+Open data
-Basic information
Entry | Database: PDB / ID: 2mxc | ||||||
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Title | Solution structure of the full length sorting nexin 3 | ||||||
Components | Sorting nexin-3 | ||||||
Keywords | PROTEIN TRANSPORT / PI3P / SNX3 / membrane / endosome | ||||||
Function / homology | Function and homology information negative regulation of early endosome to late endosome transport / late endosome to Golgi transport / protein to membrane docking / negative regulation of protein transport / membrane invagination / WNT ligand biogenesis and trafficking / intralumenal vesicle formation / retromer complex binding / phosphatidylinositol-5-phosphate binding / retromer complex ...negative regulation of early endosome to late endosome transport / late endosome to Golgi transport / protein to membrane docking / negative regulation of protein transport / membrane invagination / WNT ligand biogenesis and trafficking / intralumenal vesicle formation / retromer complex binding / phosphatidylinositol-5-phosphate binding / retromer complex / negative regulation of viral entry into host cell / phosphatidylinositol-3-phosphate binding / early phagosome / endocytic recycling / regulation of Wnt signaling pathway / phosphatidylinositol-4-phosphate binding / phosphatidylinositol-3,5-bisphosphate binding / negative regulation of phagocytosis / clathrin-coated vesicle / response to bacterium / negative regulation of protein catabolic process / positive regulation of neuron projection development / protein transport / early endosome membrane / protein phosphatase binding / early endosome / endosome membrane / Ub-specific processing proteases / extracellular exosome / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Model details | closest to the average, model1 | ||||||
Authors | Lenoir, M.M.L. / Rajesh, S.S.R. / Gruenberg, J.J.G. / Overduin, M.M.O. / Kaur, J.J.K. | ||||||
Citation | Journal: Nat Commun / Year: 2018 Title: Phosphorylation of conserved phosphoinositide binding pocket regulates sorting nexin membrane targeting. Authors: Lenoir, M. / Ustunel, C. / Rajesh, S. / Kaur, J. / Moreau, D. / Gruenberg, J. / Overduin, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2mxc.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb2mxc.ent.gz | 910.4 KB | Display | PDB format |
PDBx/mmJSON format | 2mxc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mx/2mxc ftp://data.pdbj.org/pub/pdb/validation_reports/mx/2mxc | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 19947.605 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SNX3 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O60493 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR / Details: The solution structure of SNX3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.5 mM [U-100% 13C; U-100% 15N] SNX3FL, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 0.5 mM / Component: SNX3FL-1 / Isotopic labeling: [U-100% 13C; U-100% 15N] |
Sample conditions | Ionic strength: 0.100 / pH: 6.5 / Pressure: 1.000 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Varian UnityInova / Manufacturer: Varian / Model: UnityInova / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |