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Open data
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Basic information
Entry | Database: PDB / ID: 2bup | ||||||
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Title | T13G Mutant of the ATPASE fragment of Bovine HSC70 | ||||||
![]() | Heat shock cognate 71 kDa protein | ||||||
![]() | ![]() ![]() ![]() | ||||||
Function / homology | ![]() Regulation of HSF1-mediated heat shock response / Attenuation phase / HSF1-dependent transactivation / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Sousa, M.C. / Mckay, D.B. | ||||||
![]() | ![]() Title: The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change. Authors: Sousa, M.C. / McKay, D.B. #1: ![]() Title: How Potassium Affects the Activity of the Molecular Chaperone Hsc70. II. Potassium Binds Specifically in the ATPase Active Site Authors: Wilbanks, S.M. / McKay, D.B. #2: ![]() Title: How Potassium Affects the Activity of the Molecular Chaperone Hsc70. I. Potassium is Required for Optimal ATPase Activity Authors: O'Brien, M.C. / McKay, D.B. #3: ![]() Title: Structural Basis of the 70-kilodalton Heat Shock Cognate Protein ATP Hydrolytic Activity. II. Structure of the Active Site with ADP or ATP Bound to Wild Type and Mutant ATPase Fragment. Authors: Flaherty, K.M. / Wilbanks, S.M. / Deluca-Flaherty, C. / McKay, D.B. #4: ![]() Title: Three-Dimensional Structure of the ATPase Fragment of a 70K Heat-Shock Cognate Protein Authors: Flaherty, K.M. / Deluca-Flaherty, C. / McKay, D.B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 101.2 KB | Display | ![]() |
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PDB format | ![]() | 73.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 41951.473 Da / Num. of mol.: 1 / Fragment: ATPASE / Mutation: T13G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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-Non-polymers , 7 types, 443 molecules ![](data/chem/img/PO4.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/K.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/ADP.gif)
![](data/chem/img/ATP.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/K.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/ADP.gif)
![](data/chem/img/ATP.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-PO4 / ![]() | ||||||||
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#3: Chemical | ChemComp-MG / | ||||||||
#4: Chemical | #5: Chemical | ![]() #6: Chemical | ChemComp-ADP / | ![]() #7: Chemical | ChemComp-ATP / | ![]() #8: Water | ChemComp-HOH / | ![]() |
-Details
Compound details | THE ACTIVE SITE CONTAINS A MIXTURE OF TWO GROUPS OF ATOMS. GROUP 1 IS FORMED BY ADP 486, PI 488 AND ...THE ACTIVE SITE CONTAINS A MIXTURE OF TWO GROUPS OF ATOMS. GROUP 1 IS FORMED BY ADP 486, PI 488 AND HOH 545 AND HAS AN ACCOPANCY OF 0.6. GROUP TWO IS ATP 489 AND HOH 1119 WITH AN OCCUPANCY OF 0.4 |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.54 Å3/Da / Density % sol: 51.55 % | ||||||||||||||||||||||||||||||
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Crystal grow![]() | pH: 9 / Details: pH 9.0 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MACSCIENCE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.7→100 Å / Num. obs: 46807 / % possible obs: 97.4 % / Redundancy: 4 % / Biso Wilson estimate: 17.8 Å2 / Rmerge(I) obs: 0.058 / Rsym value: 0.058 |
Reflection shell | Resolution: 1.7→1.76 Å / Rsym value: 0.14 / % possible all: 89.5 |
Reflection | *PLUS Num. measured all: 167988 |
Reflection shell | *PLUS % possible obs: 89.5 % / Rmerge(I) obs: 0.14 |
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Processing
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Refinement | Method to determine structure![]()
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Displacement parameters | Biso mean: 17.1 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.7→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.7→1.81 Å / Rfactor Rfree error: 0.01 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: CNS / Version: 0.3 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 30 Å / σ(F): 0 / % reflection Rfree: 10 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 17.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.264 / % reflection Rfree: 10 % / Rfactor Rwork: 0.222 |