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- PDB-1yft: The crystal structure of the catalytic fragment of alanyl-tRNA sy... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1yft | ||||||
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Title | The crystal structure of the catalytic fragment of alanyl-tRNA synthetase in complex wtih glycine | ||||||
![]() | Alanyl-tRNA synthetase | ||||||
![]() | LIGASE / alpha-beta fold / amino acid binding / helix-loop helix motif | ||||||
Function / homology | ![]() alanine-tRNA ligase / alanine-tRNA ligase activity / alanyl-tRNA aminoacylation / aminoacyl-tRNA editing activity / tRNA binding / zinc ion binding / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Swairjo, M.A. / Schimmel, P.R. | ||||||
![]() | ![]() Title: Breaking sieve for steric exclusion of a noncognate amino acid from active site of a tRNA synthetase. Authors: Swairjo, M.A. / Schimmel, P.R. #1: ![]() Title: Alanyl-tRNA synthetase crystal structure and design for acceptor-stem recognition. Authors: Swairjo, M.A. / Otero, F.J. / Yang, X.-L. / Lovato, M.A. / Skene, R.J. / McRee, D.E. / Ribas de Pouplana, L. / Schimmel, P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 106.4 KB | Display | ![]() |
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PDB format | ![]() | 80.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1yfrC ![]() 1yfsC ![]() 1ygbC ![]() 1riqS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Details | the biological unit is the entire asymmetric unit, i.e. one alanyl-tRNa synthetase molecule in complex with one glycine molecule. |
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Components
#1: Protein | Mass: 53772.246 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-GLY / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.26 Å3/Da / Density % sol: 46 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 6.2 Details: PEG 5000 mme, NaCL, Tris-Cl, Tris-base, glycine, pH 6.2, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 200 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 16, 2004 |
Radiation | Monochromator: curved crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.82653 Å / Relative weight: 1 |
Reflection | Resolution: 2.23→50 Å / Num. obs: 24100 / % possible obs: 99.7 % / Redundancy: 5.4 % / Rmerge(I) obs: 0.083 / Net I/σ(I): 12 |
Reflection shell | Resolution: 2.23→2.33 Å / Redundancy: 5.4 % / Rmerge(I) obs: 0.44 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1RIQ Resolution: 2.23→50 Å / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 21.9 Å2 | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.23→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.23→2.33 Å / Rfactor Rfree error: 0.233 / Total num. of bins used: 8
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