9SG89SG8 の概要
| エントリーDOI | 10.2210/pdb9sg8/pdb |
| 関連するPDBエントリー | 9SG5 9SG6 9SG7 9SG9 9SGA 9SGB 9SGC 9SGD 9SGE |
| 分子名称 | Penicillin-binding protein 1B, [(2~{S},3~{S})-3-[[(2~{R})-2-methoxy-2-phenyl-ethanoyl]amino]-4-oxidanylidene-butan-2-yl]sulfamic acid, CHLORIDE ION, ... (4 entities in total) |
| 機能のキーワード | cell wall, peptidoglycan synthesis enzyme, drug-binding protein, monobactam, transferase |
| 由来する生物種 | Streptococcus pneumoniae |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 55373.47 |
| 構造登録者 | |
| 主引用文献 | Kavas, V.,Contreras-Martel, C.,Pajk, S.,Knez, D.,Martins, A.,Gould, T.A.,Roper, D.I.,Zdovc, I.,Dessen, A.,Hrast Rambaher, M.,Gobec, S. Structure-Activity Relationship and Crystallographic Study of New Monobactams. J.Med.Chem., 69:3887-3901, 2026 Cited by PubMed Abstract: Monobactams, a subclass of β-lactam antibiotics with a monocyclic scaffold, are uniquely resistant to hydrolysis by metallo-β-lactamases, providing a distinct therapeutic advantage. Here, we report an -based structure-activity relationship (SAR) investigation of aztreonam-related monobactams. A focused library of monobactam derivatives was synthesized and evaluated for inhibition of penicillin-binding proteins (PBPs) and antibacterial activity. Ten compounds, including aztreonam, were crystallized with truncated PBP1b from , used as a model PBP. Potent PBP1b inhibitors were developed, although high enzymatic potency was not always reflected in strong antibacterial activity. Certain derivatives showed activity against , which is typically resistant to monobactams. 2D similarity search identified potent inhibitors active against , , and . Crystal structures revealed previously unrecognized binding interactions, including a halogen bond with a conserved threonine residue, underscoring the potential of these interactions to support the development of more potent PBP inhibitors. PubMed: 41632911DOI: 10.1021/acs.jmedchem.5c02427 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.811 Å) |
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