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Yorodumi- PDB-1euq: CRYSTAL STRUCTURE OF GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH A ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1euq | ||||||
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Title | CRYSTAL STRUCTURE OF GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH A TRNA-GLN MUTANT AND AN ACTIVE-SITE INHIBITOR | ||||||
Components |
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Keywords | ligase/RNA / TRNA SYNTHETASE / GLUTAMINE / TRNAGLN / E. COLI / RNA-PROTEIN 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: 3.1 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 | 1euq.cif.gz | 159.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1euq.ent.gz | 121.5 KB | Display | PDB format |
PDBx/mmJSON format | 1euq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eu/1euq ftp://data.pdbj.org/pub/pdb/validation_reports/eu/1euq | 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: 23181.812 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 / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.55 Å3/Da / Density % sol: 65.34 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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: 5.0.2 / 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: 3.1→30 Å / Num. all: 22694 / Num. obs: 22694 / % possible obs: 100 % / Redundancy: 4 % / Biso Wilson estimate: 53 Å2 / Rmerge(I) obs: 0.092 / Net I/σ(I): 0.158 |
Reflection shell | Resolution: 3.1→3.2 Å / Redundancy: 1 % / Rmerge(I) obs: 0.375 / % possible all: 100 |
Reflection | *PLUS Num. measured all: 183349 |
Reflection shell | *PLUS % possible obs: 100 % |
-Processing
Software |
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Refinement | Resolution: 3.1→30 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 3.1→30 Å
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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