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Yorodumi- PDB-1o1v: Human Ileal Lipid-Binding Protein (ILBP) in Complex with Cholyltaurine -
+Open data
-Basic information
Entry | Database: PDB / ID: 1o1v | ||||||
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Title | Human Ileal Lipid-Binding Protein (ILBP) in Complex with Cholyltaurine | ||||||
Components | Gastrotropin | ||||||
Keywords | LIPID BINDING PROTEIN / BETA CLAM STRUCTURE | ||||||
Function / homology | Function and homology information NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis / Triglyceride catabolism / fatty acid transport / Recycling of bile acids and salts / fatty acid binding / lipid metabolic process / negative regulation of cell population proliferation / lipid binding / membrane / nucleus ...NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis / Triglyceride catabolism / fatty acid transport / Recycling of bile acids and salts / fatty acid binding / lipid metabolic process / negative regulation of cell population proliferation / lipid binding / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / distance geometry (DIANA), molecular dynamics (SYBYL), energy minimization (SYBYL) | ||||||
Authors | Kurz, M. / Brachvogel, V. / Matter, H. / Stengelin, S. / Thuering, H. / Kramer, W. | ||||||
Citation | Journal: Proteins / Year: 2003 Title: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Authors: Kurz, M. / Brachvogel, V. / Matter, H. / Stengelin, S. / Thuering, H. / Kramer, W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1o1v.cif.gz | 407.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1o1v.ent.gz | 339.4 KB | Display | PDB format |
PDBx/mmJSON format | 1o1v.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1o1v_validation.pdf.gz | 450.1 KB | Display | wwPDB validaton report |
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Full document | 1o1v_full_validation.pdf.gz | 500.7 KB | Display | |
Data in XML | 1o1v_validation.xml.gz | 21.5 KB | Display | |
Data in CIF | 1o1v_validation.cif.gz | 35 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/o1/1o1v ftp://data.pdbj.org/pub/pdb/validation_reports/o1/1o1v | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 14258.038 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: FABP6 OR ILLBP OR ILBP / Plasmid: pHUGA1 / Production host: Escherichia coli (E. coli) / References: UniProt: P51161 |
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#2: Chemical | ChemComp-TCH / |
-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: 50 mM KH2PO4 / pH: 6.0 / Pressure: ambient / Temperature: 305 K | ||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: distance geometry (DIANA), molecular dynamics (SYBYL), energy minimization (SYBYL) Software ordinal: 1 Details: DIANA, MD, EM, structure based on 1832 nontrivial NOE distances from 2D-NOESY incl. 40 intermolecular distances. | ||||||||||||||||
NMR ensemble | Conformer selection criteria: lowest intermolecular restraint violation, DIANA target function Conformers calculated total number: 100 / Conformers submitted total number: 10 |