Q56H28: Angiotensin-converting enzyme 2 (ACE2)

Angiotensin-converting enzyme 2 (ACE2) is a 805-residue protein from Felis catus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q56H28.

Gene
ACE2
Organism
Felis catus
Length
805 residues
Mean pLDDT
90.3
Model
AF-Q56H28-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 90.3 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate77%
70 to 90Confident: backbone generally right15%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions6%

What pLDDT means and how to read it

Function

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. 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. Also removes the C-terminal residue from three other vasoactive peptides, neurotensin, kinetensin, and des-Arg bradykinin, but is not active on bradykinin. Also cleaves other biological peptides,…

Subunit structure

Homodimer. Interacts with the catalytically active form of TMPRSS2 (By similarity). Interacts with SLC6A19; this interaction is essential for expression and function of SLC6A19 in intestine (By similarity). Interacts with ITGA5:ITGB1 (By similarity). Probably interacts (via endocytic sorting signal motif) with AP2M1; the interaction is inhibited by phosphorylation of Tyr-781 (By similarity).…

Subcellular location

Secreted, Cell membrane, Cytoplasm, Cell projection, cilium, Apical cell membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
9DAKEM2.4 ÅA=3-740
9N7EEM2.5 ÅA=1-743
9C6OEM2.77 ÅA=3-729
9KWYEM2.82 ÅA=19-599
7C8DEM3.0 ÅA=18-740
8ZUFEM3.31 ÅA=22-805

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