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- PDB-1gsg: Structure of E.coli glutaminyl-tRNA synthetase complexed with trn... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1gsg | ||||||
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Title | Structure of E.coli glutaminyl-tRNA synthetase complexed with trnagln and ATP at 2.8 Angstroms resolution | ||||||
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![]() | LIGASE/RNA / PROTEIN-T-RNA COMPLEX / SINGLE STRAND / PROTEIN/RNA / 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 | ![]() | ||||||
![]() | Rould, M.A. / Perona, J.J. / Soell, D. / Steitz, T.A. | ||||||
![]() | ![]() 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. #1: ![]() 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. / Soell, D. #2: ![]() Title: Overproduction and Purification of Escherichia Coli tRNA(2Gln) and its Use in Crystallization of the Glutaminyl-tRNA Synthetase-tRNA(Gln) Complex Authors: Perona, J.J. / Swanson, R. / Steitz, T.A. / Soell, D. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 37.7 KB | Display | ![]() |
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PDB format | ![]() | 17.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 334 KB | Display | ![]() |
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Full document | ![]() | 334 KB | Display | |
Data in XML | ![]() | 1 KB | Display | |
Data in CIF | ![]() | 6.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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: 24134.473 Da / Num. of mol.: 1 / Source method: obtained synthetically |
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#2: Protein | Mass: 63434.641 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.75 Å3/Da / Density % sol: 67.22 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 17 ℃ / Method: vapor diffusion, hanging drop / Details: referred to J.Mol.Biol. 202.121 1988 / PH range low: 7.2 / PH range high: 6.8 | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Detector | Type: SDMS / Detector: AREA DETECTOR |
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Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Highest resolution: 2.8 Å |
Reflection | *PLUS Lowest resolution: 18 Å / Num. obs: 31768 / Num. measured all: 152900 / Rmerge(I) obs: 0.044 |
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Processing
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Refinement | Resolution: 2.8→7 Å / Rfactor Rwork: 0.279 / Rfactor obs: 0.279 | ||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→7 Å
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Refinement | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 7 Å / Rfactor all: 0.279 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS |