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Open data
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Basic information
Entry | Database: PDB / ID: 4ued | ||||||
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Title | Complex of human eIF4E with the 4E binding protein 4E-BP1 | ||||||
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Function / homology | ![]() Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S / : / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Peter, D. / Weichenrieder, O. | ||||||
![]() | ![]() Title: Molecular Architecture of 4E-BP Translational Inhibitors Bound to Eif4E. Authors: Peter, D. / Igreja, C. / Weber, R. / Wohlbold, L. / Weiler, C. / Ebertsch, L. / Weichenrieder, O. / Izaurralde, E. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 138.5 KB | Display | ![]() |
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PDB format | ![]() | 111.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4ue8C ![]() 4ue9C ![]() 4ueaC ![]() 4uebC ![]() 4uecC ![]() 4tpwS 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: 21657.625 Da / Num. of mol.: 1 / Fragment: RESIDUES 36-217 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 4333.087 Da / Num. of mol.: 1 / Fragment: RESIDUES 50-83 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
#3: Water | ChemComp-HOH / ![]() |
Sequence details | THE FIRST FOUR RESIDUES OF CHAIN A REMAIN FROM THE EXPRESSION TAG. THE FIRST FOUR RESIDUES OF CHAIN ...THE FIRST FOUR RESIDUES OF CHAIN A REMAIN FROM THE EXPRESSION |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 42 % / Description: NONE |
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Crystal grow![]() | pH: 8.5 Details: 0.03M EACH DIETHYLENE GLYCOL, TRIETHYLENE GLYCOL, TETRAETHYLENE GLYCOL, PENTAETHYLENE GLYCOL, 0.1M BICINE/TRIZMA BASE PH 8.5, 12.5% PEG1000, 12.5% PEG3350, 12.5% MPD |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Aug 25, 2014 / Details: DYNAMICALLY BENDABLE MIRRORS |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.75→37.9 Å / Num. obs: 20595 / % possible obs: 96.9 % / Observed criterion σ(I): -3 / Redundancy: 2.9 % / Biso Wilson estimate: 24.27 Å2 / Rsym value: 0.04 / Net I/σ(I): 13.4 |
Reflection shell | Resolution: 1.75→1.8 Å / Redundancy: 2.8 % / Mean I/σ(I) obs: 2.5 / Rsym value: 0.31 / % possible all: 98.1 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 4TPW CHAIN A Resolution: 1.75→37.906 Å / SU ML: 0.2 / σ(F): 1.36 / Phase error: 24.46 / Stereochemistry target values: ML Details: HYDROGENS WERE REFINED IN THE RIDING POSITIONS. THE SIDECHAINS OF THE FOLLOWING RESIDUES WERE TRUNCATED AT C-BETA ATOMS. CHAIN B, RESIDUES 73, 74. THE FOLLOWING RESIDUES WERE MODELED AS ...Details: HYDROGENS WERE REFINED IN THE RIDING POSITIONS. THE SIDECHAINS OF THE FOLLOWING RESIDUES WERE TRUNCATED AT C-BETA ATOMS. CHAIN B, RESIDUES 73, 74. THE FOLLOWING RESIDUES WERE MODELED AS DOUBLE CONFORMATIONS. CHAIN A, RESIDUES 64, 92, 172. THE FOLLOWING RESIDUES ARE DISORDERED. CHAIN A, RESIDUES 205 TO 211.
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 32.8 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.75→37.906 Å
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Refine LS restraints |
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LS refinement shell |
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