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- PDB-1g74: Toward changing specificity: adipocyte lipid binding protein muta... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1g74 | ||||||
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Title | Toward changing specificity: adipocyte lipid binding protein mutant, oleic acid bound form | ||||||
![]() | ADIPOCYTE LIPID-BINDING PROTEIN | ||||||
![]() | LIPID BINDING PROTEIN / beta-barrel / fatty acid binding protein / protein engineering / fatty acid binding | ||||||
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 | ![]() | ||||||
![]() | Reese, A.J. / Banaszak, L.J. | ||||||
![]() | ![]() Title: Specificity determinants for lipids bound to beta-barrel proteins. Authors: Reese, A.J. / Banaszak, L.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 43.6 KB | Display | ![]() |
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PDB format | ![]() | 30.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1g7nSC S: Starting model for refinement 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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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 14525.663 Da / Num. of mol.: 1 / Mutation: I73E,A75V,D77G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-PO4 / |
#3: Chemical | ChemComp-OLA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 41.49 % | |||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.8 Details: sodium/potassium phosphate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K | |||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.2 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 113 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jul 13, 2000 / Details: mirrors |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.71→27 Å / Num. obs: 12433 / % possible obs: 93.9 % / Observed criterion σ(F): 3 / Observed criterion σ(I): 3 / Redundancy: 3.31 % / Rmerge(I) obs: 0.046 / Net I/σ(I): 16.4 |
Reflection shell | Resolution: 1.71→1.77 Å / Redundancy: 3.37 % / Rmerge(I) obs: 0.304 / % possible all: 90.1 |
Reflection | *PLUS Highest resolution: 1.7 Å / Lowest resolution: 25 Å / Num. obs: 13235 / Redundancy: 3.19 % / Num. measured all: 42285 |
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Processing
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Refinement | Method to determine structure: isomorphous with apo EF-ALBP (PDB 1G7N) Starting model: EF-ALBP (PDB 1G7N) Resolution: 1.7→25 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber Details: The following amino acids have alternative conformations: Cys1, Lys9, Lys21, Glu22, Val44, Thr74, Glu116, Ser124, Glu129, and Oleate132
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Refinement step | Cycle: LAST / Resolution: 1.7→25 Å
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LS refinement shell | Resolution: 1.71→1.77 Å /
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Refinement | *PLUS Rfactor Rfree: 0.237 / Rfactor Rwork: 0.208 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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