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2xhm

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2xhm, resolution 1.96Å ()
Ligands: , , , , ,
Activity: Peptidyl-dipeptidase A, with EC number 3.4.15.1
Related: 1j38, 2x94, 2x8z, 1j36, 2x8y, 2x91, 2x95, 2x96, 2x92, 2x93, 2x97, 2x90, 1j37


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

CRYSTAL STRUCTURE OF ANCE-K26 COMPLEX

Publication Abstract from PubMed

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.

Crystal structure of a phosphonotripeptide K-26 in complex with angiotensin converting enzyme homologue (AnCE) from Drosophila melanogaster., Akif M, Ntai I, Sturrock ED, Isaac RE, Bachmann BO, Acharya KR, Biochem Biophys Res Commun. 2010 Jul 30;398(3):532-6. Epub 2010 Jul 1. PMID:20599761

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

2xhm is a 1 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

See Also

Reference

  • Akif M, Ntai I, Sturrock ED, Isaac RE, Bachmann BO, Acharya KR. Crystal structure of a phosphonotripeptide K-26 in complex with angiotensin converting enzyme homologue (AnCE) from Drosophila melanogaster. Biochem Biophys Res Commun. 2010 Jul 30;398(3):532-6. Epub 2010 Jul 1. PMID:20599761 doi:10.1016/j.bbrc.2010.06.113

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