1sry is a 2 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The three-dimensional structure of the seryl-tRNA synthetase from Thermus thermophilus has been determined and refined at 2.5 A resolution. The final model consists of a dimer of 421 residues each and 190 water molecules. The R-factor is 18.4% for all the data between 10 and 2.5 A resolution. The structure is very similar to that of the homologous enzyme from Escherichia coli, with an r.m.s. difference of 1.5 A for the 357 alpha-carbon atoms considered equivalent. The comparison of the two structures indicates increased hydrophobicity, reduced conformational entropy and reduced torsional strain as possible mechanisms by which thermostability is obtained in the enzyme from the thermophile.
Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 A resolution.,Fujinaga M, Berthet-Colominas C, Yaremchuk AD, Tukalo MA, Cusack S J Mol Biol. 1993 Nov 5;234(1):222-33. PMID:8230201[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Fujinaga M, Berthet-Colominas C, Yaremchuk AD, Tukalo MA, Cusack S. Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 A resolution. J Mol Biol. 1993 Nov 5;234(1):222-33. PMID:8230201 doi:http://dx.doi.org/10.1006/jmbi.1993.1576
