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- PDB-1qru: GLUTAMINYL-TRNA SYNTHETASE MUTANT I129T COMPLEXED WITH GLUTAMINE ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1qru | ||||||
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Title | GLUTAMINYL-TRNA SYNTHETASE MUTANT I129T COMPLEXED WITH GLUTAMINE TRANSFER RNA | ||||||
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![]() | LIGASE/RNA / AMINOACYL-TRNA SYNTHASE / PROTEIN BIOSYNTHESIS / LIGASE / ATP-B / COMPLEX (AMINOACYL-TRNA SYNTHASE-TRNA) / LIGASE-RNA COMPLEX | ||||||
Function / homology | ![]() glutamine-tRNA ligase / glutamine-tRNA ligase activity / glutaminyl-tRNA aminoacylation / glutamyl-tRNA aminoacylation / aminoacyl-tRNA synthetase multienzyme complex / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Arnez, J.G. / Steitz, T.A. | ||||||
![]() | ![]() Title: Crystal structures of three misacylating mutants of Escherichia coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP. Authors: Arnez, J.G. / Steitz, T.A. #1: ![]() Title: Structural Basis of Anticodon Loop Recognition by Glutaminyl-tRNA Synthetase Authors: Rould, M.A. / Perona, J.J. / Steitz, T.A. #2: ![]() Title: Structural Basis for Misaminoacylation by Mutant E. Coli Glutaminyl-tRNA Synthetase Enzymes Authors: Perona, J.J. / Swanson, R.N. / Rould, M.A. / Steitz, T.A. / Soll, D. #3: ![]() Title: Structure of E. Coli Glutaminyl-tRNA Synthetase Complexed with tRNA(Gln) and ATP at 2.8 A Resolution Authors: Rould, M.A. / Perona, J.J. / Soll, D. / Steitz, T.A. #4: ![]() Title: Transfer RNA Mischarging Mediated by a Mutant Escherichia Coli Glutaminyl-tRNA Synthetase Authors: Inokuchi, H. / Hoben, P. / Yamao, F. / Ozeki, H. / Soll, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 179.9 KB | Display | ![]() |
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PDB format | ![]() | 139.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 762.2 KB | Display | ![]() |
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Full document | ![]() | 786.5 KB | Display | |
Data in XML | ![]() | 24.8 KB | Display | |
Data in CIF | ![]() | 34.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: RNA chain | Mass: 24060.287 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein | Mass: 63422.586 Da / Num. of mol.: 1 / Mutation: I129T Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
#3: Chemical | ChemComp-ATP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.74 Å3/Da / Density % sol: 70 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 70 % | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 17 ℃ / Method: vapor diffusion, hanging drop / PH range low: 7.5 / PH range high: 7 | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Detector | Type: SDMS / Detector: AREA DETECTOR / Date: Dec 1, 1989 |
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Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 23275 / % possible obs: 90.7 % / Observed criterion σ(I): 0 / Redundancy: 2.7 % / Rmerge(I) obs: 0.097 |
Reflection | *PLUS Highest resolution: 3 Å / Lowest resolution: 9 Å / % possible obs: 90.7 % / Observed criterion σ(I): 0 / Redundancy: 2.7 % |
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Processing
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Refinement | Resolution: 3→7 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 3→7 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 3 Å / Lowest resolution: 7 Å / σ(F): 0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |