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Yorodumi- PDB-1etu: STRUCTURAL DETAILS OF THE BINDING OF GUANOSINE DIPHOSPHATE TO ELO... -
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-Basic information
Entry | Database: PDB / ID: 1etu | ||||||
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Title | STRUCTURAL DETAILS OF THE BINDING OF GUANOSINE DIPHOSPHATE TO ELONGATION FACTOR TU FROM E. COLI AS STUDIED BY X-RAY CRYSTALLOGRAPHY | ||||||
Components | ELONGATION FACTOR TUEF-Tu | ||||||
Keywords | TRANSPORT AND PROTECTION PROTEIN | ||||||
Function / homology | Function and homology information guanyl-nucleotide exchange factor complex / guanosine tetraphosphate binding / translational elongation / 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: 2.9 Å | ||||||
Authors | Clark, B.F.C. / Lacour, T.F.M. / Kjeldgaard, M. / Morikawa, K. / Nyborg, J. / Rubin, R. / Thirup, S. | ||||||
Citation | Journal: EMBO J. / Year: 1985 Title: Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography. Authors: la Cour, T.F. / Nyborg, J. / Thirup, S. / Clark, B.F. #1: Journal: Science / Year: 1985 Title: A Model for the Tertiary Structure of P21, the Product of the Ras Oncogene Authors: Mccormick, F. / Clark, B.F.C. / Lacour, T.F.M. / Kjeldgaard, M. / Norskov-Lauritsen, L. / Nyborg, J. #2: Journal: Gene Expression. The Translational Step and its Control Year: 1984 Title: Structure of Bacterial Elongation Factor EF-TU and its Interaction with Aminoacyl-tRNA Authors: Clark, B.F.C. / Lacour, T.F.M. / Nielsen, K.M. / Nyborg, J. / Petersen, H.U. / Siboska, G.E. / Wikman, F.P. #3: Journal: FEBS Lett. / Year: 1981 Title: Structural Features of the Gdp Binding Site of Elongation Factor TU from Escherichia Coli as Determined by X-Ray Diffraction Authors: Rubin, J.R. / Morikawa, K. / Nyborg, J. / Lacour, T.F.M. / Clark, B.F.C. / Miller, D.L. #4: Journal: J.Mol.Biol. / Year: 1978 Title: High Resolution X-Ray Crystallographic Analysis of a Modified Form of the Elongation Factor TU(Colon) Guanosine Diphosphate Complex Authors: Morikawa, K. / Lacour, T.F.M. / Nyborg, J. / Rasmussen, K.M. / Miller, D.L. / Clark, B.F.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1etu.cif.gz | 47.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1etu.ent.gz | 34.1 KB | Display | PDB format |
PDBx/mmJSON format | 1etu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/et/1etu ftp://data.pdbj.org/pub/pdb/validation_reports/et/1etu | 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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Atom site foot note | 1: SEE REMARK 5. |
-Components
#1: Protein | Mass: 43209.270 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P0A6N1, UniProt: P0CE47*PLUS |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-GDP / |
Sequence details | EF-TU IS CODED FOR BY TWO DIFFERENT GENES. THE SEQUENCE STRUCTURE ANALYSIS CARRIED OUT ON THIS ...EF-TU IS CODED FOR BY TWO DIFFERENT GENES. THE SEQUENCE STRUCTURE ANALYSIS CARRIED OUT ON THIS MIXTURE SHOWS THAT THE C-TERMINAL RESIDUE OCCURS AS GLY/SER IN THE RATIO OF 3/1. THIS RESIDUE IS IDENTIFIED |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 4.6 Å3/Da / Density % sol: 73.26 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7 / Method: vapor diffusion / Details: referred to J.Mol.Biol. 125.325-338 | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Processing
Refinement | Highest resolution: 2.9 Å Details: ATOMS WITH AN OCCUPANCY OF 0.0 ARE POORLY DEFINED IN THE DENSITY. | ||||||||||||
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Refinement step | Cycle: LAST / Highest resolution: 2.9 Å
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