3FHJ
Independent saturation of three TrpRS subsites generates a partially-assembled state similar to those observed in molecular simulations
Summary for 3FHJ
Entry DOI | 10.2210/pdb3fhj/pdb |
Related | 1D2R 1I6K 1I6L 1I6M 1M83 1MAU 1MB2 2OV4 3FI0 |
Descriptor | Tryptophanyl-tRNA synthetase, TRYPTOPHAN, PHOSPHATE ION, ... (4 entities in total) |
Functional Keywords | ligand-dependent domain rearrangement, mechanistic pathway, molecular simulations, aminoacyl-trna synthetase, atp-binding, cytoplasm, ligase, nucleotide-binding, protein biosynthesis, translation |
Biological source | Bacillus stearothermophilus |
Total number of polymer chains | 6 |
Total formula weight | 227232.53 |
Authors | Laowanapiban, P.,Kapustina, M.,Vonrhein, C.,Delarue, M.,Koehl, P.,Carter Jr., C.W. (deposition date: 2008-12-09, release date: 2009-02-03, Last modification date: 2023-09-06) |
Primary citation | Laowanapiban, P.,Kapustina, M.,Vonrhein, C.,Delarue, M.,Koehl, P.,Carter, C.W. Independent saturation of three TrpRS subsites generates a partially assembled state similar to those observed in molecular simulations. Proc.Natl.Acad.Sci.Usa, 106:1790-1795, 2009 Cited by PubMed: 19174517DOI: 10.1073/pnas.0812752106 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.65 Å) |
Structure validation
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