2XHM

Crystal structure of AnCE-K26 complex

Summary for 2XHM

• Entry DOI: 10.2210/pdb2xhm/pdb
• Related: 1J36 1J37 1J38 2X8Y 2X8Z 2X90 2X91 2X92 2X93 2X94 2X95 2X96 2X97
• Descriptor: ANGIOTENSIN CONVERTING ENZYME, beta-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, N-ACETYL-L-ILE-L-TYR-(R)-1-AMINO-2-(4-HYDROXYPHENYL)ETHYLPHOSPHONIC ACID, ... (7 entities in total)
• Functional Keywords: hydrolase, ace inhibitor, zinc metallopeptidase
• Biological source: DROSOPHILA MELANOGASTER (FRUIT FLY)
• Total number of polymer chains: 1
• Total formula weight: 71507.22

Authors

Akif, M.,Ntai, I.,Sturrock, E.D.,Isaac, R.E.,Bachmann, B.O.,Acharya, K.R. (deposition date: 2010-06-18, release date: 2010-07-14, Last modification date: 2024-10-16)

Primary citation

Akif, M.,Ntai, I.,Sturrock, E.D.,Isaac, R.E.,Bachmann, B.O.,Acharya, K.R.
Crystal Structure of a Phosphonotripeptide K-26 in Complex with Angiotensin Converting Enzyme Homologue (Ance) from Drosophila Melanogaster.
Biochem.Biophys.Res.Commun., 398:532-, 2010

PubMed Abstract: Angiotensin-I converting enzyme (ACE, a zinc dependent dipeptidyl carboxypeptidase) is a major target of drugs due to its role in the modulation of blood pressure and cardiovascular disorders. Here we present a crystal structure of AnCE (an ACE homologue from Drosophila melanogaster with a single enzymatic domain) in complex with a natural product-phosphonotripeptide, K-26 at 1.96A resolution. The inhibitor binds exclusively in the S(1) and S(2) binding pockets of AnCE (coordinating the zinc ion) through ionic and hydrogen bond interactions. A detailed structural comparison of AnCE.K-26 complex with individual domains of human somatic ACE provides useful information for further exploration of ACE inhibitor pharmacophores involving phosphonic acids.

PubMed: 20599761
DOI: 10.1016/J.BBRC.2010.06.113

Experimental method

X-RAY DIFFRACTION (1.96 Å)