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- PDB-1lzw: Structural basis of ClpS-mediated switch in ClpA substrate recognition -
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Open data
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Basic information
Entry | Database: PDB / ID: 1lzw | ||||||
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Title | Structural basis of ClpS-mediated switch in ClpA substrate recognition | ||||||
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![]() | CHAPERONE / alpha-beta-protein (ClpS) / alpha-protein (ClpA-ND) | ||||||
Function / homology | ![]() endopeptidase Clp complex / ATP-dependent peptidase activity / molecular function inhibitor activity / protein quality control for misfolded or incompletely synthesized proteins / protein unfolding / protein catabolic process / cellular response to heat / protein-folding chaperone binding / response to heat / response to oxidative stress ...endopeptidase Clp complex / ATP-dependent peptidase activity / molecular function inhibitor activity / protein quality control for misfolded or incompletely synthesized proteins / protein unfolding / protein catabolic process / cellular response to heat / protein-folding chaperone binding / response to heat / response to oxidative stress / ATP hydrolysis activity / proteolysis / ATP binding / cytoplasm / cytosol 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 | ![]() | 60.7 KB | Display | ![]() |
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PDB format | ![]() | 44 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 434.9 KB | Display | ![]() |
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Full document | ![]() | 445.3 KB | Display | |
Data in XML | ![]() | 12.2 KB | Display | |
Data in CIF | ![]() | 15.7 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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2 | ![]()
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Unit cell |
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Components on special symmetry positions |
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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-PT / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.49 Å3/Da / Density % sol: 64.76 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 5.6 Details: 20% iPr, 20% PEG 4000, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 100K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: Dec 8, 2001 / Details: mirrors |
Radiation | Monochromator: beam collimation 100 x 100 um monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→19.69 Å / Num. obs: 14343 / % possible obs: 98.6 % / Redundancy: 5.3 % / Biso Wilson estimate: 32.1 Å2 / Rmerge(I) obs: 0.107 / Rsym value: 0.122 / Net I/σ(I): 17.9 |
Reflection shell | Highest resolution: 2.5 Å / % possible all: 98.6 |
Reflection | *PLUS Lowest resolution: 40 Å / Num. obs: 26527 / % possible obs: 98.3 % / Num. measured all: 55297 / Rmerge(I) obs: 0.11 |
Reflection shell | *PLUS % possible obs: 95.7 % / Rmerge(I) obs: 0.478 / Mean I/σ(I) obs: 1.52 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 35.8347 Å2 / ksol: 0.354532 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 46.6 Å2
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Refine analyze | Luzzati coordinate error free: 0.37 Å / Luzzati sigma a free: 0.47 Å | ||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→19.69 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5→2.66 Å / Rfactor Rfree error: 0.023 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 40 Å / Num. reflection obs: 14573 / Num. reflection Rfree: 718 / % reflection Rfree: 10 % / Rfactor Rfree: 0.269 / Rfactor Rwork: 0.241 | ||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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