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Open data
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Basic information
Entry | Database: PDB / ID: 5lp6 | |||||||||
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Title | Crystal structure of Tubulin-Stathmin-TTL-Thiocolchicine Complex | |||||||||
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![]() | STRUCTURAL PROTEIN / Microtubules / thiocolchicine / tubulin / tubulin-tyrosine ligase | |||||||||
Function / homology | ![]() tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / microtubule-based process / regulation of microtubule polymerization or depolymerization / tubulin binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / spindle microtubule / structural constituent of cytoskeleton ...tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / microtubule-based process / regulation of microtubule polymerization or depolymerization / tubulin binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / spindle microtubule / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron projection development / microtubule cytoskeleton / nervous system development / mitotic cell cycle / growth cone / microtubule / neuron projection / protein heterodimerization activity / nucleotide binding / GTPase activity / GTP binding / Golgi apparatus / metal ion binding / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Marangon, J. / Christodoulou, M. / Casagrande, F. / Tiana, G. / Dalla Via, L. / Aliverti, A. / Passarella, D. / Cappelletti, G. / Ricagno, S. | |||||||||
![]() | ![]() Title: Tools for the rational design of bivalent microtubule-targeting drugs. Authors: Marangon, J. / Christodoulou, M.S. / Casagrande, F.V. / Tiana, G. / Dalla Via, L. / Aliverti, A. / Passarella, D. / Cappelletti, G. / Ricagno, S. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 442.7 KB | Display | ![]() |
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PDB format | ![]() | 349.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2 MB | Display | ![]() |
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Full document | ![]() | 2 MB | Display | |
Data in XML | ![]() | 72.6 KB | Display | |
Data in CIF | ![]() | 98.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4o2bS 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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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS ensembles :
NCS oper:
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Components
-Protein , 4 types, 6 molecules ACBDEF
#1: Protein | Mass: 48966.324 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Protein | Mass: 49999.887 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #3: Protein | | Mass: 16844.162 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Stretches between 1-3; 28-42;141-144 were not traceable in the electron density Source: (gene. exp.) ![]() ![]() ![]() ![]() #4: Protein | | Mass: 44378.496 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Stretches between 103-124; 154-160;177-179; 364- 371; 382-385 were not traceable in the electron density Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 8 types, 105 molecules ![](data/chem/img/GTP.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/GDP.gif)
![](data/chem/img/MES.gif)
![](data/chem/img/71P.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/GDP.gif)
![](data/chem/img/MES.gif)
![](data/chem/img/71P.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
#5: Chemical | #6: Chemical | ChemComp-MG / #7: Chemical | ChemComp-CL / | #8: Chemical | #9: Chemical | ChemComp-MES / | #10: Chemical | ChemComp-71P / ~{ | #11: Chemical | ChemComp-CA / | #12: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.32 Å3/Da / Density % sol: 47 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, hanging drop Details: Crystals grew overnight in precipitant solution consisting of 6.5% (v/v) polyethylene glycol 4000, 4% (v/v) glycerol, 0.1 M MES, 30 mM CaCl2 and 30 mM MgCl2 (pH 6.6) reaching their maximum ...Details: Crystals grew overnight in precipitant solution consisting of 6.5% (v/v) polyethylene glycol 4000, 4% (v/v) glycerol, 0.1 M MES, 30 mM CaCl2 and 30 mM MgCl2 (pH 6.6) reaching their maximum dimensions within few days |
-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER R 4M / Detector: PIXEL / Date: Dec 4, 2015 |
Radiation | Monochromator: Si (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97895 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→58.85 Å / Num. obs: 65141 / % possible obs: 99.8 % / Redundancy: 13.3 % / Rmerge(I) obs: 0.128 / Net I/σ(I): 17.4 |
Reflection shell | Resolution: 2.9→3.06 Å / Redundancy: 13.5 % / Rmerge(I) obs: 1.428 / Mean I/σ(I) obs: 1.9 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4O2B Resolution: 2.9→58.85 Å / Cor.coef. Fo:Fc: 0.911 / Cor.coef. Fo:Fc free: 0.88 / SU B: 25.752 / SU ML: 0.466 / Cross valid method: THROUGHOUT / ESU R Free: 0.481 / 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: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 76.372 Å2
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Refinement step | Cycle: 1 / Resolution: 2.9→58.85 Å
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Refine LS restraints |
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