9QMP

E.coli seryl-tRNA synthetase

Summary for 9QMP

Entry DOI	10.2210/pdb9qmp/pdb
Descriptor	Serine--tRNA ligase (2 entities in total)
Functional Keywords	aminoacyl-trna synthetase, atp binding, translation
Biological source	Escherichia coli K-12
Total number of polymer chains	1
Total formula weight	48477.95
Authors	Cusack, S. (deposition date: 2025-03-24, release date: 2025-05-14)
Primary citation	Cusack, S.,Berthet-Colominas, C.,Hartlein, M.,Nassar, N.,Leberman, R. A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A. Nature, 347:249-255, 1990 Cited by PubMed Abstract: The three-dimensional crystal structure of seryl-transfer RNA synthetase from Escherichia coli, refined at 2.5 A resolution, is described. It has an N-terminal domain that forms an antiparallel alpha helical coiled-coil, stretching 60 A out into the solvent and stabilized by interhelical hydrophobic interactions and an active-site alpha-beta domain based around a seven-stranded antiparallel beta sheet. Unlike the three other known synthetase structures, the enzyme contains no classical nucleotide-binding fold, and is the first representative of a second class of aminoacyl-tRNA synthetase structures. PubMed: 2205803 DOI: 10.1038/347249a0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.48 Å)

Structure validation