5W6M
Crystal structure of the human histidyl-tRNA synthetase mutant D175E
Summary for 5W6M
Entry DOI | 10.2210/pdb5w6m/pdb |
Descriptor | Histidine--tRNA ligase, cytoplasmic (1 entity in total) |
Functional Keywords | trna-synthetase, cmt mutant, ligase |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 2 |
Total formula weight | 101845.39 |
Authors | Blocquel, D.,Yang, X.L. (deposition date: 2017-06-16, release date: 2018-06-20, Last modification date: 2023-10-04) |
Primary citation | Blocquel, D.,Sun, L.,Matuszek, Z.,Li, S.,Weber, T.,Kuhle, B.,Kooi, G.,Wei, N.,Baets, J.,Pan, T.,Schimmel, P.,Yang, X.L. CMT disease severity correlates with mutation-induced open conformation of histidyl-tRNA synthetase, not aminoacylation loss, in patient cells. Proc.Natl.Acad.Sci.USA, 2019 Cited by PubMed: 31501329DOI: 10.1073/pnas.1908288116 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.696 Å) |
Structure validation
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