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- PDB-8hpg: Crystal structure of phenylpyruvate reductase from Lactobacillus ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8hpg | ||||||
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Title | Crystal structure of phenylpyruvate reductase from Lactobacillus sp. CGMCC 9967 | ||||||
![]() | Phenylpyruvate reductase | ||||||
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Function / homology | ![]() ![]() ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Yang, J.H. / Song, W. | ||||||
Funding support | 1items
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![]() | ![]() Title: One-Pot Biocatalytic Transformation of L-DOPA to D-Danshensu Authors: Yang, J.H. / Song, W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 237.9 KB | Display | ![]() |
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PDB format | ![]() | 190.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 33752.609 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: ppr / Production host: ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.62 Å3/Da / Density % sol: 53.02 % |
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Crystal grow![]() | Temperature: 293.15 K / Method: vapor diffusion / pH: 3.5 Details: PEG 1000, Citric acid, B-Nicotinamide adeinie dinucleotide |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SEALED TUBE / Type: BRUKER D8 QUEST / Wavelength: 1.54184 Å |
Detector | Type: Bruker PHOTON II / Detector: PIXEL / Date: May 10, 2022 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 3.89→23.49 Å / Num. obs: 3064 / % possible obs: 86.7394 % / Redundancy: 2 % / Rmerge(I) obs: 0.141 / Rpim(I) all: 0.062 / Net I/σ(I): 7.29 |
Reflection shell | Resolution: 3.89→4.47 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.371 / Num. unique obs: 925 / CC1/2: 0.748 / % possible all: 54.7 |
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Processing
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Refinement | Method to determine structure![]() ![]()
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 42.129 Å2
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Refinement step | Cycle: 1 / Resolution: 3.895→23.49 Å
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Refine LS restraints |
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