membrane, Cytoplasm, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6H5W | X-ray | 1.37 Å | A=642-1232 |
| 9H1E | X-ray | 1.45 Å | A=642-1238 |
| 7Q27 | X-ray | 1.5 Å | A=642-1238 |
| 9QAN | X-ray | 1.5 Å | A=642-1238 |
| 9QAP | X-ray | 1.5 Å | A=645-1222 |
| 5AMB | X-ray | 1.55 Å | A/B=30-658 |
| 6F9T | X-ray | 1.6 Å | A=642-1232 |
| 7Q25 | X-ray | 1.6 Å | A/B=30-657 |
| 7Q29 | X-ray | 1.6 Å | A=642-1238 |
| 8QFX | X-ray | 1.6 Å | A/B/C/D=30-657 |
| 5AMC | X-ray | 1.65 Å | A/B=30-658 |
| 7Q28 | X-ray | 1.65 Å | A=642-1238 |
| 6F9V | X-ray | 1.69 Å | A/B=30-657 |
| 6TT3 | X-ray | 1.7 Å | A/B=30-657 |
| 7Q26 | X-ray | 1.7 Å | A/B=30-657 |
| 9H1B | X-ray | 1.7 Å | A/B=30-657 |
| 6EN5 | X-ray | 1.75 Å | A/B/C/D=30-657 |
| 7Z6Z | X-ray | 1.75 Å | A/B=30-657 |
| 4C2O | X-ray | 1.8 Å | A=642-1230 |
| 4UFA | X-ray | 1.8 Å | A/B=30-657 |
Showing 20 of 97 experimental structures (best resolution first).
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