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Open data
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Basic information
Entry | Database: PDB / ID: 5lnf | ||||||
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Title | Solution NMR structure of farnesylated PEX19, C-terminal domain | ||||||
![]() | Peroxisomal biogenesis factor 19 | ||||||
![]() | CHAPERONE / PEX19 / farnesylation / post translational modification / allostery | ||||||
Function / homology | ![]() peroxisome membrane biogenesis / peroxisome membrane class-1 targeting sequence binding / establishment of protein localization to peroxisome / negative regulation of lipid binding / peroxisome membrane targeting sequence binding / protein import into peroxisome membrane / protein targeting to peroxisome / Class I peroxisomal membrane protein import / protein carrier chaperone / peroxisome organization ...peroxisome membrane biogenesis / peroxisome membrane class-1 targeting sequence binding / establishment of protein localization to peroxisome / negative regulation of lipid binding / peroxisome membrane targeting sequence binding / protein import into peroxisome membrane / protein targeting to peroxisome / Class I peroxisomal membrane protein import / protein carrier chaperone / peroxisome organization / peroxisome fission / ABC transporters in lipid homeostasis / peroxisomal membrane / chaperone-mediated protein folding / brush border membrane / peroxisome / ATPase binding / protein stabilization / protein-containing complex / nucleoplasm / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Emmanouilidis, L. / Schuetz, U. / Tripsianes, K. / Madl, T. / Radke, J. / Rucktaeschel, R. / Wilmanns, M. / Schliebs, W. / Erdmann, R. / Sattler, M. | ||||||
![]() | ![]() Title: Allosteric modulation of peroxisomal membrane protein recognition by farnesylation of the peroxisomal import receptor PEX19. Authors: Emmanouilidis, L. / Schutz, U. / Tripsianes, K. / Madl, T. / Radke, J. / Rucktaschel, R. / Wilmanns, M. / Schliebs, W. / Erdmann, R. / Sattler, M. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 843.6 KB | Display | ![]() |
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PDB format | ![]() | 735.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 415.4 KB | Display | ![]() |
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Full document | ![]() | 548.4 KB | Display | |
Data in XML | ![]() | 58.1 KB | Display | |
Data in CIF | ![]() | 72.2 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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NMR ensembles |
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Components
#1: Protein | Mass: 15664.643 Da / Num. of mol.: 1 / Fragment: UNP residues 161-299 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-FAR / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample |
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Sample conditions | Ionic strength: 50 mM / Label: NMR buffer / pH: 6.5 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software | Name: CNS / Developer: BRUNGER A. T. ET.AL. / Classification: refinement |
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NMR ensemble | Conformers submitted total number: 20 |