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Yorodumi- PDB-1icm: ESCHERICHIA COLI-DERIVED RAT INTESTINAL FATTY ACID BINDING PROTEI... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1icm | ||||||
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Title | ESCHERICHIA COLI-DERIVED RAT INTESTINAL FATTY ACID BINDING PROTEIN WITH BOUND MYRISTATE AT 1.5 A RESOLUTION AND I-FABPARG106-->GLN WITH BOUND OLEATE AT 1.74 A RESOLUTION | ||||||
Components | INTESTINAL FATTY ACID BINDING PROTEIN | ||||||
Keywords | BINDING PROTEIN(FATTY ACID) | ||||||
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 / long-chain fatty acid transport / microvillus / 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 / long-chain fatty acid transport / microvillus / fatty acid transport / fatty acid metabolic process / fatty acid binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.5 Å | ||||||
Authors | Eads, J.C. / Sacchettini, J.C. / Kromminga, A. / Gordon, J.I. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1993 Title: Escherichia coli-derived rat intestinal fatty acid binding protein with bound myristate at 1.5 A resolution and I-FABPArg106-->Gln with bound oleate at 1.74 A resolution. Authors: Eads, J. / Sacchettini, J.C. / Kromminga, A. / Gordon, J.I. #1: Journal: J.Biol.Chem. / Year: 1992 Title: Refinement of the Structure of Recombinant Rat Intestinal Fatty Acid-Binding Apoprotein at 1.2 Angstroms Resolution Authors: Scapin, G. / Gordon, J.I. / Sacchettini, J.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1icm.cif.gz | 40.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1icm.ent.gz | 28.1 KB | Display | PDB format |
PDBx/mmJSON format | 1icm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1icm_validation.pdf.gz | 421.8 KB | Display | wwPDB validaton report |
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Full document | 1icm_full_validation.pdf.gz | 425.6 KB | Display | |
Data in XML | 1icm_validation.xml.gz | 9.3 KB | Display | |
Data in CIF | 1icm_validation.cif.gz | 12.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ic/1icm ftp://data.pdbj.org/pub/pdb/validation_reports/ic/1icm | HTTPS FTP |
-Related 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: 15015.015 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / References: UniProt: P02693 |
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#2: Chemical | ChemComp-MYR / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 1.96 Å3/Da / Density % sol: 37.13 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 17 ℃ / pH: 7.1 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
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: 1.5 Å / Lowest resolution: 20 Å / Num. obs: 12574 / Num. measured all: 34869 / Rmerge(I) obs: 0.0469 |
-Processing
Software |
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Refinement | Rfactor obs: 0.159 / Highest resolution: 1.5 Å | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.5 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.5 Å / Lowest resolution: 20 Å / Rfactor obs: 0.159 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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