+Open data
-Basic information
Entry | Database: PDB / ID: 5zi0 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Ketoreductase LbCR mutant - M8 | |||||||||
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 / Resolution: 2.302 Å | |||||||||
Authors | Gong, X.M. / Zheng, G.W. / Xu, J.H. | |||||||||
Funding support | China, 2items
| |||||||||
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 |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 5zi0.cif.gz | 205.5 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb5zi0.ent.gz | 163.3 KB | Display | PDB format |
PDBx/mmJSON format | 5zi0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5zi0_validation.pdf.gz | 458.3 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 5zi0_full_validation.pdf.gz | 466 KB | Display | |
Data in XML | 5zi0_validation.xml.gz | 41.3 KB | Display | |
Data in CIF | 5zi0_validation.cif.gz | 60.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zi/5zi0 ftp://data.pdbj.org/pub/pdb/validation_reports/zi/5zi0 | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 29567.482 Da / Num. of mol.: 4 / Mutation: M154I,A155D,V198I,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 / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.23 Å3/Da / Density % sol: 44.81 % |
---|---|
Crystal grow | Temperature: 291.15 K / Method: vapor diffusion, sitting drop Details: 0.1M MIB buffer (malonic acid:imidazole:boric acid in a mo-lar ratio of 2:3:3) pH 6.0, 21% (v/v) PEG 1500 |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U1 / Wavelength: 0.97918 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Dec 10, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97918 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→50 Å / Num. obs: 46187 / % possible obs: 97.6 % / Redundancy: 10.2 % / Rmerge(I) obs: 0.062 / Net I/σ(I): 18.906 |
Reflection shell | Resolution: 2.3→2.34 Å / Rmerge(I) obs: 0.094 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.302→31.006 Å / SU ML: 0.24 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 20.64
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.302→31.006 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell |
|