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Yorodumi- PDB-2ju3: Solution-state NMR structures of apo-LFABP (Liver Fatty Acid-Bind... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2ju3 | ||||||
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Title | Solution-state NMR structures of apo-LFABP (Liver Fatty Acid-Binding Protein) | ||||||
Components | Fatty acid-binding protein, liver | ||||||
Keywords | LIPID BINDING PROTEIN / protein / apo / LFABP / iLBP / FABP / Acetylation / Cytoplasm / Lipid-binding / Phosphorylation / Transport | ||||||
Function / homology | Function and homology information Regulation of lipid metabolism by PPARalpha / Triglyceride catabolism / lysophospholipid:sodium symporter activity / Heme degradation / response to vitamin B3 / Cytoprotection by HMOX1 / oleic acid binding / apical cortex / positive regulation of fatty acid beta-oxidation / bile acid binding ...Regulation of lipid metabolism by PPARalpha / Triglyceride catabolism / lysophospholipid:sodium symporter activity / Heme degradation / response to vitamin B3 / Cytoprotection by HMOX1 / oleic acid binding / apical cortex / positive regulation of fatty acid beta-oxidation / bile acid binding / intestinal absorption / long-chain fatty acid transmembrane transporter activity / heterocyclic compound binding / antioxidant activity / peroxisomal matrix / fatty acid transport / long-chain fatty acid transport / fatty acid binding / phospholipid binding / cellular response to hydrogen peroxide / cellular response to hypoxia / chromatin binding / negative regulation of apoptotic process / protein-containing complex / nucleoplasm / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics | ||||||
Authors | He, Y. / Yang, X. / Wang, H. / Estephan, R. / Francis, F. / Kodukula, S. / Storch, J. / Stark, R.E. | ||||||
Citation | Journal: Biochemistry / Year: 2007 Title: Solution-State Molecular Structure of Apo and Oleate-Liganded Liver Fatty Acid-Binding Protein Authors: He, Y. / Yang, X. / Wang, H. / Estephan, R. / Francis, F. / Kodukula, S. / Storch, J. / Stark, R.E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ju3.cif.gz | 394.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ju3.ent.gz | 341.5 KB | Display | PDB format |
PDBx/mmJSON format | 2ju3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ju/2ju3 ftp://data.pdbj.org/pub/pdb/validation_reports/ju/2ju3 | HTTPS FTP |
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-Related structure data
Related structure data | 2ju7C 2ju8C C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 14293.544 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Fabp1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): pLys / References: UniProt: P02692 |
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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 |
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Sample conditions | Ionic strength: 0.05 / pH: 6 / Pressure: ambient / Temperature: 303 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing, torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 |