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Open data
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Basic information
Entry | Database: PDB / ID: 2q9s | ||||||
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Title | Linoleic Acid Bound to Fatty Acid Binding Protein 4 | ||||||
![]() | Fatty acid-binding protein | ||||||
![]() | LIPID BINDING PROTEIN / beta clamshell | ||||||
Function / homology | ![]() Triglyceride catabolism / hormone receptor binding / long-chain fatty acid transmembrane transporter activity / cellular response to lithium ion / long-chain fatty acid binding / white fat cell differentiation / fatty acid transport / long-chain fatty acid transport / brown fat cell differentiation / fatty acid metabolic process ...Triglyceride catabolism / hormone receptor binding / long-chain fatty acid transmembrane transporter activity / cellular response to lithium ion / long-chain fatty acid binding / white fat cell differentiation / fatty acid transport / long-chain fatty acid transport / brown fat cell differentiation / fatty acid metabolic process / cholesterol homeostasis / fatty acid binding / response to bacterium / positive regulation of inflammatory response / cellular response to tumor necrosis factor / positive regulation of cold-induced thermogenesis / negative regulation of DNA-templated transcription / positive regulation of cell population proliferation / nucleoplasm / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gillilan, R.E. / Ayers, S.D. / Noy, N. | ||||||
![]() | ![]() Title: Structural Basis for Activation of Fatty Acid-binding Protein 4. Authors: Gillilan, R.E. / Ayers, S.D. / Noy, N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 41.4 KB | Display | ![]() |
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PDB format | ![]() | 27.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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 on special symmetry positions |
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Details | The assembly is a dimer. The second half is generated by [-x,y,1/2-z] |
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Components
#1: Protein | Mass: 17001.518 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-SO4 / |
#3: Chemical | ChemComp-EIC / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.74 Å3/Da / Density % sol: 55.09 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 0.1 M Sodium Cacodylate, 0.1 M Ammonium Sulfate, 35% PEG 8000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Apr 30, 2006 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9176 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→50 Å / Num. obs: 8446 / % possible obs: 98.7 % / Redundancy: 9.4 % / Rmerge(I) obs: 0.082 / Χ2: 1.166 / Net I/σ(I): 24.7 |
Reflection shell | Resolution: 2.3→2.38 Å / Redundancy: 9.6 % / Rmerge(I) obs: 0.176 / Num. unique all: 834 / Χ2: 1.158 / % possible all: 99.3 |
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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: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 25.784 Å2
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Refinement step | Cycle: LAST / Resolution: 2.3→12 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.3→2.42 Å / Total num. of bins used: 10
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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