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Open data
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Basic information
Entry | Database: PDB / ID: 1hu3 | ||||||
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Title | MIDDLE DOMAIN OF HUMAN EIF4GII | ||||||
![]() | EIF4GII | ||||||
![]() | TRANSLATION / eIF4G / HEAT repeat | ||||||
Function / homology | ![]() RNA cap binding / eukaryotic translation initiation factor 4F complex / translation factor activity, RNA binding / regulation of translational initiation / translation initiation factor activity / ISG15 antiviral mechanism / mRNA binding / RNA binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Marcotrigiano, J. / Lomakin, I. / Pestova, T.V. / Hellen, C.U.T. / Sonenberg, N. / Burley, S.K. | ||||||
![]() | ![]() Title: A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery. Authors: Marcotrigiano, J. / Lomakin, I.B. / Sonenberg, N. / Pestova, T.V. / Hellen, C.U. / Burley, S.K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 51.8 KB | Display | ![]() |
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PDB format | ![]() | 40.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 425.7 KB | Display | ![]() |
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Full document | ![]() | 431.3 KB | Display | |
Data in XML | ![]() | 10.9 KB | Display | |
Data in CIF | ![]() | 14.3 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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Unit cell |
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Components
#1: Protein | Mass: 30826.410 Da / Num. of mol.: 1 / Fragment: RESIDUES 745-1003 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.56 Å3/Da / Density % sol: 52.02 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: 0.1M acetate (4.6), 0.1M ammonium acetate, 20-22% PEG4000, and 5mM tris(carboxyethyl)phosphine, VAPOR DIFFUSION, HANGING DROP, temperature 277K | |||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: BRANDEIS - B4 / Detector: CCD / Date: Jun 28, 2000 |
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97928 Å / Relative weight: 1 |
Reflection | Resolution: 2.37→20 Å / Num. all: 170724 / Num. obs: 12425 / % possible obs: 97.5 % / Observed criterion σ(I): 4 / Redundancy: 4 % / Rmerge(I) obs: 0.044 |
Reflection shell | Resolution: 2.37→2.45 Å / Redundancy: 3 % / Rmerge(I) obs: 0.195 / % possible all: 85 |
Reflection | *PLUS Lowest resolution: 20 Å / Num. measured all: 170724 |
Reflection shell | *PLUS % possible obs: 85 % |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 2.37→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.37→2.39 Å
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Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 20 Å / σ(F): 2 / % reflection Rfree: 10 % / Rfactor obs: 0.239 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS Type: c_angle_deg / Dev ideal: 1.7 | ||||||||||||||||||||
LS refinement shell | *PLUS Rfactor Rfree: 0.328 / Rfactor Rwork: 0.317 |