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Yorodumi- PDB-1kzw: Solution structure of Human Intestinal Fatty acid binding protein -
+Open data
-Basic information
Entry | Database: PDB / ID: 1kzw | ||||||
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Title | Solution structure of Human Intestinal Fatty acid binding protein | ||||||
Components | INTESTINAL FATTY ACID-BINDING PROTEIN (A54) | ||||||
Keywords | LIPID BINDING PROTEIN / NMR spectroscopy / 15N isotope labelling / Fatty acid binding / Type 2 diabetes / Single base polymorphism / Holo-form | ||||||
Function / homology | Function and homology information intestinal lipid absorption / apical cortex / long-chain fatty acid transmembrane transporter activity / long-chain fatty acid binding / Triglyceride catabolism / microvillus / fatty acid transport / fatty acid metabolic process / fatty acid binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics, , energy minimization | ||||||
Authors | Zhang, F. / Luecke, C. / Baier, L.J. / Sacchettini, J.C. / Hamilton, J.A. | ||||||
Citation | Journal: Biochemistry / Year: 2003 Title: Solution structure of human intestinal fatty acid binding protein with a naturally-occurring single amino acid substitution (A54T) that is associated with altered lipid metabolism Authors: Zhang, F. / Luecke, C. / Baier, L.J. / Sacchettini, J.C. / Hamilton, J.A. #1: Journal: J.Biomol.NMR / Year: 1997 Title: SOLUTION STRUCTURE OF HUMAN INTESTINAL FATTY ACID BINDING PROTEIN: IMPLICATIONS FOR LIGAND ENTRY AND EXIT Authors: Zhang, F. / Luecke, C. / Baier, L.J. / Sacchettini, J.C. / Hamilton, J.A. #2: Journal: J.Biol.Chem. / Year: 1996 Title: A POLYMORPHISM IN THE HUMAN INTESTINAL FATTY ACID BINDING PROTEIN ALTERS FATTY ACID TRANSPORT ACROSS CACO-2 CELLS Authors: Baier, L.J. / Bogardus, C. / Sacchettini, J.C. #3: Journal: J.Clin.Invest. / Year: 1995 Title: AN AMINO ACID SUBSTITUTION IN THE HUMAN INTESTINAL FATTY ACID BINDING PROTEIN IS ASSOCIATED WITH INCREASED FATTY ACID BINDING, INCREASED FAT OXIDATION, AND INSULIN RESISTANCE Authors: Baier, L.J. / Sacchettini, J.C. / Knowler, W.C. / Eads, J. / Paolisso, G. / Tataranni, P.A. / Mochizuki, H. / Bennet, H.P. / Bogardus, C. / Prochazka, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1kzw.cif.gz | 819.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1kzw.ent.gz | 704.4 KB | Display | PDB format |
PDBx/mmJSON format | 1kzw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kz/1kzw ftp://data.pdbj.org/pub/pdb/validation_reports/kz/1kzw | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 15098.044 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: FABP2 / Plasmid: PET-3D / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P12104 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample conditions | Ionic strength: 20mM phosphate buffer / pH: 6.5 / Pressure: ambient / Temperature: 310 K | |||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 500 MHz |
-Processing
NMR software |
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Refinement | Method: simulated annealing, torsion angle dynamics, , energy minimization Software ordinal: 1 Details: the structures are based on a total number of 2538 distance restraints | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 300 / Conformers submitted total number: 20 |