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- PDB-5te1: C20S, C293G Mutant N-terminal Human ATP Citrate Lyase Bound to 4R... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5te1 | ||||||
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Title | C20S, C293G Mutant N-terminal Human ATP Citrate Lyase Bound to 4R-Hydroxycitrate | ||||||
![]() | ATP-citrate synthase | ||||||
![]() | TRANSFERASE / ATP grasp domain / 4R hydroxycitrate | ||||||
Function / homology | ![]() ATP citrate synthase activity / ATP citrate synthase / Fatty acyl-CoA biosynthesis / citrate metabolic process / ChREBP activates metabolic gene expression / acetyl-CoA biosynthetic process / oxaloacetate metabolic process / coenzyme A metabolic process / lipid biosynthetic process / cholesterol biosynthetic process ...ATP citrate synthase activity / ATP citrate synthase / Fatty acyl-CoA biosynthesis / citrate metabolic process / ChREBP activates metabolic gene expression / acetyl-CoA biosynthetic process / oxaloacetate metabolic process / coenzyme A metabolic process / lipid biosynthetic process / cholesterol biosynthetic process / tricarboxylic acid cycle / fatty acid biosynthetic process / azurophil granule lumen / ficolin-1-rich granule lumen / Neutrophil degranulation / extracellular exosome / extracellular region / nucleoplasm / ATP binding / membrane / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Hu, J. / Fraser, M.E. | ||||||
![]() | ![]() Title: Binding of hydroxycitrate to human ATP-citrate lyase. Authors: Hu, J. / Komakula, A. / Fraser, M.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 558.1 KB | Display | ![]() |
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PDB format | ![]() | 461.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 482.2 KB | Display | ![]() |
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Full document | ![]() | 491.9 KB | Display | |
Data in XML | ![]() | 57.5 KB | Display | |
Data in CIF | ![]() | 84.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5tdeC ![]() 5tdfC ![]() 5tdmC ![]() 5tdzC ![]() 5teqC ![]() 5tesC ![]() 5tetC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 90611.508 Da / Num. of mol.: 2 / Mutation: C20S, C293G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.63 Å3/Da / Density % sol: 53.29 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, hanging drop Details: 12.5% P3350, 200 mM MES pH 5.9, 125 mM ammonium acetate pH 5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Aug 23, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97944 Å / Relative weight: 1 |
Reflection | Resolution: 2.25→49.01 Å / Num. obs: 82560 / % possible obs: 93.2 % / Redundancy: 2.8 % / Net I/σ(I): 6.1 |
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Processing
Software | Name: PHENIX / Version: (1.10_2152: ???) / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.25→49.01 Å / SU ML: 0.27 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 25.11
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.25→49.01 Å
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Refine LS restraints |
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LS refinement shell |
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