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Open data
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Basic information
Entry | Database: PDB / ID: 7uli | ||||||||||||
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Title | Apo HMG-CoA Reductase from Arabidopsis thaliana (HMG1) | ||||||||||||
![]() | 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1 | ||||||||||||
![]() | OXIDOREDUCTASE / Apo | ||||||||||||
Function / homology | ![]() hydroxymethylglutaryl-CoA reductase (NADPH) / hydroxymethylglutaryl-CoA reductase (NADPH) activity / isopentenyl diphosphate biosynthetic process, mevalonate pathway / sterol biosynthetic process / coenzyme A metabolic process / isoprenoid biosynthetic process / peroxisomal membrane / endoplasmic reticulum membrane / endoplasmic reticulum Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Haywood, J. / Bond, C.S. | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: A fungal tolerance trait and selective inhibitors proffer HMG-CoA reductase as a herbicide mode-of-action. Authors: Haywood, J. / Breese, K.J. / Zhang, J. / Waters, M.T. / Bond, C.S. / Stubbs, K.A. / Mylne, J.S. #1: ![]() Title: Structure-guided investigations into HMG-CoA reductase as a herbicide target Authors: Haywood, J. / Breese, K.J. / Zhang, J. / Waters, M.T. / Bond, C.S. / Stubbs, K.A. / Mylne, J.S. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 150 KB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 430 KB | Display | ![]() |
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Full document | ![]() | 437.9 KB | Display | |
Data in XML | ![]() | 15.3 KB | Display | |
Data in CIF | ![]() | 21.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8ecgC ![]() 1hw8S S: Starting model for refinement C: citing same article ( |
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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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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 63660.516 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P14891, hydroxymethylglutaryl-CoA reductase (NADPH) |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.92 Å3/Da / Density % sol: 35.85 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop Details: 0.2 M ammonium sulfate, 0.1 M HEPES, 35% w/v poly(acrylic acid sodium salt)2100 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Dec 1, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.95372 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→45.302 Å / Num. obs: 39592 / % possible obs: 100 % / Redundancy: 13.3 % / CC1/2: 1 / Net I/σ(I): 14.8 |
Reflection shell | Resolution: 1.9→1.94 Å / Num. unique obs: 2488 / CC1/2: 0.549 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1HW8 Resolution: 1.9→45.302 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.946 / WRfactor Rfree: 0.222 / WRfactor Rwork: 0.185 / SU B: 5.331 / SU ML: 0.14 / Average fsc free: 0.8225 / Average fsc work: 0.8248 / Cross valid method: FREE R-VALUE / ESU R: 0.129 / ESU R Free: 0.127 Details: Hydrogens have been added in their riding positions
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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 BULK SOLVENT | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 46.286 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→45.302 Å
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Refine LS restraints |
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LS refinement shell |
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