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Yorodumi- PDB-1qrs: GLUTAMINYL-TRNA SYNTHETASE MUTANT D235N COMPLEXED WITH GLUTAMINE ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1qrs | ||||||
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Title | GLUTAMINYL-TRNA SYNTHETASE MUTANT D235N COMPLEXED WITH GLUTAMINE TRANSFER RNA | ||||||
Components |
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Keywords | LIGASE/RNA / AMINOACYL-TRNA SYNTHASE / PROTEIN BIOSYNTHESIS / LIGASE / ATP-B / COMPLEX (AMINOACYL-TRNA SYNTHASE-TRNA) / LIGASE-RNA COMPLEX | ||||||
Function / homology | Function and homology information glutamine-tRNA ligase / glutamine-tRNA ligase activity / glutaminyl-tRNA aminoacylation / glutamyl-tRNA aminoacylation / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.6 Å | ||||||
Authors | Arnez, J.G. / Steitz, T.A. | ||||||
Citation | Journal: Biochemistry / Year: 1996 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: Journal: Nature / Year: 1991 Title: Structural Basis of Anticodon Loop Recognition by Glutaminyl-tRNA Synthetase Authors: Rould, M.A. / Perona, J.J. / Steitz, T.A. #2: Journal: Science / Year: 1989 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: Journal: Science / Year: 1989 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: Journal: Proc.Natl.Acad.Sci.USA / Year: 1984 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qrs.cif.gz | 181.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qrs.ent.gz | 147.5 KB | Display | PDB format |
PDBx/mmJSON format | 1qrs.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qr/1qrs ftp://data.pdbj.org/pub/pdb/validation_reports/qr/1qrs | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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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.) Escherichia coli (E. coli) / Strain: K-12 / Description: LAMBDA PL PROMOTER / Gene: TRNAGLN2 / Variant: DELTAH1DELTATRP / Plasmid details: PLC28 DERIVATIVE / Plasmid: PRS3 (PLC28 DERIVATIVE) / Gene (production host): TRNAGLN2 / Production host: Escherichia coli (E. coli) |
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#2: Protein | Mass: 63433.648 Da / Num. of mol.: 1 / Mutation: D235N Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: X3R2 (GLNS DELETION STRAIN) / Description: GLNS PROMOTER (NO OVEREXPRESSION) / Gene: GLNS7 / Plasmid details: DERIVATIVE OF PBR / Plasmid: PYY140 (DERIVATIVE OF PBR322) / Gene (production host): GLNS7 / Production host: Escherichia coli (E. coli) / Keywords: MUTANT D235N / References: UniProt: P00962, glutamine-tRNA ligase |
#3: Chemical | ChemComp-ATP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 3 |
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-Sample preparation
Crystal | Density Matthews: 3.78 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 30, 1990 |
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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: 36285 / % possible obs: 91.4 % / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Rmerge(I) obs: 0.047 |
Reflection | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 8 Å / % possible obs: 91.4 % / Observed criterion σ(I): 0 / Redundancy: 3.3 % |
-Processing
Software |
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Refinement | Resolution: 2.6→6 Å / σ(F): 0 /
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Displacement parameters | Biso mean: 31.25 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.4 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→6 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 6 Å / σ(F): 0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |