Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with seryl-3'-aminoadenosine

Summary for 2HL1

Related1Y2Q 2HKZ 2HL0 2HL2
DescriptorThreonyl-tRNA synthetase, SERINE-3'-AMINOADENOSINE (3 entities in total)
Functional Keywordstranslation, editing, aminoacyl-trna synthetase, enzyme mechanism, enantioselectivity, ligase
Biological sourcePyrococcus abyssi
Cellular locationCytoplasm Q9UZ14
Total number of polymer chains2
Total molecular weight34183.29
Hussain, T.,Kruparani, S.P.,Pal, B.,Sankaranarayanan, R. (deposition date: 2006-07-06, release date: 2006-08-29, Last modification date: 2011-07-13)
Primary citation
Hussain, T.,Kruparani, S.P.,Pal, B.,Dock-Bregeon, A.C.,Dwivedi, S.,Shekar, M.R.,Sureshbabu, K.,Sankaranarayanan, R.
Post-transfer editing mechanism of a D-aminoacyl-tRNA deacylase-like domain in threonyl-tRNA synthetase from archaea
Embo J., 25:4152-4162, 2006
PubMed: 16902403 (PDB entries with the same primary citation)
DOI: 10.1038/sj.emboj.7601278
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.285110.7%3.6%3.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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