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Open data
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Basic information
Entry | Database: PDB / ID: 2j7k | ||||||
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Title | Crystal structure of the T84A mutant EF-G:GDPCP complex | ||||||
![]() | ELONGATION FACTOR G | ||||||
![]() | TRANSLATION / ELONGATION FACTOR / NUCLEOTIDE-BINDING / P-LOOP / THR84ALA / MUTATION / GTP-BINDING / NUCLEOTIDE- BINDING / PROTEIN BIOSYNTHESIS | ||||||
Function / homology | ![]() 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 | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Hansson, S. / Logan, D.T. | ||||||
![]() | ![]() Title: New Insights Into the Role of the P-Loop Lysine: Implications from the Crystal Structure of a Mutant EF-G:Gdpcp Complex Authors: Hansson, S. / Logan, D.T. #1: ![]() Title: Crystal Structure of a Mutant Elongation Factor G Trapped with a GTP Analogue Authors: Hansson, S. / Singh, R. / Gudkov, A.T. / Liljas, A. / Logan, D.T. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AD" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AD" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 141.8 KB | Display | ![]() |
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PDB format | ![]() | 109.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 736.2 KB | Display | ![]() |
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Full document | ![]() | 745.3 KB | Display | |
Data in XML | ![]() | 24.6 KB | Display | |
Data in CIF | ![]() | 33.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2bm0S S: Starting model for refinement |
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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: 76947.078 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-GCP / |
#3: Chemical | ChemComp-MG / |
#4: Water | ChemComp-HOH / |
Compound details | ENGINEERED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54.11 % / Description: NONE |
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Crystal grow | pH: 7.3 Details: 17 % PEG8000 100 MM HEPES 46 MM TRIS 10 MM MGCL2 10 MM GDPCP, pH 7.3 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Feb 21, 2005 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.065 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→26 Å / Num. obs: 17014 / % possible obs: 95.4 % / Observed criterion σ(I): 2.5 / Redundancy: 7.4 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 18.6 |
Reflection shell | Resolution: 2.9→3 Å / Rmerge(I) obs: 0.47 / Mean I/σ(I) obs: 3.2 / % possible all: 98.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2BM0 Resolution: 2.9→26 Å / Cross valid method: THROUGHOUT / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. PEPTIDE BOND BETWEEN RESIDUES 85 AND 86 IS A CIS-PEPTIDE.
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Displacement parameters | Biso mean: 67.74 Å2 | ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→26 Å
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LS refinement shell | Resolution: 2.9→2.97 Å / Num. reflection Rwork: 1679 |