{"title":"铜绿假单胞菌trmB蛋白模型的分子建模及与选定化合物的对接分析。","authors":"Sakshi Bhati, Imteyaz Qamar, Nagendra Singh","doi":"10.6026/973206300210657","DOIUrl":null,"url":null,"abstract":"<p><p>Antimicrobial resistance (AMR) threatens global health with rising antibiotic-resistant infections, requiring novel antimicrobial targets. Therefore, it is of interest to report the molecular modeling and docking analysis <i>trmB</i> from <i>Pseudomonas aeruginosa</i> with suitable compounds. We show two compounds (5136 and 9865603) from the chemical library have optimal binding with the modelled <i>trmB</i> from <i>Pseudomonas aeruginosa</i> for further consideration.</p>","PeriodicalId":8962,"journal":{"name":"Bioinformation","volume":"21 4","pages":"657-664"},"PeriodicalIF":1.9000,"publicationDate":"2025-04-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12236524/pdf/","citationCount":"0","resultStr":"{\"title\":\"Molecular modelling and docking analysis of a modelled <i>trmB</i> protein from <i>Pseudomonas aeruginosa</i> with selected chemical compounds.\",\"authors\":\"Sakshi Bhati, Imteyaz Qamar, Nagendra Singh\",\"doi\":\"10.6026/973206300210657\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Antimicrobial resistance (AMR) threatens global health with rising antibiotic-resistant infections, requiring novel antimicrobial targets. Therefore, it is of interest to report the molecular modeling and docking analysis <i>trmB</i> from <i>Pseudomonas aeruginosa</i> with suitable compounds. We show two compounds (5136 and 9865603) from the chemical library have optimal binding with the modelled <i>trmB</i> from <i>Pseudomonas aeruginosa</i> for further consideration.</p>\",\"PeriodicalId\":8962,\"journal\":{\"name\":\"Bioinformation\",\"volume\":\"21 4\",\"pages\":\"657-664\"},\"PeriodicalIF\":1.9000,\"publicationDate\":\"2025-04-30\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12236524/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Bioinformation\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.6026/973206300210657\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2025/1/1 0:00:00\",\"PubModel\":\"eCollection\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bioinformation","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.6026/973206300210657","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2025/1/1 0:00:00","PubModel":"eCollection","JCR":"","JCRName":"","Score":null,"Total":0}
Molecular modelling and docking analysis of a modelled trmB protein from Pseudomonas aeruginosa with selected chemical compounds.
Antimicrobial resistance (AMR) threatens global health with rising antibiotic-resistant infections, requiring novel antimicrobial targets. Therefore, it is of interest to report the molecular modeling and docking analysis trmB from Pseudomonas aeruginosa with suitable compounds. We show two compounds (5136 and 9865603) from the chemical library have optimal binding with the modelled trmB from Pseudomonas aeruginosa for further consideration.
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