4EOX

X-ray Structure of Polypeptide Deformylase Bound to a Acylprolinamide inhibitor

Summary for 4EOX

• Entry DOI: 10.2210/pdb4eox/pdb
• Descriptor: Peptide deformylase, NICKEL (II) ION, N-benzoyl-1-[(2R)-3-cyclopentyl-2-{[formyl(hydroxy)amino]methyl}propanoyl]-L-prolinamide, ... (4 entities in total)
• Functional Keywords: alpha-beta, peptide deformylase metal ion binding, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Streptococcus pneumoniae
• Total number of polymer chains: 1
• Total formula weight: 23195.22

Authors

Ward, P.,Campobasso, N. (deposition date: 2012-04-16, release date: 2012-05-30, Last modification date: 2024-02-28)

Primary citation

Axten, J.M.,Medina, J.R.,Blackledge, C.W.,Duquenne, C.,Grant, S.W.,Bobko, M.A.,Peng, T.,Miller, W.H.,Pinckney, T.,Gallagher, T.F.,Kulkarni, S.,Lewandowski, T.,Van Aller, G.S.,Zonis, R.,Ward, P.,Campobasso, N.
Acylprolinamides: a new class of peptide deformylase inhibitors with in vivo antibacterial activity.
Bioorg.Med.Chem.Lett., 22:4028-4032, 2012

PubMed Abstract: A new class of PDF inhibitor with potent, broad spectrum antibacterial activity is described. Optimization of blood stability and potency provided compounds with improved pharmacokinetics that were suitable for in vivo experiments. Compound 5c, which has robust antibacterial activity, demonstrated efficacy in two respiratory tract infection models.

PubMed: 22579486
DOI: 10.1016/j.bmcl.2012.04.086

Experimental method

X-RAY DIFFRACTION (1.783 Å)