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- PDB-3td2: Crystal structures of Peptidyl-tRNA hydrolase from Mycobacterium ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3td2 | ||||||
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Title | Crystal structures of Peptidyl-tRNA hydrolase from Mycobacterium tuberculosis - Form 5 | ||||||
![]() | Peptidyl-tRNA hydrolase | ||||||
![]() | HYDROLASE / Pth / Hydrolysis of Peptidyl-tRNA / Peptidyl-tRNA / Cytosol | ||||||
Function / homology | ![]() peptidyl-tRNA hydrolase / aminoacyl-tRNA hydrolase activity / translation / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Selvaraj, M. / Ahmad, R. / Varshney, U. / Vijayan, M. | ||||||
![]() | ![]() Title: Structures of new crystal forms of Mycobacterium tuberculosis peptidyl-tRNA hydrolase and functionally important plasticity of the molecule Authors: Selvaraj, M. / Ahmad, R. / Varshney, U. / Vijayan, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 84.1 KB | Display | ![]() |
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PDB format | ![]() | 64.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 422.9 KB | Display | ![]() |
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Full document | ![]() | 426.6 KB | Display | |
Data in XML | ![]() | 10.2 KB | Display | |
Data in CIF | ![]() | 13.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3tckC ![]() 3tcnC ![]() 3td6C ![]() 2z2iS C: citing same article ( S: Starting model for refinement |
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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: Protein | Mass: 20485.531 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P65865, UniProt: P9WHN7*PLUS, peptidyl-tRNA hydrolase |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.25 Å3/Da / Density % sol: 45.25 % |
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Crystal grow | Temperature: 291 K / Method: microbatch under oil / pH: 7.5 Details: 0.1M HEPES, 25% PEG 8000, 5% dioxane, pH 7.5, Microbatch under oil, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Jun 8, 2010 |
Radiation | Monochromator: Osmic mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→30 Å / Num. obs: 6725 / % possible obs: 99.7 % / Redundancy: 3.9 % / Biso Wilson estimate: 72.9 Å2 / Rmerge(I) obs: 0.081 |
Reflection shell | Resolution: 2.5→2.64 Å |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2Z2I Resolution: 2.5→30 Å / Cor.coef. Fo:Fc: 0.939 / Cor.coef. Fo:Fc free: 0.946 / SU B: 26.989 / SU ML: 0.309 / Cross valid method: THROUGHOUT / ESU R Free: 0.308 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 62.471 Å2
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Refinement step | Cycle: LAST / Resolution: 2.5→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5→2.565 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Origin x: 15.9793 Å / Origin y: -20.6115 Å / Origin z: 10.5145 Å
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