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Yorodumi- PDB-1efm: STRUCTURE OF THE GDP DOMAIN OF EF-TU AND LOCATION OF THE AMINO AC... -
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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 | ||||||
Components | ELONGATION FACTOR TUEF-Tu | ||||||
Keywords | ELONGATION FACTOR | ||||||
Function / homology | Function and homology information 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 Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.7 Å | ||||||
Authors | Jurnak, F. | ||||||
Citation | Journal: Science / Year: 1985 Title: Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins. Authors: Jurnak, F. #1: Journal: J.Biol.Chem. / Year: 1980 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: Journal: J.Mol.Biol. / Year: 1977 Title: Preliminary X-Ray Diffraction Data for Tetragonal Crystals of Trypsinized Escherichia Coli Elongation Factor Authors: Jurnak, F. / Rich, A. / Miller, D. #3: Journal: Proc.Natl.Acad.Sci.USA / Year: 1980 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1efm.cif.gz | 22.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1efm.ent.gz | 9.2 KB | Display | PDB format |
PDBx/mmJSON format | 1efm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ef/1efm ftp://data.pdbj.org/pub/pdb/validation_reports/ef/1efm | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-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.) Escherichia coli (E. coli) / References: UniProt: P02990, UniProt: P0CE48*PLUS |
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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: X-RAY DIFFRACTION |
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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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