+Open data
-Basic information
Entry | Database: PDB / ID: 5b6k | ||||||
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Title | Crystal structure of Ketoreductase 1 from Candida glabrata | ||||||
Components | Uncharacterized protein CgKR1 | ||||||
Keywords | OXIDOREDUCTASE / ketoreductase | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Candida glabrata (fungus) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.701 Å | ||||||
Authors | Qin, B. / Mori, T. / Abe, I. / You, S. | ||||||
Citation | Journal: To Be Published Title: Engineering of Candida glabrata Ketoreductase 1 for Asymmetric Reduction of alpha-Halo Ketones Authors: Qin, F. / Qin, B. / Mori, T. / Wang, Y. / Meng, L. / Zhang, X. / Jia, X. / Abe, I. / You, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5b6k.cif.gz | 88.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5b6k.ent.gz | 65.3 KB | Display | PDB format |
PDBx/mmJSON format | 5b6k.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5b6k_validation.pdf.gz | 441.3 KB | Display | wwPDB validaton report |
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Full document | 5b6k_full_validation.pdf.gz | 441.6 KB | Display | |
Data in XML | 5b6k_validation.xml.gz | 16.9 KB | Display | |
Data in CIF | 5b6k_validation.cif.gz | 25.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b6/5b6k ftp://data.pdbj.org/pub/pdb/validation_reports/b6/5b6k | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 40755.969 Da / Num. of mol.: 1 / Fragment: UNP residues 8-352 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (fungus) Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65 Gene: GRE2(A), CAGL0E05170g / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta2(DE3) / References: UniProt: Q6FV31 |
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#2: Chemical | ChemComp-SO4 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.55 Å3/Da / Density % sol: 51.84 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5.6 Details: 100mM sodium citrate buffer (pH 5.5), 1995mM (NH4)2SO4 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: AR-NW12A / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 270 / Detector: CCD / Date: Feb 26, 2016 |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→50 Å / Num. obs: 44487 / % possible obs: 99.7 % / Redundancy: 7.58 % / Rmerge(I) obs: 0.052 / Net I/σ(I): 25.32 |
Reflection shell | Resolution: 1.7→1.8 Å / Redundancy: 7.37 % / Rmerge(I) obs: 0.431 / Mean I/σ(I) obs: 5.23 / % possible all: 99.7 |
-Processing
Software |
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Refinement | Resolution: 1.701→35.473 Å / SU ML: 0.15 / Cross valid method: FREE R-VALUE / σ(F): 1.38 / Phase error: 18.34
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.701→35.473 Å
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Refine LS restraints |
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LS refinement shell |
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