Angiotensin-converting enzyme 2 (ACE2) is a 805-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9BYF1.
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The mean pLDDT of this model is 90.7 (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 | 78% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 5% |
What pLDDT means and how to read it
Essential counter-regulatory carboxypeptidase of the renin-angiotensin hormone system that is a critical regulator of blood volume, systemic vascular resistance, and thus cardiovascular homeostasis (PubMed:27217402). Converts angiotensin I to angiotensin 1-9, a nine-amino acid peptide with anti-hypertrophic effects in cardiomyocytes, and angiotensin II to angiotensin 1-7, which then acts as a beneficial vasodilator and anti-proliferation agent, counterbalancing the actions of the vasoconstrictor angiotensin II (PubMed:10924499, PubMed:10969042, PubMed:11815627, PubMed:14504186, PubMed:19021774). Also removes the C-terminal residue from three other vasoactive peptides, neurotensin,…
Homodimer (PubMed:32132184). Interacts with the catalytically active form of TMPRSS2 (PubMed:21068237). Interacts with SLC6A19; this interaction is essential for expression and function of SLC6A19 in intestine (By similarity). Interacts with ITGA5:ITGB1 (PubMed:15276642, PubMed:33102950). Probably interacts (via endocytic sorting signal motif) with AP2M1; the interaction is inhibited by…
Secreted, Cell membrane, Cytoplasm, Cell projection, cilium, Apical cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9SPA | X-ray | 1.79 Å | C=19-615 |
| 28KD | X-ray | 2.02 Å | A/B=19-615 |
| 8BYJ | X-ray | 2.07 Å | A/B=19-615 |
| 8B9P | X-ray | 2.11 Å | A/B=19-615 |
| 8XSF | EM | 2.16 Å | A=1-805 |
| 1R42 | X-ray | 2.2 Å | A=1-615 |
| 7JVO | X-ray | 2.2 Å | B=766-779 |
| 8TOR | X-ray | 2.2 Å | A=18-614 |
| 9RVA | X-ray | 2.2 Å | A=19-740 |
| 9UE7 | EM | 2.27 Å | D/E/F=1-615 |
| 8TOQ | X-ray | 2.3 Å | A=18-614 |
| 8BFW | X-ray | 2.33 Å | A/C=19-615 |
| 8TOS | X-ray | 2.35 Å | A=18-614 |
| 7UFK | X-ray | 2.38 Å | A/B=19-615 |
| 9RVT | X-ray | 2.39 Å | A/B/D/G=19-615 |
| 7EKH | X-ray | 2.4 Å | A=19-615 |
| 6M0J | X-ray | 2.45 Å | A=19-615 |
| 7T9K | EM | 2.45 Å | D/E=18-615 |
| 7LO4 | X-ray | 2.46 Å | A=19-614 |
| 8WE1 | EM | 2.47 Å | A=1-805 |
Showing 20 of 343 experimental structures (best resolution first).
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