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Yorodumi- PDB-3kkl: Crystal structure of functionally unknown HSP33 from Saccharomyce... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3kkl | ||||||
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Title | Crystal structure of functionally unknown HSP33 from Saccharomyces cerevisiae | ||||||
Components | Probable chaperone protein HSP33 | ||||||
Keywords | HYDROLASE / peptidase / heat shock protein / Chaperone / Protease / Stress response | ||||||
Function / homology | Function and homology information D-lactate dehydratase / glyoxalase III activity / methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione / cellular response to nutrient levels / chaperone-mediated protein folding / protein folding chaperone / P-body / cytoplasm Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.03 Å | ||||||
Authors | Hwang, K.Y. / Sung, M.W. / Lee, W.H. | ||||||
Citation | Journal: To be Published Title: Crystal structure of functionally unknown HSP33 from Saccharomyces cerevisiae Authors: Hwang, K.Y. / Sung, M.W. / Lee, W.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3kkl.cif.gz | 93.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3kkl.ent.gz | 71.8 KB | Display | PDB format |
PDBx/mmJSON format | 3kkl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3kkl_validation.pdf.gz | 427.7 KB | Display | wwPDB validaton report |
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Full document | 3kkl_full_validation.pdf.gz | 444.1 KB | Display | |
Data in XML | 3kkl_validation.xml.gz | 19.4 KB | Display | |
Data in CIF | 3kkl_validation.cif.gz | 26.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kk/3kkl ftp://data.pdbj.org/pub/pdb/validation_reports/kk/3kkl | HTTPS FTP |
-Related structure data
Related structure data | 1qvzS S: Starting model for refinement |
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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: 26878.396 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Gene: HSP33, YOR391C / Plasmid: pET22b / Production host: Escherichia coli (E. coli) / References: UniProt: Q08914, Hydrolases; Glycosylases #2: 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: 1.81 Å3/Da / Density % sol: 32.18 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 0.2M Tri-sodium Citrate dihydrate, 23%(w/v) polyethylene glycol 3350, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: PAL/PLS / Beamline: 4A / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Sep 30, 2007 |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.03→50 Å / Num. obs: 24915 / % possible obs: 92.5 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 1 / Num. measured all: 109787 |
Reflection shell | Resolution: 2.03→2.1 Å / % possible all: 87.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1qvz Resolution: 2.03→19.76 Å / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 38.2 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.03→19.76 Å
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Refine LS restraints |
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