+Open data
-Basic information
Entry | Database: PDB / ID: 2ds6 | ||||||
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Title | Structure of the ZBD in the tetragonal crystal form | ||||||
Components | ATP-dependent Clp protease ATP-binding subunit clpX | ||||||
Keywords | METAL BINDING PROTEIN / PROTEIN BINDING / substrate binding domain / zinc finger domain | ||||||
Function / homology | Function and homology information protein denaturation / HslUV protease complex / endopeptidase Clp complex / ATP-dependent peptidase activity / protein unfolding / proteolysis involved in protein catabolic process / ATP-dependent protein folding chaperone / disordered domain specific binding / unfolded protein binding / protease binding ...protein denaturation / HslUV protease complex / endopeptidase Clp complex / ATP-dependent peptidase activity / protein unfolding / proteolysis involved in protein catabolic process / ATP-dependent protein folding chaperone / disordered domain specific binding / unfolded protein binding / protease binding / protein dimerization activity / cell division / ATP hydrolysis activity / zinc ion binding / ATP binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Park, E.Y. / Lee, B.G. / Hong, S.B. / Song, H.K. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2007 Title: Structural Basis of SspB-tail Recognition by the Zinc Binding Domain of ClpX. Authors: Park, E.Y. / Lee, B.G. / Hong, S.B. / Kim, H.W. / Jeon, H. / Song, H.K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ds6.cif.gz | 29.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ds6.ent.gz | 19.5 KB | Display | PDB format |
PDBx/mmJSON format | 2ds6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2ds6_validation.pdf.gz | 435 KB | Display | wwPDB validaton report |
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Full document | 2ds6_full_validation.pdf.gz | 435.4 KB | Display | |
Data in XML | 2ds6_validation.xml.gz | 6.5 KB | Display | |
Data in CIF | 2ds6_validation.cif.gz | 8.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ds/2ds6 ftp://data.pdbj.org/pub/pdb/validation_reports/ds/2ds6 | HTTPS FTP |
-Related structure data
Related structure data | 2ds5SC 2ds7C 2ds8C S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 5758.631 Da / Num. of mol.: 2 / Fragment: Zinc binding domain(ZBD) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: pET-15b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P0A6H1 #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.53 Å3/Da / Density % sol: 51.39 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: 100mM tri-sodium citrate, pH 5.6, 2% ethyleneimine polymer, 500mM NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Nov 30, 2003 / Details: mirrors |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→50 Å / Num. obs: 7652 / % possible obs: 94.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 2→2.03 Å / % possible all: 64.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2DS5 Resolution: 2→50 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.04 Å / Rfactor Rfree error: 0.0593 /
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