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Yorodumi- PDB-1ab0: C1G/V32D/F57H MUTANT OF MURINE ADIPOCYTE LIPID BINDING PROTEIN AT... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ab0 | ||||||
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Title | C1G/V32D/F57H MUTANT OF MURINE ADIPOCYTE LIPID BINDING PROTEIN AT PH 4.5 | ||||||
Components | ADIPOCYTE LIPID BINDING PROTEIN | ||||||
Keywords | FATTY ACID BINDING PROTEIN | ||||||
Function / homology | Function and homology information 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 | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Ory, J. / Kane, C. / Simpson, M. / Banaszak, L. / Bernlohr, D. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1997 Title: Biochemical and crystallographic analyses of a portal mutant of the adipocyte lipid-binding protein. Authors: Ory, J. / Kane, C.D. / Simpson, M.A. / Banaszak, L.J. / Bernlohr, D.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ab0.cif.gz | 37.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ab0.ent.gz | 25.4 KB | Display | PDB format |
PDBx/mmJSON format | 1ab0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ab/1ab0 ftp://data.pdbj.org/pub/pdb/validation_reports/ab/1ab0 | HTTPS FTP |
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-Related structure data
Related structure data | 1acdC 1libS 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
#1: Protein | Mass: 14500.526 Da / Num. of mol.: 1 / Mutation: C1G, V32D, F57H Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Cell: ADIPOCYTE / Production host: Escherichia coli (E. coli) / References: UniProt: P04117 |
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#2: 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: 2.2 Å3/Da / Density % sol: 45.6 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 4.5 / Details: 2.4M AMSO4 50MM NAKPO4 100 MM ACETATE, PH 4.5 | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Jun 27, 1994 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→26 Å / Num. obs: 10324 / % possible obs: 97 % / Observed criterion σ(I): 2 / Redundancy: 10.4 % / Biso Wilson estimate: 14.3 Å2 / Rsym value: 0.105 / Net I/σ(I): 8.7 |
Reflection shell | Resolution: 1.89→2.01 Å / Redundancy: 3.9 % / Mean I/σ(I) obs: 0.9 / Rsym value: 0.566 / % possible all: 65 |
Reflection | *PLUS Num. measured all: 103340 / Rmerge(I) obs: 0.1051 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1LIB Resolution: 1.9→25 Å / Rfactor Rfree error: 0.0035 / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2
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Displacement parameters | Biso mean: 30.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.9→25 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→1.99 Å / Rfactor Rfree error: 0.002 / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.843C / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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