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- PDB-1ifb: REFINED APOPROTEIN STRUCTURE OF RAT INTESTINAL FATTY ACID BINDING... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ifb | ||||||
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Title | REFINED APOPROTEIN STRUCTURE OF RAT INTESTINAL FATTY ACID BINDING PROTEIN PRODUCED IN ESCHERICHIA COLI | ||||||
![]() | INTESTINAL FATTY ACID BINDING PROTEIN | ||||||
![]() | FATTY ACID-BINDING PROTEIN | ||||||
Function / homology | ![]() Triglyceride catabolism / intestinal lipid absorption / apical cortex / intestinal absorption / long-chain fatty acid transmembrane transporter activity / long-chain fatty acid binding / microvillus / fatty acid transport / long-chain fatty acid transport / fatty acid metabolic process ...Triglyceride catabolism / intestinal lipid absorption / apical cortex / intestinal absorption / long-chain fatty acid transmembrane transporter activity / long-chain fatty acid binding / microvillus / fatty acid transport / long-chain fatty acid transport / fatty acid metabolic process / fatty acid binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Sacchettini, J.C. / Gordon, J.I. / Banaszak, L.J. | ||||||
![]() | ![]() Title: Refined apoprotein structure of rat intestinal fatty acid binding protein produced in Escherichia coli. Authors: Sacchettini, J.C. / Gordon, J.I. / 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 | ![]() | 37.7 KB | Display | ![]() |
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PDB format | ![]() | 26.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 370 KB | Display | ![]() |
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Full document | ![]() | 378.1 KB | Display | |
Data in XML | ![]() | 5.3 KB | Display | |
Data in CIF | ![]() | 7.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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
#1: Protein | Mass: 15015.015 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.97 Å3/Da / Density % sol: 37.63 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.3 / Method: free interface diffusion | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 10 Å / Rmerge(I) obs: 0.082 |
Reflection shell | *PLUS Highest resolution: 2 Å / Lowest resolution: 2.5 Å / Rmerge(I) obs: 0.162 |
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Processing
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Refinement | Rfactor Rwork: 0.188 / Highest resolution: 1.96 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.96 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.96 Å / Lowest resolution: 7 Å / Num. reflection obs: 5990 / σ(F): 1.5 / Rfactor obs: 0.188 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d |