5A2R
A New Crystal Structure of the Drosophila melanogaster Angiotensin Converting Enzyme Homologue AnCE.
Summary for 5A2R
| Entry DOI | 10.2210/pdb5a2r/pdb |
| Descriptor | ANGIOTENSIN-CONVERTING ENZYME, D-MALATE, ZINC ION, ... (6 entities in total) |
| Functional Keywords | hydrolase, angiotensin converting enzyme, drosophila melanogaster, drosophila proteins, animals, peptidyl- dipeptidase a, molecular structure |
| Biological source | DROSOPHILA MELANOGASTER (FRUIT FLY) |
| Total number of polymer chains | 1 |
| Total formula weight | 69932.66 |
| Authors | Harrison, C.,Acharya, K.R. (deposition date: 2015-05-22, release date: 2015-08-26, Last modification date: 2024-11-13) |
| Primary citation | Harrison, C.,Acharya, K.R. A New High-Resolution Crystal Structure of the Drosophila Melanogaster Angiotensin Converting Enzyme Homologue, Ance. FEBS Open Bio, 5:661-, 2015 Cited by PubMed Abstract: Angiotensin converting enzyme (ACE) is a zinc-dependent dipeptidyl carboxypeptidase with an essential role in blood pressure homeostasis in mammals. ACE has long been targeted in the treatment of hypertension through ACE inhibitors, however current inhibitors are known to cause severe side effects. Therefore, there is a requirement for a new generation of ACE inhibitors and structural information will be invaluable in their development. ACE is a challenging enzyme to work with due to its extensive glycosylation. As such, the Drosophila melanogaster ACE homologue, AnCE, which shares ∼60% sequence similarity with human ACE, can be used as a model for studying inhibitor binding. The presence of ligands originating from the crystallisation condition at the AnCE active site has proved an obstacle to studying the binding of new inhibitor precursors. Here we present the crystal structure of AnCE (in a new crystal form) at 1.85 Å resolution, using crystals grown under different conditions. This new structure may be more suitable for studying the binding of new compounds, with the potential of developing a new generation of improved ACE inhibitors. PubMed: 26380810DOI: 10.1016/J.FOB.2015.08.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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