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- PDB-1efm: STRUCTURE OF THE GDP DOMAIN OF EF-TU AND LOCATION OF THE AMINO AC... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1efm | ||||||
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Title | STRUCTURE OF THE GDP DOMAIN OF EF-TU AND LOCATION OF THE AMINO ACIDS HOMOLOGOUS TO RAS ONCOGENE PROTEINS | ||||||
![]() | ELONGATION FACTOR TU | ||||||
![]() | ELONGATION FACTOR | ||||||
Function / homology | ![]() guanyl-nucleotide exchange factor complex / translational elongation / guanosine tetraphosphate binding / translation elongation factor activity / response to antibiotic / GTPase activity / GTP binding / RNA binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Jurnak, F. | ||||||
![]() | ![]() Title: Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins. Authors: Jurnak, F. #1: ![]() Title: Biochemical and Structural Studies of the Tetragonal Crystalline Modification of the Escherichia Coli Elongation Factor TU Authors: Jurnak, F. / McPherson, A. / Wang, A.H.J. / Rich, A. #2: ![]() Title: Preliminary X-Ray Diffraction Data for Tetragonal Crystals of Trypsinized Escherichia Coli Elongation Factor Authors: Jurnak, F. / Rich, A. / Miller, D. #3: ![]() Title: Primary Structure of Elongation Factor TU from Escherichia Coli Authors: Arai, K. / Clark, B.F.C. / Duffy, L. / Jones, M.D. / Kaziro, Y. / Laursen, R.A. / L'Italien, J. / Miller, D.L. / Nagarkatti, S. / Nakamura, S. / Nielsen, K.M. / Petersen, T.E. / Takahashi, K. / Wade, 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 | ![]() | 22.2 KB | Display | ![]() |
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PDB format | ![]() | 9.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 410.5 KB | Display | ![]() |
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Full document | ![]() | 412.3 KB | Display | |
Data in XML | ![]() | 1.9 KB | Display | |
Data in CIF | ![]() | 3.7 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: 41651.613 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-GDP / |
Compound details | TRYPSIN-MODIFIED EF-TU CONTAINS TWO MAJOR FRAGMENTS CONSISTING OF RESIDUES 1-44 AND 59-393. ...TRYPSIN-MODIFIED EF-TU CONTAINS TWO MAJOR FRAGMENTS CONSISTING |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.88 Å3/Da / Density % sol: 74.77 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4,8,14,20 and 22 ℃ / pH: 7.6 / Method: vapor diffusion, hanging drop / Details: referred to J.Mol.Biol. 185.215-217 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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Processing
Refinement | Highest resolution: 2.7 Å | ||||||||||||
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Refinement step | Cycle: LAST / Highest resolution: 2.7 Å
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