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- PDB-1jjj: SOLUTION STRUCTURE OF RECOMBINANT HUMAN EPIDERMAL-TYPE FATTY ACID... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1jjj | ||||||
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Title | SOLUTION STRUCTURE OF RECOMBINANT HUMAN EPIDERMAL-TYPE FATTY ACID BINDING PROTEIN | ||||||
![]() | EPIDERMAL-TYPE FATTY ACID BINDING PROTEIN (E-FABP) | ||||||
![]() | LIPID BINDING PROTEIN / BETA BARREL / FATTY ACID CARRIER / HOLO FORM / NMR SPECTROSCOPY / 15N ISOTOPE ENRICHMENT | ||||||
Function / homology | ![]() regulation of prostaglandin biosynthetic process / regulation of retrograde trans-synaptic signaling by endocanabinoid / lipid transport across blood-brain barrier / positive regulation of peroxisome proliferator activated receptor signaling pathway / negative regulation of glucose transmembrane transport / regulation of sensory perception of pain / phosphatidylcholine biosynthetic process / retinoic acid binding / long-chain fatty acid transmembrane transporter activity / Signaling by Retinoic Acid ...regulation of prostaglandin biosynthetic process / regulation of retrograde trans-synaptic signaling by endocanabinoid / lipid transport across blood-brain barrier / positive regulation of peroxisome proliferator activated receptor signaling pathway / negative regulation of glucose transmembrane transport / regulation of sensory perception of pain / phosphatidylcholine biosynthetic process / retinoic acid binding / long-chain fatty acid transmembrane transporter activity / Signaling by Retinoic Acid / Triglyceride catabolism / epidermis development / fatty acid transport / long-chain fatty acid transport / secretory granule membrane / fatty acid binding / lipid metabolic process / glucose metabolic process / azurophil granule lumen / glucose homeostasis / positive regulation of cold-induced thermogenesis / postsynaptic density / lipid binding / synapse / Neutrophil degranulation / extracellular exosome / extracellular region / nucleoplasm / identical protein binding / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / TORSION ANGLE DYNAMICS, SIMULATED ANNEALING, ENERGY MINIMIZATION | ||||||
![]() | Gutierrez-Gonzalez, L.H. / Ludwig, C. / Hohoff, C. / Rademacher, M. / Hanhoff, T. / Rueterjans, H. / Spener, F. / Luecke, C. | ||||||
![]() | ![]() Title: Solution structure and backbone dynamics of human epidermal-type fatty acid-binding protein (E-FABP) Authors: Gutierrez-Gonzalez, L.H. / Ludwig, C. / Hohoff, C. / Rademacher, M. / Hanhoff, T. / Rueterjans, H. / Spener, F. / Luecke, C. #1: ![]() Title: Expression, Purification, and Crystal Structure Determination of Recombinant Human Epidermal-Type Fatty Acid Binding Protein Authors: Hohoff, C. / Boerchers, T. / Ruestow, B. / Spener, F. / Van Tilbeurgh, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 817 KB | Display | ![]() |
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PDB format | ![]() | 704.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 354.5 KB | Display | ![]() |
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Full document | ![]() | 458.4 KB | Display | |
Data in XML | ![]() | 36.9 KB | Display | |
Data in CIF | ![]() | 67.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 15185.457 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 1.5-2 MM E-FABP PHOSPHATE BUFFER; 0.05% SODIUM AZIDE |
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Sample conditions | Ionic strength: 20 mM POTASSIUM PHOSPHATE / pH: 5.60 / Pressure: AMBIENT / Temperature: 298.00 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: TORSION ANGLE DYNAMICS, SIMULATED ANNEALING, ENERGY MINIMIZATION Software ordinal: 1 Details: THE STRUCTURES ARE BASED ON A TOTAL OF 2008 NOE-DERIVED DISTANCE RESTRAINTS | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 300 / Conformers submitted total number: 20 |