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- PDB-1mg9: The structural basis of ClpS-mediated switch in ClpA substrate re... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1mg9 | ||||||
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Title | The structural basis of ClpS-mediated switch in ClpA substrate recognition | ||||||
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![]() | CHAPERONE / AAA+ATPASE / SUBSTRATE SENSOR | ||||||
Function / homology | ![]() endopeptidase Clp complex / molecular function inhibitor activity / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / protein unfolding / protein catabolic process / protein-folding chaperone binding / cellular response to heat / response to heat / response to oxidative stress ...endopeptidase Clp complex / molecular function inhibitor activity / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / protein unfolding / protein catabolic process / protein-folding chaperone binding / cellular response to heat / response to heat / response to oxidative stress / ATP hydrolysis activity / proteolysis / ATP binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Zeth, K. / Ravelli, R.B. / Paal, K. / Cusack, S. / Bukau, B. / Dougan, D.A. | ||||||
![]() | ![]() Title: Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA Authors: Zeth, K. / Ravelli, R.B. / Paal, K. / Cusack, S. / Bukau, B. / Dougan, D.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 | ![]() | 58.3 KB | Display | ![]() |
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PDB format | ![]() | 42.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1lzwSC S: Starting model for refinement C: citing same article ( |
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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
#1: Protein | Mass: 12125.969 Da / Num. of mol.: 1 / Mutation: H66A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein | Mass: 16573.650 Da / Num. of mol.: 1 / Fragment: Residues 1-146 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#3: Chemical | ChemComp-SPK / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.01 Å3/Da / Density % sol: 59.17 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7 Details: i-PR, PEG8000, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 18K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 278 K / pH: 7.5 / Details: Zeth, K., (2002) Acta Crystallogr., D58, 1207. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: ADSC QUANTUM 4 / Detector: CCD / Date: Oct 6, 2001 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→28.71 Å / Num. obs: 28962 / Observed criterion σ(I): 0 / Redundancy: 5 % / Biso Wilson estimate: 31.1 Å2 |
Reflection | *PLUS Lowest resolution: 20 Å / Num. obs: 28042 / % possible obs: 94.5 % / Num. measured all: 75277 / Rmerge(I) obs: 0.082 |
Reflection shell | *PLUS % possible obs: 96.8 % / Rmerge(I) obs: 0.272 / Mean I/σ(I) obs: 2.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1LZW Resolution: 2.3→28.72 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 422671.97 / Data cutoff high rms absF: 422671.97 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 24.2356 Å2 / ksol: 0.30147 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 47.2 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.3→28.72 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.3→2.44 Å / Rfactor Rfree error: 0.024 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 20 Å / Num. reflection obs: 15214 / Num. reflection Rfree: 1423 / % reflection Rfree: 10 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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