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Open data
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Basic information
Entry | Database: PDB / ID: 1kax | ||||||
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Title | 70KD HEAT SHOCK COGNATE PROTEIN ATPASE DOMAIN, K71M MUTANT | ||||||
![]() | 70KD HEAT SHOCK COGNATE PROTEIN | ||||||
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Function / homology | ![]() synaptic vesicle uncoating / chaperone-mediated autophagy translocation complex disassembly / slow axonal transport / clathrin-uncoating ATPase activity / protein targeting to lysosome involved in chaperone-mediated autophagy / late endosomal microautophagy / presynaptic cytosol / Prp19 complex / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | O'Brien, M.C. / Flaherty, K.M. / Mckay, D.B. | ||||||
![]() | ![]() Title: Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis. Authors: O'Brien, M.C. / Flaherty, K.M. / 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: 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. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 94.9 KB | Display | ![]() |
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PDB format | ![]() | 73.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 453.1 KB | Display | ![]() |
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Full document | ![]() | 455.8 KB | Display | |
Data in XML | ![]() | 9.1 KB | Display | |
Data in CIF | ![]() | 16.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-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: 41997.539 Da / Num. of mol.: 1 / Fragment: ATPASE DOMAIN / Mutation: K71M Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 5 types, 445 molecules 








#2: Chemical | ![]() #3: Chemical | ChemComp-MG / | #4: Chemical | #5: Chemical | ChemComp-ATP / | ![]() #6: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.56 Å3/Da / Density % sol: 51.87 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop / PH range low: 10 / PH range high: 6 | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: RIGAKU / Detector: IMAGE PLATE |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Num. obs: 38288 / % possible obs: 81 % / Observed criterion σ(I): 2 / Redundancy: 3 % / Rmerge(I) obs: 0.033 |
Reflection | *PLUS Highest resolution: 1.7 Å / Num. measured all: 116095 |
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Processing
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Refinement | Resolution: 1.7→6 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 1.7→6 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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