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TitleACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis.
Journal, issue, pagesJ. Biol. Chem., Vol. 279, Page 17996-18007, Year 2004
Publish dateOct 7, 2003 (structure data deposition date)
AuthorsTowler, P. / Staker, B. / Prasad, S.G. / Menon, S. / Tang, J. / Parsons, T. / Ryan, D. / Fisher, M. / Williams, D. / Dales, N.A. ...Towler, P. / Staker, B. / Prasad, S.G. / Menon, S. / Tang, J. / Parsons, T. / Ryan, D. / Fisher, M. / Williams, D. / Dales, N.A. / Patane, M.A. / Pantoliano, M.W.
External linksJ. Biol. Chem. / PubMed:14754895
MethodsX-ray diffraction
Resolution2.2 - 3 Å
Structure data

PDB-1r42:
Native Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2)
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-1r4l:
Inhibitor Bound Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2)
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-CL:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-XX5:
(S,S)-2-{1-CARBOXY-2-[3-(3,5-DICHLORO-BENZYL)-3H-IMIDAZOL-4-YL]-ETHYLAMINO}-4-METHYL-PENTANOIC ACID

Source
  • homo sapiens (human)
KeywordsHYDROLASE / zinc metallopeptidase domain / collectrin homology domain / native or open conformation / chloride ion binding site / zinc binding site / inhibitor bound conformation / zinc ion binding site

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