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- PDB-2zt7: Crystal structure of human Glycyl-tRNA synthetase (GlyRS) in comp... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2zt7 | ||||||
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Title | Crystal structure of human Glycyl-tRNA synthetase (GlyRS) in complex with Glycine and ATP | ||||||
![]() | Glycyl-tRNA synthetase | ||||||
![]() | LIGASE / AP4A / Glycine / ATP / Gly-AMP / tRNA / Aminoacyl-tRNA synthetase / ATP-binding / Charcot-Marie-Tooth disease / Disease mutation / Nucleotide-binding / Phosphoprotein / Protein biosynthesis | ||||||
Function / homology | ![]() mitochondrial glycyl-tRNA aminoacylation / bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity / glycine-tRNA ligase / glycine-tRNA ligase activity / Mitochondrial tRNA aminoacylation / diadenosine tetraphosphate biosynthetic process / Cytosolic tRNA aminoacylation / tRNA aminoacylation for protein translation / secretory granule / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases ...mitochondrial glycyl-tRNA aminoacylation / bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity / glycine-tRNA ligase / glycine-tRNA ligase activity / Mitochondrial tRNA aminoacylation / diadenosine tetraphosphate biosynthetic process / Cytosolic tRNA aminoacylation / tRNA aminoacylation for protein translation / secretory granule / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / transferase activity / protein dimerization activity / mitochondrial matrix / axon / mitochondrion / extracellular exosome / ATP binding / identical protein binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Guo, R.T. / Yang, X.L. / Schimmel, P. | ||||||
![]() | ![]() Title: Crystal structures and biochemical analyses suggest unique mechanism and role for human GlyRS in Ap4A homeostasis Authors: Guo, R.T. / Chong, Y.E. / Guo, M. / Yang, X.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 125.5 KB | Display | ![]() |
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PDB format | ![]() | 95 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2zt5C ![]() 2zt6C ![]() 2zt8C ![]() 2zxfC ![]() 2pmeS 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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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 78704.828 Da / Num. of mol.: 1 / Fragment: UNP residues 55-739 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-GLY / |
#3: Chemical | ChemComp-ATP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.42 Å3/Da / Density % sol: 64.08 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 25mM Tris-HCl, 150mM NaCl, 10mM MgCl2, 3.8-4.0M Sodium Formate, pH7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: May 20, 2008 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→50 Å / Num. all: 30017 / Num. obs: 29864 / % possible obs: 98.2 % / Observed criterion σ(F): 0 / Redundancy: 6.7 % / Rmerge(I) obs: 0.047 / Net I/σ(I): 38.3 |
Reflection shell | Resolution: 2.7→50 Å / Redundancy: 4.5 % / Rmerge(I) obs: 0.347 / Mean I/σ(I) obs: 4.1 / Num. unique all: 2711 / % possible all: 91.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2PME Resolution: 2.7→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: 57 Å2 | |||||||||||||||||||||||||
Refine analyze | Luzzati sigma a obs: 0.68 Å | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.7→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.7→2.8 Å
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