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- PDB-4zv3: Crystal structure of the N- and C-terminal domains of mouse acyl-... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4zv3 | ||||||
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Title | Crystal structure of the N- and C-terminal domains of mouse acyl-CoA thioesterase 7 | ||||||
![]() | Cytosolic acyl coenzyme A thioester hydrolase | ||||||
![]() | HYDROLASE / Thioesterase / Double hotdog / Inflammation | ||||||
Function / homology | ![]() long-chain fatty acyl-CoA hydrolase activity / palmitic acid biosynthetic process / palmitoyl-CoA hydrolase / Mitochondrial Fatty Acid Beta-Oxidation / acyl-CoA metabolic process / fatty acyl-CoA hydrolase activity / fatty acid catabolic process / carboxylic ester hydrolase activity / mitochondrial matrix / neuron projection ...long-chain fatty acyl-CoA hydrolase activity / palmitic acid biosynthetic process / palmitoyl-CoA hydrolase / Mitochondrial Fatty Acid Beta-Oxidation / acyl-CoA metabolic process / fatty acyl-CoA hydrolase activity / fatty acid catabolic process / carboxylic ester hydrolase activity / mitochondrial matrix / neuron projection / neuronal cell body / extracellular exosome / nucleoplasm / identical protein binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Swarbrick, C.M.D. / Forwood, J.K. | ||||||
![]() | ![]() Title: Crystal structure of the N- and C-terminal domains of mouse acyl-CoA thioesterase 7 Authors: Swarbrick, C.M.D. / Forwood, J.K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 188 KB | Display | ![]() |
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PDB format | ![]() | 150.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 36 KB | Display | |
Data in CIF | ![]() | 46.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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
#1: Protein | Mass: 35417.508 Da / Num. of mol.: 3 / Fragment: unp residues 55-369 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.58 Å3/Da / Density % sol: 52.39 % |
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Crystal grow | Temperature: 296 K / Method: vapor diffusion, hanging drop / Details: 200 mM sodium citrate, 12% PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Aug 13, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→34.91 Å / Num. obs: 18941 / % possible obs: 99.9 % / Redundancy: 3.3 % / Rmerge(I) obs: 0.157 / Net I/σ(I): 5.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2Q2B, 2V1O Resolution: 3.1→32.1 Å / Cor.coef. Fo:Fc: 0.911 / Cor.coef. Fo:Fc free: 0.872 / SU B: 0.015 / SU ML: 0 / Cross valid method: THROUGHOUT / ESU R: 0.479 / ESU R Free: 0.589 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||
Displacement parameters | Biso mean: 82.907 Å2
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Refinement step | Cycle: LAST / Resolution: 3.1→32.1 Å
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LS refinement shell | Resolution: 3.1→3.18 Å / Total num. of bins used: 20
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