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Yorodumi- PDB-1g74: Toward changing specificity: adipocyte lipid binding protein muta... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1g74 | ||||||
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Title | Toward changing specificity: adipocyte lipid binding protein mutant, oleic acid bound form | ||||||
Components | ADIPOCYTE LIPID-BINDING PROTEIN | ||||||
Keywords | LIPID BINDING PROTEIN / beta-barrel / fatty acid binding protein / protein engineering / fatty acid binding | ||||||
Function / homology | Function and homology information Triglyceride catabolism / hormone receptor binding / long-chain fatty acid transmembrane transporter activity / long-chain fatty acid binding / cellular response to lithium ion / white fat cell differentiation / long-chain fatty acid transport / fatty acid transport / brown fat cell differentiation / cholesterol homeostasis ...Triglyceride catabolism / hormone receptor binding / long-chain fatty acid transmembrane transporter activity / long-chain fatty acid binding / cellular response to lithium ion / white fat cell differentiation / long-chain fatty acid transport / fatty acid transport / brown fat cell differentiation / cholesterol homeostasis / fatty acid metabolic process / 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 | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / isomorphous with apo EF-ALBP (PDB 1G7N) / Resolution: 1.7 Å | ||||||
Authors | Reese, A.J. / Banaszak, L.J. | ||||||
Citation | Journal: J.Lipid Res. / Year: 2004 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1g74.cif.gz | 43.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1g74.ent.gz | 30.1 KB | Display | PDB format |
PDBx/mmJSON format | 1g74.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g7/1g74 ftp://data.pdbj.org/pub/pdb/validation_reports/g7/1g74 | HTTPS FTP |
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-Related structure data
Related structure data | 1g7nSC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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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.) Mus musculus (house mouse) / Gene: ALBP / Plasmid: RSET / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P04117 |
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#2: Chemical | ChemComp-PO4 / |
#3: Chemical | ChemComp-OLA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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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: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 Å |
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 |
-Processing
Software |
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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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