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8JE6

Crystal Structure of Anopheles culicifacies Prolyl-tRNA Synthetase (AcPRS) in complex with Halofuginone and ATP analogue

Summary for 8JE6
Entry DOI10.2210/pdb8je6/pdb
DescriptorPROLYL-TRNA SYNTHETASE, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, 7-bromo-6-chloro-3-{3-[(2R,3S)-3-hydroxypiperidin-2-yl]-2-oxopropyl}quinazolin-4(3H)-one, ... (5 entities in total)
Functional Keywordsmalaria, vector, anopheles, mosquito, larvicidal, aminoacyl-trna synthetase, ligase, ligase-inhibitor complex, ligase/inhibitor
Biological sourceAnopheles culicifacies
Total number of polymer chains2
Total formula weight118223.19
Authors
Goswami, R.,Manickam, Y.,Gupta, S.,Chhibber-Goel, J.,Harlos, K.,Sharma, A. (deposition date: 2023-05-15, release date: 2024-11-27, Last modification date: 2025-06-11)
Primary citationGoswami, R.,Manickam, Y.,Goel, J.C.,Gupta, S.,B M, S.,Sharma, A.
Chemical targeting of prolyl-tRNA synthetase stalls ovarian development and kills malaria vectors.
J.Infect.Dis., 2025
Cited by
PubMed Abstract: Along with rising resistance to antimalarials, the emergence of insecticide resistance in Anopheles mosquito species also remains a serious concern. Here, we reveal two potent compounds that show larvicidal and endectocidal activity against malaria vectors, Anopheles culicifacies and Anopheles stephensi, respectively.
PubMed: 40048639
DOI: 10.1093/infdis/jiaf095
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.883 Å)
Structure validation

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