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1S17

Identification of Novel Potent Bicyclic Peptide Deformylase Inhibitors

Summary for 1S17
Entry DOI10.2210/pdb1s17/pdb
Related1IX1 1N5N
DescriptorPeptide deformylase, NICKEL (II) ION, 2-(3,4-DIHYDRO-3-OXO-2H-BENZO[B][1,4]THIAZIN-2-YL)-N-HYDROXYACETAMIDE, ... (5 entities in total)
Functional Keywordspeptide deformylase inhibitor, rational drug design, antibiotic, protein-ligand complex, hydrolase
Biological sourcePseudomonas aeruginosa
Total number of polymer chains2
Total formula weight42419.64
Authors
Molteni, V.,He, X.,Nabakka, J.,Yang, K.,Kreusch, A.,Gordon, P.,Bursulaya, B.,Ryder, N.S.,Goldberg, R.,He, Y. (deposition date: 2004-01-05, release date: 2004-03-30, Last modification date: 2023-08-23)
Primary citationMolteni, V.,He, X.,Nabakka, J.,Yang, K.,Kreusch, A.,Gordon, P.,Bursulaya, B.,Warner, I.,Shin, T.,Biorac, T.,Ryder, N.S.,Goldberg, R.,Doughty, J.,He, Y.
Identification of novel potent bicyclic peptide deformylase inhibitors
Bioorg.Med.Chem.Lett., 14:1477-1481, 2004
Cited by
PubMed Abstract: Screening of our compound collection using Staphylococcus aureus Ni-Peptide deformylase (PDF) afforded a very potent PDF inhibitor with an IC(50) in the low nanomolar range but with poor antibacterial activity (MIC). Three-dimensional structural information obtained from Pseudomonas aeruginosa Ni-PDF complexed with the inhibitor suggested the synthesis of a variety of analogues that would maintain high binding affinity while attempting to improve antibacterial activity. Many of the compounds synthesized proved to be excellent PDF-Ni inhibitors and some showed increased antibacterial activity in selected strains.
PubMed: 15006385
DOI: 10.1016/j.bmcl.2004.01.014
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

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