+Open data
-Basic information
Entry | Database: PDB / ID: 5zfm | |||||||||
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Title | Ketoreductase LbCR mutant - M6 | |||||||||
Components | 3-oxoacyl-acyl carrier protein reductase | |||||||||
Keywords | OXIDOREDUCTASE / ketoreductase / short-chain dehydrogenase/reductase (SDR) | |||||||||
Function / homology | Function and homology information | |||||||||
Biological species | Lactobacillus brevis (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | |||||||||
Authors | Gong, X.M. / Zheng, G.W. / Xu, J.H. | |||||||||
Funding support | China, 2items
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Citation | Journal: Acs Catalysis / Year: 2019 Title: Development of an Engineered Ketoreductase with Simultaneously Improved Thermostability and Activity for Making a Bulky Atorvastatin Precursor Authors: Gong, X.M. / Zhen, Q. / Li, F.L. / Zeng, B.B. / Zheng, G.W. / Xu, J.H. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5zfm.cif.gz | 220.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5zfm.ent.gz | 172.7 KB | Display | PDB format |
PDBx/mmJSON format | 5zfm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5zfm_validation.pdf.gz | 458.8 KB | Display | wwPDB validaton report |
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Full document | 5zfm_full_validation.pdf.gz | 461.7 KB | Display | |
Data in XML | 5zfm_validation.xml.gz | 47 KB | Display | |
Data in CIF | 5zfm_validation.cif.gz | 71.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zf/5zfm ftp://data.pdbj.org/pub/pdb/validation_reports/zf/5zfm | HTTPS FTP |
-Related 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: 29553.455 Da / Num. of mol.: 4 / Mutation: M154A,A155D,A201D,A202L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Lactobacillus brevis (strain ATCC 367 / JCM 1170) (bacteria) Strain: ATCC 367 / JCM 1170 / Gene: LVIS_0330 Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) References: UniProt: Q03TH6 #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: 2.33 Å3/Da / Density % sol: 47.25 % |
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Crystal grow | Temperature: 291.15 K / Method: vapor diffusion, sitting drop Details: PEG 4000, MES buffer, sodium chloride, glycyl-glycyl-glycine |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.97775 Å |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jun 9, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97775 Å / Relative weight: 1 |
Reflection | Resolution: 2→44.28 Å / Num. obs: 72544 / % possible obs: 99.08 % / Redundancy: 6.6 % / Rmerge(I) obs: 0.197 / Net I/σ(I): 10.143 |
Reflection shell | Resolution: 2→2.071 Å / Rmerge(I) obs: 0.516 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→44.278 Å / SU ML: 0.2 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 19.62
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→44.278 Å
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Refine LS restraints |
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LS refinement shell |
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