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1R4L

Inhibitor Bound Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2)

Summary for 1R4L
Entry DOI10.2210/pdb1r4l/pdb
Related1R42
Descriptorangiotensin I converting enzyme 2, disordered segment of collectrin homology domain, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total)
Functional Keywordszinc metallopeptidase domain, collectrin homology domain, inhibitor bound conformation, chloride ion binding site, zinc ion binding site, hydrolase
Biological sourceHomo sapiens (human)
More
Total number of polymer chains5
Total formula weight76979.55
Authors
Towler, P.,Staker, B.,Prasad, S.G.,Menon, S.,Ryan, D.,Tang, J.,Parsons, T.,Fisher, M.,Williams, D.,Dales, N.A.,Patane, M.A.,Pantoliano, M.W. (deposition date: 2003-10-07, release date: 2004-02-03, Last modification date: 2023-08-23)
Primary citationTowler, 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.
ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis.
J.Biol.Chem., 279:17996-18007, 2004
Cited by
PubMed: 14754895
DOI: 10.1074/jbc.M311191200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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