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Open data
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Basic information
Entry | Database: PDB / ID: 1tui | ||||||
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Title | INTACT ELONGATION FACTOR TU IN COMPLEX WITH GDP | ||||||
![]() | ELONGATION FACTOR TU | ||||||
![]() | ELONGATION FACTOR / PROTEIN BIOSYNTHESIS / GTP-BINDING | ||||||
Function / homology | ![]() translation elongation factor activity / GTPase activity / GTP binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Polekhina, G. / Thirup, S. / Kjeldgaard, M. / Nissen, P. / Lippmann, C. / Nyborg, J. | ||||||
![]() | ![]() Title: Helix unwinding in the effector region of elongation factor EF-Tu-GDP. Authors: Polekhina, G. / Thirup, S. / Kjeldgaard, M. / Nissen, P. / Lippmann, C. / Nyborg, J. #1: ![]() Title: Crystal Structure of the Ternary Complex of Phe-tRNAphe, EF-TU, and a GTP Analog Authors: Nissen, P. / Kjeldgaard, M. / Thirup, S. / Polekhina, G. / Reshetnikova, L. / Clark, B.F. / Nyborg, J. #2: ![]() Title: The Crystal Structure of Elongation Factor EF-TU from Thermus Aquaticus in the GTP Conformation Authors: Kjeldgaard, M. / Nissen, P. / Thirup, S. / Nyborg, J. #3: ![]() Title: Crystal Structure of Active Elongation Factor TU Reveals Major Domain Rearrangements Authors: Berchtold, H. / Reshetnikova, L. / Reiser, C.O. / Schirmer, N.K. / Sprinzl, M. / Hilgenfeld, R. #4: ![]() Title: Refined Structure of Elongation Factor EF-TU from Escherichia Coli Authors: Kjeldgaard, M. / Nyborg, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 238.7 KB | Display | ![]() |
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PDB format | ![]() | 194.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.4 MB | Display | ![]() |
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Full document | ![]() | 1.5 MB | Display | |
Data in XML | ![]() | 55.2 KB | Display | |
Data in CIF | ![]() | 74 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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1 |
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Unit cell |
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Components
#1: Protein | Mass: 44742.980 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.72 Å3/Da / Density % sol: 66.95 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 30, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | % possible obs: 99.9 % / Redundancy: 4.1 % / Rmerge(I) obs: 0.067 |
Reflection | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 20 Å / Num. obs: 56660 |
Reflection shell | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 2.8 Å / % possible obs: 99.9 % / Num. unique obs: 5586 / Rmerge(I) obs: 0.434 |
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Processing
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Refinement | Resolution: 2.7→20 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 2.7→20 Å
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Software | *PLUS Name: TNT / Classification: refinement | |||||||||||||||
Refinement | *PLUS Rfactor obs: 0.235 / Rfactor Rfree: 0.306 | |||||||||||||||
Solvent computation | *PLUS | |||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||
Refine LS restraints | *PLUS
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