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Yorodumi- PDB-1efg: THE CRYSTAL STRUCTURE OF ELONGATION FACTOR G COMPLEXED WITH GDP, ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1efg | ||||||
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Title | THE CRYSTAL STRUCTURE OF ELONGATION FACTOR G COMPLEXED WITH GDP, AT 2.7 ANGSTROMS RESOLUTION | ||||||
Components | (ELONGATION FACTOR G) x 3 | ||||||
Keywords | ELONGATION FACTOR | ||||||
Function / homology | Function and homology information ribosome disassembly / translational elongation / translation elongation factor activity / GDP binding / ribosome binding / GTPase activity / GTP binding / magnesium ion binding / cytosol Similarity search - Function | ||||||
Biological species | Thermus thermophilus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.7 Å | ||||||
Authors | Czworkowski, J. / Wang, J. / Steitz, T.A. / Moore, P.B. | ||||||
Citation | Journal: EMBO J. / Year: 1994 Title: The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution. Authors: Czworkowski, J. / Wang, J. / Steitz, T.A. / Moore, P.B. #1: Journal: Nucleic Acids Res. / Year: 1989 Title: Nucleotide Sequence of the Thermus Thermophilus Hb8 Gene Coding for Elongation Factor G Authors: Yakhnin, A.V. / Vorozheykina, D.P. / Matvienko, N.I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1efg.cif.gz | 35.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1efg.ent.gz | 17.7 KB | Display | PDB format |
PDBx/mmJSON format | 1efg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1efg_validation.pdf.gz | 414.4 KB | Display | wwPDB validaton report |
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Full document | 1efg_full_validation.pdf.gz | 415.5 KB | Display | |
Data in XML | 1efg_validation.xml.gz | 1.5 KB | Display | |
Data in CIF | 1efg_validation.cif.gz | 7.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ef/1efg ftp://data.pdbj.org/pub/pdb/validation_reports/ef/1efg | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 76963.078 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: P13551, UniProt: Q5SHN5*PLUS |
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#2: Protein/peptide | Mass: 3081.790 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 |
#3: Protein/peptide | Mass: 2400.951 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB8 |
#4: Chemical | ChemComp-GDP / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.87 Å3/Da / Density % sol: 57.17 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / pH: 7.8 / Details: pH 7.8, temperature 277K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 26380 / % possible obs: 97.6 % |
-Processing
Software |
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Refinement | Resolution: 2.7→10 Å / σ(F): 2 Details: AN OVERALL TEMPERATURE FACTOR HAS BEEN DETERMINED FOR EACH OF THE FIVE DOMAINS.
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Displacement parameters | Biso mean: 33.18 Å2 | ||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.45 Å | ||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.7→10 Å
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.267 / Rfactor Rfree: 0.396 / Rfactor Rwork: 0.267 | ||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||
Displacement parameters | *PLUS |