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Open data
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Basic information
Entry | Database: PDB / ID: 2fyj | ||||||
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Title | NMR Solution structure of calcium-loaded LRP double module | ||||||
![]() | Low-density lipoprotein receptor-related protein 1 | ||||||
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Function / homology | ![]() alpha-2 macroglobulin receptor activity / apolipoprotein receptor activity / positive regulation of lipid transport / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Jensen, G.A. / Andersen, O.M. / Bonvin, A.M. / Bjerrum-Bohr, I. / Etzerodt, M. / O'shea, C. / Poulsen, F.M. / Kragelund, B.B. | ||||||
![]() | ![]() Title: Binding Site Structure of One LRP-RAP Complex:Implications for a Common Ligand-Receptor Binding Motif. Authors: Jensen, G.A. / Andersen, O.M. / Bonvin, A.M. / Bjerrum-Bohr, I. / Etzerodt, M. / O'shea, C. / Poulsen, F.M. / Kragelund, B.B. #1: ![]() Title: The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein. Authors: Nielsen, P.R. / Ellgaard, L. / Etzerodt, M. / Thogersen, H.C. / Poulsen, F.M. #2: Journal: J.Biol.Chem. / Year: 2000 Title: Identification of the minimal functional unit in the low density lipoprotein receptor-related protein for binding the receptor-associated protein (RAP). A conserved acidic residue in the ...Title: Identification of the minimal functional unit in the low density lipoprotein receptor-related protein for binding the receptor-associated protein (RAP). A conserved acidic residue in the complement-type repeats is important for recognition of RAP Authors: Andersen, O.M. / Christensen, L.L. / Chrsitensen, P.A. / Sorensen, E.S. / Jakobsen, C. / Moestrup, S.K. / Etzerodt, M. / Thogersen, H.C. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 334.4 KB | Display | ![]() |
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PDB format | ![]() | 287 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2fylC C: citing same article ( |
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Similar structure data | |
Other databases |
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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: 8944.620 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
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NMR experiment |
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Sample preparation
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Sample conditions |
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-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: SIMMULATED ANNEALING USING XPLOR-NIH, REFINEMENT IN EXPLICIT WATER LAYER USING CNS Software ordinal: 1 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: lowest energy, fewest violations Conformers calculated total number: 200 / Conformers submitted total number: 15 |