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Yorodumi- PDB-1fen: CRYSTALLOGRAPHIC STUDIES ON COMPLEXES BETWEEN RETINOIDS AND PLASM... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fen | ||||||
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Title | CRYSTALLOGRAPHIC STUDIES ON COMPLEXES BETWEEN RETINOIDS AND PLASMA RETINOL-BINDING PROTEIN | ||||||
Components | RETINOL BINDING PROTEIN | ||||||
Keywords | TRANSPORT PROTEIN | ||||||
Function / homology | Function and homology information retinol transport / retinol transmembrane transporter activity / retinal binding / retinol binding / extracellular space Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.9 Å | ||||||
Authors | Zanotti, G. / Marcello, M. / Malpeli, G. / Sartori, G. / Berni, R. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1994 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: Journal: J.Biol.Chem. / Year: 1993 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: Journal: J.Biol.Chem. / Year: 1993 Title: Crystal Structure of Liganded and Unliganded Forms of Bovine Plasma Retinol-Binding Protein Authors: Zanotti, G. / Berni, R. / Monaco, H.L. #3: Journal: J.Mol.Biol. / Year: 1993 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fen.cif.gz | 51.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fen.ent.gz | 37.1 KB | Display | PDB format |
PDBx/mmJSON format | 1fen.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fen_validation.pdf.gz | 434.8 KB | Display | wwPDB validaton report |
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Full document | 1fen_full_validation.pdf.gz | 444.9 KB | Display | |
Data in XML | 1fen_validation.xml.gz | 6.9 KB | Display | |
Data in CIF | 1fen_validation.cif.gz | 10.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fe/1fen ftp://data.pdbj.org/pub/pdb/validation_reports/fe/1fen | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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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.) Bos taurus (cattle) / References: UniProt: P18902 |
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#2: Chemical | ChemComp-AZE / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.07 Å3/Da / Density % sol: 40.65 % | |||||||||||||||||||||||||
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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: 1.9 Å / Lowest resolution: 9999 Å / Num. obs: 10137 / % possible obs: 60 % / Observed criterion σ(I): 0 / Num. measured all: 16650 / Rmerge(I) obs: 0.07 |
-Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.9→9 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 1.9→9 Å
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection all: 10137 / Rfactor all: 0.193 | ||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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