Publication : The free yeast aspartyl-tRNA synthetase differs from the tRNA(Asp)-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain.

First Author  Sauter C Year  2000
Journal  J Mol Biol Volume  299
Pages  1313-24 PubMed ID  10873455
Issue  5
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4 Bio Entities

Id Name Short Name Type
IPR004523 Aspartyl-tRNA synthetases Asp-tRNA_synthase Family
IPR004524 Aspartate-tRNA ligase, class IIb, bacterial/mitochondrial-type Asp-tRNA-ligase_IIb_bac/mt Family
IPR002312 Aspartyl/Asparaginyl-tRNA synthetase, class IIb Asp/Asn-tRNA-synth_IIb Family
IPR020780 Aspartyl-tRNA synthetase, archaea Asp-tRNA-synth_arc Family



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)