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1j36

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1j36, resolution 2.40Å ()
Ligands: ,
Activity: Peptidyl-dipeptidase A, with EC number 3.4.15.1
Related: 1j37, 1j38
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

Crystal Structure of Drosophila AnCE

Publication Abstract from PubMed

Angiotensin I-converting enzymes (ACEs) are zinc metallopeptidases that cleave carboxy-terminal dipeptides from short peptide hormones. We have determined the crystal structures of AnCE, a Drosophila homolog of ACE, with and without bound inhibitors to 2.4 A resolution. AnCE contains a large internal channel encompassing the entire protein molecule. This substrate-binding channel is composed of two chambers, reminiscent of a peanut shell. The inhibitor and zinc-binding sites are located in the narrow bottleneck connecting the two chambers. The substrate and inhibitor specificity of AnCE appears to be determined by extensive hydrogen-bonding networks and ionic interactions in the active site channel. The catalytically important zinc ion is coordinated by the conserved Glu395 and histidine residues from a HExxH motif.

Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril., Kim HM, Shin DR, Yoo OJ, Lee H, Lee JO, FEBS Lett. 2003 Mar 13;538(1-3):65-70. PMID:12633854

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

About this Structure

1j36 is a 2 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

See Also

Reference

  • Kim HM, Shin DR, Yoo OJ, Lee H, Lee JO. Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril. FEBS Lett. 2003 Mar 13;538(1-3):65-70. PMID:12633854

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