1S17
Identification of Novel Potent Bicyclic Peptide Deformylase Inhibitors
Summary for 1S17
Entry DOI | 10.2210/pdb1s17/pdb |
Related | 1IX1 1N5N |
Descriptor | Peptide 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 Keywords | peptide deformylase inhibitor, rational drug design, antibiotic, protein-ligand complex, hydrolase |
Biological source | Pseudomonas aeruginosa |
Total number of polymer chains | 2 |
Total formula weight | 42419.64 |
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 citation | Molteni, 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: 15006385DOI: 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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