1ASZ

THE ACTIVE SITE OF YEAST ASPARTYL-TRNA SYNTHETASE: STRUCTURAL AND FUNCTIONAL ASPECTS OF THE AMINOACYLATION REACTION

Summary for 1ASZ

DescriptorT-RNA (75-MER), ASPARTYL-tRNA SYNTHETASE, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
Functional Keywordscomplex (aminoacyl-trna synthase-trna), complex (aminoacyl-trna synthase-trna) complex, complex (aminoacyl-trna synthase/trna)
Biological sourceSaccharomyces cerevisiae
Total number of polymer chains4
Total molecular weight161430.6
Authors
Cavarelli, J.,Rees, B.,Thierry, J.C.,Moras, D. (deposition date: 1995-01-19, release date: 1995-05-08, Last modification date: 2011-07-13)
Primary citation
Cavarelli, J.,Eriani, G.,Rees, B.,Ruff, M.,Boeglin, M.,Mitschler, A.,Martin, F.,Gangloff, J.,Thierry, J.C.,Moras, D.
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction.
EMBO J., 13:327-337, 1994
PubMed: 8313877 (PDB entries with the same primary citation)
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (3 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRNA backbone37 4.8% 13.8% 0.44MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
169963
PDB entries from 2020-10-14