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Open data
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Basic information
Entry | Database: PDB / ID: 5woe | ||||||
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Title | Solution structure of the sorting nexin 25 phox-homology domain | ||||||
![]() | Sorting nexin-25 | ||||||
![]() | TRANSPORT PROTEIN / endosome / Mdm1 / PX domain / PXA domain / PXC domain / RGS domain / sorting nexin / SNX / SNX13 / SNX14 / SNX19 / SNX25 | ||||||
Function / homology | ![]() : / receptor catabolic process / type I transforming growth factor beta receptor binding / phosphatidylinositol binding / negative regulation of transforming growth factor beta receptor signaling pathway / protein transport / endosome membrane / intracellular membrane-bounded organelle Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Chin, Y.K.Y. / Mas, C. / Mobli, M. / Collins, B.M. | ||||||
![]() | ![]() Title: Classification of the human phox homology (PX) domains based on their phosphoinositide binding specificities. Authors: Chandra, M. / Chin, Y.K. / Mas, C. / Feathers, J.R. / Paul, B. / Datta, S. / Chen, K.E. / Jia, X. / Yang, Z. / Norwood, S.J. / Mohanty, B. / Bugarcic, A. / Teasdale, R.D. / Henne, W.M. / ...Authors: Chandra, M. / Chin, Y.K. / Mas, C. / Feathers, J.R. / Paul, B. / Datta, S. / Chen, K.E. / Jia, X. / Yang, Z. / Norwood, S.J. / Mohanty, B. / Bugarcic, A. / Teasdale, R.D. / Henne, W.M. / Mobli, M. / Collins, B.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 897.7 KB | Display | ![]() |
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PDB format | ![]() | 771.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 472.9 KB | Display | ![]() |
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Full document | ![]() | 612.8 KB | Display | |
Data in XML | ![]() | 40.4 KB | Display | |
Data in CIF | ![]() | 64.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6ecmC ![]() 6edxC ![]() 6ee0C ![]() 6mbiC C: citing same article ( |
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Similar 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: 14245.309 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Type: solution Contents: 0.8 mM [U-99% 13C; U-99% 15N] SNX25, 20 mM HEPES, 100 mM NaCl, 2 mM DTT, 90% H2O/10% D2O Label: Apo / Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 100 mM / Label: 1 / pH: 7 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE II / Manufacturer: Bruker / Model: AVANCE II / Field strength: 900 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 5 | |||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |