PDBsum entry 1j36

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Hydrolase/hydrolase inhibitor PDB id
Protein chains
598 a.a. *
LPR ×2
_ZN ×2
Waters ×403
* Residue conservation analysis

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Key reference
Title Crystal structure of drosophila angiotensin i-Converting enzyme bound to captopril and lisinopril.
Authors H.M.Kim, D.R.Shin, O.J.Yoo, H.Lee, J.O.Lee.
Ref. FEBS Lett, 2003, 538, 65-70. [DOI no: 10.1016/S0014-5793(03)00128-5]
PubMed id 12633854
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.
Figure 1.
Fig. 1. Schematic diagram of the Drosophila AnCE structure. The zinc ion and the bound inhibitor, captopril, are shown in green and red, respectively.
Figure 4.
Fig. 4. Proposed reaction intermediates of AnCE (A) and thermolysin (B). His337 and His497 of AnCE are located close to Tyr507 and may have an effect on catalysis. The scissile peptide bonds are marked with curved red lines.
The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2003, 538, 65-70) copyright 2003.
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