1QXW
Crystal structure of Staphyloccocus aureus in complex with an aminoketone inhibitor 54135.
Summary for 1QXW
| Entry DOI | 10.2210/pdb1qxw/pdb |
| Related | 1QXY 1QXZ |
| Descriptor | methionyl aminopeptidase, COBALT (II) ION, ACETATE ION, ... (5 entities in total) |
| Functional Keywords | pita bread fold, hydrolase |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 1 |
| Total formula weight | 27973.50 |
| Authors | Douangamath, A.,Dale, G.E.,D'Arcy, A.,Oefner, C. (deposition date: 2003-09-09, release date: 2004-03-16, Last modification date: 2024-02-14) |
| Primary citation | Douangamath, A.,Dale, G.E.,D'Arcy, A.,Almstetter, M.,Eckl, R.,Frutos-Hoener, A.,Henkel, B.,Illgen, K.,Nerdinger, S.,Schulz, H.,MacSweeney, A.,Thormann, M.,Treml, A.,Pierau, S.,Wadman, S.,Oefner, C. Crystal structures of staphylococcusaureus methionine aminopeptidase complexed with keto heterocycle and aminoketone inhibitors reveal the formation of a tetrahedral intermediate. J.Med.Chem., 47:1325-1328, 2004 Cited by PubMed Abstract: High-resolution crystal structures of Staphylococcus aureus methionine aminopeptidase I in complex with various keto heterocycles and aminoketones were determined, and the intermolecular ligand interactions with the enzyme are reported. The compounds are effective inhibitors of the S. aureus enzyme because of the formation of an uncleavable tetrahedral intermediate upon binding. The electron densities unequivocally show the enzyme-catalyzed transition-state analogue mimicking that for amide bond hydrolysis of substrates. PubMed: 14998322DOI: 10.1021/jm034188j PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.67 Å) |
Structure validation
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