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Open data
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Basic information
Entry | Database: PDB / ID: 1b56 | ||||||
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Title | HUMAN RECOMBINANT EPIDERMAL FATTY ACID BINDING PROTEIN | ||||||
![]() | FATTY ACID BINDING PROTEIN | ||||||
![]() | LIPID BINDING PROTEIN / LIPID-BINDING / FATTY ACID TRANSPORT / BETA BARREL | ||||||
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 / Signaling by Retinoic Acid / long-chain fatty acid transmembrane transporter activity ...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 / Signaling by Retinoic Acid / long-chain fatty acid transmembrane transporter activity / 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 | ![]() ![]() ![]() | ||||||
![]() | Van Tilbeurgh, H. / Hohoff, C. / Borchers, T. / Spener, F. | ||||||
![]() | ![]() Title: Expression, purification, and crystal structure determination of recombinant human epidermal-type fatty acid binding protein. Authors: Hohoff, C. / Borchers, T. / Rustow, 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 | ![]() | 41.3 KB | Display | ![]() |
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PDB format | ![]() | 32.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 414.7 KB | Display | ![]() |
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Full document | ![]() | 418 KB | Display | |
Data in XML | ![]() | 5 KB | Display | |
Data in CIF | ![]() | 6.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2hmbS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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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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#2: Chemical | ChemComp-PLM / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.55 Å3/Da / Density % sol: 52 % | ||||||||||||||||||||
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Crystal grow | pH: 6 / Details: pH 6.0 | ||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||
Crystal grow | *PLUS pH: 5.6 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.95 Å / Relative weight: 1 |
Reflection | Resolution: 2.05→20 Å / Num. obs: 10321 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / Redundancy: 7 % / Rmerge(I) obs: 0.07 / Rsym value: 0.07 / Net I/σ(I): 20 |
Reflection shell | Resolution: 2.05→2.12 Å / Redundancy: 7 % / Rmerge(I) obs: 0.275 / Mean I/σ(I) obs: 12 / % possible all: 100 |
Reflection | *PLUS Num. measured all: 72226 / Rmerge(I) obs: 0.07 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2HMB Resolution: 2.05→8 Å / Cross valid method: THROUGHOUT / σ(F): 0 Details: PROBABLY ALTERNATIVE CONFORMATIONS FOR THE LOOP BETWEEN RESIDUES 59 AND 62 N TERMINAL REGION DISORDERED NATURE OF THE BOUND LIGAND NOT CERTAIN COULD BE A MIXTURE OF LIGANDS, NO EXTRA LIGAND ...Details: PROBABLY ALTERNATIVE CONFORMATIONS FOR THE LOOP BETWEEN RESIDUES 59 AND 62 N TERMINAL REGION DISORDERED NATURE OF THE BOUND LIGAND NOT CERTAIN COULD BE A MIXTURE OF LIGANDS, NO EXTRA LIGAND WAS USED IN THE CRYSTALLIZATION LIQUOR.
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Displacement parameters | Biso mean: 28.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.05→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.265 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |