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- PDB-1k6k: Crystal Structure of ClpA, an AAA+ Chaperone-like Regulator of Cl... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1k6k | ||||||
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Title | Crystal Structure of ClpA, an AAA+ Chaperone-like Regulator of ClpAP protease implication to the functional difference of two ATPase domains | ||||||
![]() | ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA | ||||||
![]() | HYDROLASE / ClpA / chaperone / ATPase / adaptor binding / N-domain | ||||||
Function / homology | ![]() endopeptidase Clp complex / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / protein unfolding / cellular response to heat / response to oxidative stress / ATP hydrolysis activity / ATP binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Guo, F. / Maurizi, M.R. / Esser, L. / Xia, D. | ||||||
![]() | ![]() Title: Crystal structure of ClpA, an HSP100 chaperone and regulator of ClpAP protease Authors: Guo, F. / Maurizi, M.R. / Esser, L. / Xia, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 39.9 KB | Display | ![]() |
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PDB format | ![]() | 28.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 364.8 KB | Display | ![]() |
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Full document | ![]() | 368.2 KB | Display | |
Data in XML | ![]() | 4.2 KB | Display | |
Data in CIF | ![]() | 6.1 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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Unit cell |
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Components
#1: Protein | Mass: 16200.268 Da / Num. of mol.: 1 / Fragment: N-terminal, residues 1-143 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.88 Å3/Da / Density % sol: 34.59 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, hanging drop / pH: 7 / Details: VAPOR DIFFUSION, HANGING DROP, pH 7.0 at 294K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 21.5-22.5 ℃ / pH: 7.5 | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||
Radiation wavelength | Relative weight: 1 | ||||||||||||||||||||
Reflection | Resolution: 1.8→14 Å / Num. obs: 7959 / % possible obs: 67.4 % / Observed criterion σ(I): 0 | ||||||||||||||||||||
Reflection | *PLUS Lowest resolution: 14 Å / Num. obs: 7990 / % possible obs: 67.2 % / Rmerge(I) obs: 0.028 | ||||||||||||||||||||
Reflection shell | *PLUS % possible obs: 21.1 % / Rmerge(I) obs: 0.199 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: ClpA N-domain Resolution: 1.8→14 Å / Cross valid method: THROUGHOUT /
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Refinement step | Cycle: LAST / Resolution: 1.8→14 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 40 Å / Rfactor Rfree: 0.263 / Rfactor Rwork: 0.214 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.336 / Rfactor Rwork: 0.283 |