Pub. Date : 2010 Jul 30
PMID : 20599761
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Crystal structure of a phosphonotripeptide K-26 in complex with angiotensin converting enzyme homologue (AnCE) from Drosophila melanogaster. | phosphonotripeptide k-26 | Angiotensin converting enzyme | Drosophila melanogaster |
| 2 | Crystal structure of a phosphonotripeptide K-26 in complex with angiotensin converting enzyme homologue (AnCE) from Drosophila melanogaster. | phosphonotripeptide k-26 | Angiotensin converting enzyme | Drosophila melanogaster |
| 3 | 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. | phosphonotripeptide | Angiotensin converting enzyme | Drosophila melanogaster |
| 4 | 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. | phosphonotripeptide | Angiotensin converting enzyme | Drosophila melanogaster |
| 5 | 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. | Hydrogen | Angiotensin converting enzyme | Drosophila melanogaster |
| 6 | 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. | Phosphorous Acids | Angiotensin converting enzyme | Drosophila melanogaster |