+Open data
-Basic information
Entry | Database: PDB / ID: 1uc4 | |||||||||
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Title | Structure of diol dehydratase complexed with (S)-1,2-propanediol | |||||||||
Components | (diol dehydrase ...) x 3 | |||||||||
Keywords | LYASE / ALPHA/BETA BARREL | |||||||||
Function / homology | Function and homology information propanediol dehydratase / propanediol dehydratase activity / cobalamin binding / metal ion binding Similarity search - Function | |||||||||
Biological species | Klebsiella oxytoca (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | |||||||||
Authors | Shibata, N. / Nakanishi, Y. / Fukuoka, M. / Yamanishi, M. / Yasuoka, N. / Toraya, T. | |||||||||
Citation | Journal: J.BIOL.CHEM. / Year: 2003 Title: Structural rationalization for the lack of stereospecificity in coenzyme B12-dependent diol dehydratase Authors: Shibata, N. / Nakanishi, Y. / Fukuoka, M. / Yamanishi, M. / Yasuoka, N. / Toraya, T. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1uc4.cif.gz | 383.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1uc4.ent.gz | 303.2 KB | Display | PDB format |
PDBx/mmJSON format | 1uc4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uc/1uc4 ftp://data.pdbj.org/pub/pdb/validation_reports/uc/1uc4 | HTTPS FTP |
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-Related structure data
Related structure data | 1uc5C 1egmS 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
-Diol dehydrase ... , 3 types, 6 molecules ALBEGM
#1: Protein | Mass: 60408.133 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Klebsiella oxytoca (bacteria) / Plasmid: pUSI2E / Production host: Escherichia coli (E. coli) / References: UniProt: Q59470, propanediol dehydratase #2: Protein | Mass: 24141.678 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Klebsiella oxytoca (bacteria) / Plasmid: pUSI2E / Production host: Escherichia coli (E. coli) / References: UniProt: Q59471, propanediol dehydratase #3: Protein | Mass: 19198.695 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Klebsiella oxytoca (bacteria) / Plasmid: pUSI2E / Production host: Escherichia coli (E. coli) / References: UniProt: Q59472, propanediol dehydratase |
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-Non-polymers , 5 types, 1421 molecules
#4: Chemical | ChemComp-NH4 / #5: Chemical | #6: Chemical | #7: Chemical | #8: 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: 2.25 Å3/Da / Density % sol: 44.82 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 278 K / Method: vapor diffusion / pH: 8 Details: PEG6000, ammonium sulfate, Tris, (S)-1,2,-propanediol, pH 8.0, VAPOR DIFFUSION, temperature 278K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: sandwich-drop vapor diffusion | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 0.708 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Apr 14, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.708 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→50 Å / % possible obs: 87.3 % / Observed criterion σ(F): 0 / Rmerge(I) obs: 0.055 |
Reflection shell | Resolution: 1.8→1.86 Å / Rmerge(I) obs: 0.119 / % possible all: 0.671 |
Reflection | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 30 Å / Num. obs: 152278 / Num. measured all: 1991323 |
Reflection shell | *PLUS % possible obs: 67.1 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1EGM Resolution: 1.8→36.92 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.8→36.92 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement | *PLUS Lowest resolution: 30 Å / Rfactor Rfree: 0.23 | |||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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