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- PDB-1fel: CRYSTALLOGRAPHIC STUDIES ON COMPLEXES BETWEEN RETINOIDS AND PLASM... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1fel | ||||||
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Title | CRYSTALLOGRAPHIC STUDIES ON COMPLEXES BETWEEN RETINOIDS AND PLASMA RETINOL-BINDING PROTEIN | ||||||
![]() | RETINOL BINDING PROTEIN | ||||||
![]() | TRANSPORT PROTEIN | ||||||
Function / homology | ![]() retinol transport / retinol transmembrane transporter activity / retinal binding / retinol binding / extracellular space Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Zanotti, G. / Marcello, M. / Malpeli, G. / Sartori, G. / Berni, R. | ||||||
![]() | ![]() Title: Crystallographic studies on complexes between retinoids and plasma retinol-binding protein. Authors: Zanotti, G. / Marcello, M. / Malpeli, G. / Folli, C. / Sartori, G. / Berni, R. #1: ![]() Title: The Interaction of N-Ethyl Retinamide with Plasma Retinol-Binding Protein (Rbp) and the Crystal Structure of the Retinoid-Rbp Complex at 1.9 Angstroms Resolution Authors: Zanotti, G. / Malpeli, G. / Berni, R. #2: ![]() Title: Crystal Structure of Liganded and Unliganded Forms of Bovine Plasma Retinol-Binding Protein Authors: Zanotti, G. / Berni, R. / Monaco, H.L. #3: ![]() Title: Crystal Structure of the Trigonal Form of Human Plasma Retinol-Binding Protein at 2.5 Angstroms Resolution Authors: Zanotti, G. / Ottonello, S. / Berni, R. / Monaco, H.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 52.6 KB | Display | ![]() |
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PDB format | ![]() | 37.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 426.8 KB | Display | ![]() |
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Full document | ![]() | 444.5 KB | Display | |
Data in XML | ![]() | 8.4 KB | Display | |
Data in CIF | ![]() | 12 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 21095.654 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-FEN / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.09 Å3/Da / Density % sol: 41.02 % | |||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 41 % | |||||||||||||||||||||||||
Crystal grow | *PLUS Method: microdialysis / PH range low: 5.3 / PH range high: 5 | |||||||||||||||||||||||||
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: 1.8 Å / Lowest resolution: 9999 Å / Num. obs: 12128 / % possible obs: 71 % / Observed criterion σ(I): 0 / Num. measured all: 49962 / Rmerge(I) obs: 0.062 |
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Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.8→9 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 1.8→9 Å
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection all: 12128 / Rfactor all: 0.204 | ||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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