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Yorodumi- PDB-1euy: GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH A TRNA MUTANT AND AN AC... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1euy | ||||||
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Title | GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH A TRNA MUTANT AND AN ACTIVE SITE INHIBITOR | ||||||
Components |
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Keywords | ligase/RNA / TRNA SYNTHETASE / GLUTAMINE / TRNAGLN / E. COLI / COMPLEX / 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 / SYNCHROTRON / Resolution: 2.6 Å | ||||||
Authors | Sherlin, L.D. / Bullock, T.L. / Newberry, K.J. / Lipman, R.S.A. / Hou, Y.-M. / Beijer, B. / Sproat, B.S. / Perona, J.J. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2000 Title: Influence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases. Authors: Sherlin, L.D. / Bullock, T.L. / Newberry, K.J. / Lipman, R.S. / Hou, Y.M. / Beijer, B. / Sproat, B.S. / Perona, J.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1euy.cif.gz | 161.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1euy.ent.gz | 122.2 KB | Display | PDB format |
PDBx/mmJSON format | 1euy.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1euy_validation.pdf.gz | 797 KB | Display | wwPDB validaton report |
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Full document | 1euy_full_validation.pdf.gz | 821.7 KB | Display | |
Data in XML | 1euy_validation.xml.gz | 16.8 KB | Display | |
Data in CIF | 1euy_validation.cif.gz | 25.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eu/1euy ftp://data.pdbj.org/pub/pdb/validation_reports/eu/1euy | HTTPS FTP |
-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: 23817.186 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: Product of runoff T7 Polymerase transcription from synthetic DNA template |
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#2: Protein | Mass: 62894.062 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: P00962, glutamine-tRNA ligase |
#3: Chemical | ChemComp-QSI / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.62 Å3/Da / Density % sol: 66.03 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 2.1 M (NH4)2SO4, 70 mM Buffer, 20 mM MgCl2, 20 mM BME at 298 K, pH 7.0, VAPOR DIFFUSION, HANGING DROP | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions |
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Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.1 / Wavelength: 0.98 |
Detector | Type: OTHER / Detector: CCD / Date: Apr 12, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→30 Å / Num. all: 48345 / Num. obs: 48345 / % possible obs: 95.5 % / Observed criterion σ(I): 0 / Redundancy: 3 % / Biso Wilson estimate: 56 Å2 / Rmerge(I) obs: 0.056 / Net I/σ(I): 0.151 |
Reflection shell | Resolution: 2.6→2.7 Å / Redundancy: 1 % / Rmerge(I) obs: 0.274 / % possible all: 95.2 |
Reflection | *PLUS Num. measured all: 309007 |
Reflection shell | *PLUS % possible obs: 95.2 % / Mean I/σ(I) obs: 3.5 |
-Processing
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Refinement | Resolution: 2.6→30 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2.6→30 Å
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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