3FX6

X-RAY crystallographic studies on the complex of carboxypeptidase A with the inhibitor using alpha-nitro ketone as the zinc-binding group

Summary for 3FX6

• Entry DOI: 10.2210/pdb3fx6/pdb
• Descriptor: Carboxypeptidase A1, ZINC ION, (2R)-4,4-dihydroxy-5-nitro-2-(phenylmethyl)pentanoic acid, ... (4 entities in total)
• Functional Keywords: alpha-nitro ketone, inhibitor, hydrolase, carboxypeptidase, metal-binding, metalloprotease, polymorphism, protease, secreted, zinc, zymogen
• Biological source: Bos taurus (Bovine)
• Cellular location: Secreted, extracellular space: P00730
• Total number of polymer chains: 3
• Total formula weight: 104514.34

Authors

Wang, S.F.,Jin, J.Y.,Tian, G.R. (deposition date: 2009-01-20, release date: 2009-08-25, Last modification date: 2024-10-16)

Primary citation

Wang, S.F.,Tian, G.R.,Zhang, W.Z.,Jin, J.Y.
Characterization of alpha-nitromethyl ketone as a new zinc-binding group based on structural analysis of its complex with carboxypeptidase A
Bioorg.Med.Chem.Lett., 19:5009-5011, 2009

PubMed Abstract: Zinc-binding groups (ZBGs) are exhaustively applied in the development of the new inhibitors against a wide variety of physiologically and pathologically important zinc proteases. Here the alpha-nitro ketone was presented as a new ZBG, which is a transition-state analog featured by the unique bifurcated hydrogen bonds at the active site of carboxypeptidase A based on the structural analysis. Introduction of a nitro group at the alpha-position of the ketone could provide more non-covalent interactions without loss of the abilities to form a tetrahedral transition-state analog.

PubMed: 19646864
DOI: 10.1016/j.bmcl.2009.07.060

Experimental method

X-RAY DIFFRACTION (1.851 Å)