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- PDB-1kzx: Solution structure of human intestinal fatty acid binding protein... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1kzx | ||||||
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Title | Solution structure of human intestinal fatty acid binding protein with a naturally-occurring single amino acid substitution (A54T) | ||||||
![]() | INTESTINAL FATTY ACID-BINDING PROTEIN (T54) | ||||||
![]() | LIPID BINDING PROTEIN / NMR spectroscopy / 15N isotope labelling / Fatty acid binding / Type 2 diabetes / Single base polymorphism / Holo-form | ||||||
Function / homology | ![]() 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 | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics, energy minimization | ||||||
![]() | Zhang, F. / Luecke, C. / Baier, L.J. / Sacchettini, J.C. / Hamilton, J.A. | ||||||
![]() | ![]() 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: ![]() 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: ![]() 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: ![]() 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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Remark 999 | SEQUENCE The mutation is due to a naturally occuring polymorphism in the human genome. This ...SEQUENCE The mutation is due to a naturally occuring polymorphism in the human genome. This polymorphism at codon 54, which changes ALA-54 (0.71 allele frequency in a population of native americans) to THR-54 (0.29 allelle frequency), has been associated with type-2 diabetes and insulin resistance. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 820.9 KB | Display | ![]() |
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PDB format | ![]() | 686.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 361.9 KB | Display | ![]() |
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Full document | ![]() | 471.6 KB | Display | |
Data in XML | ![]() | 39.9 KB | Display | |
Data in CIF | ![]() | 70.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 15128.069 Da / Num. of mol.: 1 / Mutation: A54T Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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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 |
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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 2497 distance restraints | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 300 / Conformers submitted total number: 20 |