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-Structure paper
Title | Ligand co-crystallization of aminoacyl-tRNA synthetases from infectious disease organisms. |
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Journal, issue, pages | Sci Rep, Vol. 7, Page 223-223, Year 2017 |
Publish date | Jun 30, 2011 (structure data deposition date) |
Authors | Moen, S.O. / Edwards, T.E. / Dranow, D.M. / Clifton, M.C. / Sankaran, B. / Van Voorhis, W.C. / Sharma, A. / Manoil, C. / Staker, B.L. / Myler, P.J. / Lorimer, D.D. |
External links | Sci Rep / PubMed:28303005 |
Methods | X-ray diffraction |
Resolution | 2.05 - 2.65 Å |
Structure data | PDB-3sp1: PDB-3tze: PDB-4e51: PDB-4ex5: PDB-4g6z: PDB-4gri: |
Chemicals | ChemComp-ZN: ChemComp-AMP: ChemComp-CL: ChemComp-HOH: ChemComp-TRP: ChemComp-K: ChemComp-HIS: ChemComp-LYS: ChemComp-GLU: ChemComp-MPD: ChemComp-NA: |
Source |
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Keywords | LIGASE / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID / lyme disease / peptide synthesis / protein biosynthesis / tRNA / CysRS / Cysteine tRNA ligase / amino acylation / eukaryotic pathogen / Microsporidia / Fungi / intracellular parasite / aminoacylation / tRNA activation / charged tRNA / histidyl-adenylate / ATP-dependent / tRNA synthetase / aaRS / TRANSFERASE / NIAID / National Institute of Allergy and Infectious Diseases / aminoacyl-tRNA synthetase / lysine tRNA ligase / protein synthesis / ATP-depenedent / tRNAlys / class IIb tRNA synthetase / class 1b aaRS / tRNA charging / GluRS / tRNAglu |