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- PDB-3h0s: Crystal structure of the carboxyltransferase domain of acetyl-coe... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3h0s | ||||||
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Title | Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase in complex with compound 7 | ||||||
![]() | Acetyl-CoA carboxylase | ||||||
![]() | TRANSFERASE / ACETYL-COA CARBOXYLASE / CARBOXYLTRANSFERASE / INHIBITOR / ACC / CT / ATP-binding / Biotin / Cytoplasm / Fatty acid biosynthesis / Ligase / Lipid synthesis / Metal-binding / Multifunctional enzyme / Nucleotide-binding | ||||||
Function / homology | ![]() : / Biotin transport and metabolism / Fatty acyl-CoA biosynthesis / Carnitine metabolism / acetyl-CoA carboxylase / carboxyl- or carbamoyltransferase activity / acetyl-CoA binding / biotin carboxylase / acetyl-CoA carboxylase complex / biotin carboxylase activity ...: / Biotin transport and metabolism / Fatty acyl-CoA biosynthesis / Carnitine metabolism / acetyl-CoA carboxylase / carboxyl- or carbamoyltransferase activity / acetyl-CoA binding / biotin carboxylase / acetyl-CoA carboxylase complex / biotin carboxylase activity / malonyl-CoA biosynthetic process / acetyl-CoA carboxylase activity / acetyl-CoA biosynthetic process / long-chain fatty acid biosynthetic process / fatty acid biosynthetic process / protein import into nucleus / endoplasmic reticulum membrane / protein homodimerization activity / mitochondrion / ATP binding / identical protein binding / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Vajdos, F. | ||||||
![]() | ![]() Title: Discovery of small molecule isozyme non-specific inhibitors of mammalian acetyl-CoA carboxylase 1 and 2. Authors: Corbett, J.W. / Freeman-Cook, K.D. / Elliott, R. / Vajdos, F. / Rajamohan, F. / Kohls, D. / Marr, E. / Zhang, H. / Tong, L. / Tu, M. / Murdande, S. / Doran, S.D. / Houser, J.A. / Song, W. / ...Authors: Corbett, J.W. / Freeman-Cook, K.D. / Elliott, R. / Vajdos, F. / Rajamohan, F. / Kohls, D. / Marr, E. / Zhang, H. / Tong, L. / Tu, M. / Murdande, S. / Doran, S.D. / Houser, J.A. / Song, W. / Jones, C.J. / Coffey, S.B. / Buzon, L. / Minich, M.L. / Dirico, K.J. / Tapley, S. / McPherson, R.K. / Sugarman, E. / Harwood, H.J. / Esler, 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 | ![]() | 473.3 KB | Display | ![]() |
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PDB format | ![]() | 382.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
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Full document | ![]() | 1.6 MB | Display | |
Data in XML | ![]() | 107.6 KB | Display | |
Data in CIF | ![]() | 159.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3h0jC ![]() 3h0qC ![]() 1w2xS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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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: 87237.977 Da / Num. of mol.: 3 / Fragment: Residues 1476-2233 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: FAS3, ACC1, YNR016C, N3175 / Production host: ![]() ![]() References: UniProt: Q00955, acetyl-CoA carboxylase, biotin carboxylase #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.18 Å3/Da / Density % sol: 70.54 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion / pH: 5.5 Details: 0.1 M Na citrate ,pH 5.5, 200 mM NaCl, 8% PEG8000, 10% glycerol, vapor diffusion, temperature 298K |
-Data collection
Diffraction source | Source: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Detector | Type: RIGAKU RAXIS HTC / Detector: IMAGE PLATE / Date: Jan 16, 2006 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.43→40.7 Å / Num. obs: 159230 / % possible obs: 98.3 % / Redundancy: 3.5 % / Rmerge(I) obs: 0.065 / Χ2: 1.271 / Net I/σ(I): 21.112 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1W2X Resolution: 2.43→40.7 Å / Cor.coef. Fo:Fc: 0.967 / Cor.coef. Fo:Fc free: 0.939 / WRfactor Rfree: 0.204 / WRfactor Rwork: 0.148 / Occupancy max: 1 / Occupancy min: 0.35 / FOM work R set: 0.848 / SU B: 6.065 / SU ML: 0.138 / SU R Cruickshank DPI: 0.213 / SU Rfree: 0.2 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.213 / ESU R Free: 0.2 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 164.91 Å2 / Biso mean: 56.371 Å2 / Biso min: 21.96 Å2
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Refinement step | Cycle: LAST / Resolution: 2.43→40.7 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.43→2.494 Å / Total num. of bins used: 20
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