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Open data
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Basic information
Entry | Database: PDB / ID: 3t1q | ||||||
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Title | MglA bound to GppNHp in complex with MglB | ||||||
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![]() | HYDROLASE/SIGNALING PROTEIN / G domain containing protein / bacterial GTPase / Bacterial Polarity / Motility / GTPase activating protein / alpha/beta proteins / homodimer / Pole localisation / HYDROLASE-SIGNALING PROTEIN complex | ||||||
Function / homology | ![]() positive regulation of TOR signaling / guanyl-nucleotide exchange factor activity / cellular response to amino acid stimulus / molecular adaptor activity / GTPase activity / GTP binding / identical protein binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Miertzschke, M. / Vetter, I.R. / Koerner, C. / Wittinghofer, A. | ||||||
![]() | ![]() Title: Structural analysis of the Ras-like G protein MglA and its cognate GAP MglB and implications for bacterial polarity. Authors: Miertzschke, M. / Koerner, C. / Vetter, I.R. / Keilberg, D. / Hot, E. / Leonardy, S. / Sogaard-Andersen, L. / Wittinghofer, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 100.7 KB | Display | ![]() |
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PDB format | ![]() | 75.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 774.9 KB | Display | ![]() |
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Full document | ![]() | 781 KB | Display | |
Data in XML | ![]() | 18.7 KB | Display | |
Data in CIF | ![]() | 25.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3t12C ![]() 3t1oC ![]() 3t1rC ![]() 3t1sC ![]() 3t1tC ![]() 3t1vC ![]() 3t1xC ![]() 1j3wS C: citing same article ( 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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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 21999.305 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||||
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#2: Protein | Mass: 14326.399 Da / Num. of mol.: 2 / Fragment: UNP residues 6-139 / Mutation: E14A, R15A, G65S, R124A, E127A, R131A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Chemical | ChemComp-GNP / | #4: Chemical | ChemComp-MG / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.15 Å3/Da / Density % sol: 60.95 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 1.25M LiCl, 0.1M Hepes, 15% PEG 6000 , pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.15K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Date: Nov 30, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8726 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→45.18 Å / Num. all: 18013 / Num. obs: 17955 / % possible obs: 99.7 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 |
Reflection shell | Resolution: 2.7→2.85 Å / % possible all: 99.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1J3W Resolution: 2.7→45.18 Å / Cor.coef. Fo:Fc: 0.939 / Cor.coef. Fo:Fc free: 0.897 / SU B: 11.416 / SU ML: 0.236 / Cross valid method: THROUGHOUT / ESU R Free: 0.334 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 39.684 Å2
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Refinement step | Cycle: LAST / Resolution: 2.7→45.18 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.7→2.77 Å / Total num. of bins used: 20
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