1j38 is a 2 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ 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
