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Yorodumi- PDB-1ifb: REFINED APOPROTEIN STRUCTURE OF RAT INTESTINAL FATTY ACID BINDING... -
+Open data
-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 | ||||||
Components | INTESTINAL FATTY ACID BINDING PROTEIN | ||||||
Keywords | FATTY ACID-BINDING PROTEIN | ||||||
Function / homology | Function and homology information 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 | Rattus rattus (black rat) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.96 Å | ||||||
Authors | Sacchettini, J.C. / Gordon, J.I. / Banaszak, L.J. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1989 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ifb.cif.gz | 37.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ifb.ent.gz | 26.2 KB | Display | PDB format |
PDBx/mmJSON format | 1ifb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/if/1ifb ftp://data.pdbj.org/pub/pdb/validation_reports/if/1ifb | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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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.) Rattus rattus (black rat) / References: UniProt: P02693 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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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 |
-Processing
Software | Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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 |