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Yorodumi- PDB-1ejw: CRYSTAL STRUCTURE OF WILD-TYPE KLEBSIELLA AEROGENES UREASE AT 298K -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ejw | ||||||
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Title | CRYSTAL STRUCTURE OF WILD-TYPE KLEBSIELLA AEROGENES UREASE AT 298K | ||||||
Components |
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Keywords | HYDROLASE / alpha-beta barrel / nickel metalloenzyme | ||||||
Function / homology | Function and homology information urease complex / urease / urease activity / urea catabolic process / nickel cation binding / cytoplasm Similarity search - Function | ||||||
Biological species | Klebsiella aerogenes (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.9 Å | ||||||
Authors | Pearson, M.A. / Karplus, P.A. | ||||||
Citation | Journal: To be Published Title: Crystal Structure of Wild-type Klebsiella aerogenes Urease at 298K Authors: Pearson, M.A. / Karplus, P.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ejw.cif.gz | 162.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ejw.ent.gz | 131.3 KB | Display | PDB format |
PDBx/mmJSON format | 1ejw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ejw_validation.pdf.gz | 445.5 KB | Display | wwPDB validaton report |
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Full document | 1ejw_full_validation.pdf.gz | 458.8 KB | Display | |
Data in XML | 1ejw_validation.xml.gz | 33.4 KB | Display | |
Data in CIF | 1ejw_validation.cif.gz | 48.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ej/1ejw ftp://data.pdbj.org/pub/pdb/validation_reports/ej/1ejw | HTTPS FTP |
-Related structure data
Related structure data | |
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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: 60409.352 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Klebsiella aerogenes (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P18314, urease | ||
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#2: Protein | Mass: 11125.690 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Klebsiella aerogenes (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P18315, urease | ||
#3: Protein | Mass: 11100.928 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Klebsiella aerogenes (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P18316, urease | ||
#4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 23 |
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-Sample preparation
Crystal | Density Matthews: 2.51 Å3/Da / Density % sol: 51.02 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: lithium sulfate, Hepes, EDTA, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: F1 / Wavelength: 0.918 |
Detector | Type: PRINCETON 2K / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.918 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→100 Å / Num. obs: 59435 / % possible obs: 95 % / Redundancy: 4.7 % / Rmerge(I) obs: 0.132 |
Reflection shell | Highest resolution: 1.9 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.339 / % possible all: 89 |
-Processing
Software |
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Refinement | Resolution: 1.9→10 Å
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Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
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