+Open data
-Basic information
Entry | Database: PDB / ID: 4pzg | ||||||
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Title | Crystal structure of human sorting nexin 10 (SNX10) | ||||||
Components | Sorting nexin-10 | ||||||
Keywords | PROTEIN TRANSPORT / sorting nexin / phox-homology domain | ||||||
Function / homology | Function and homology information extrinsic component of endosome membrane / apical cytoplasm / tooth eruption / gastric acid secretion / 1-phosphatidylinositol binding / phosphatidylinositol phosphate binding / bone mineralization involved in bone maturation / vesicle organization / ruffle assembly / endosome organization ...extrinsic component of endosome membrane / apical cytoplasm / tooth eruption / gastric acid secretion / 1-phosphatidylinositol binding / phosphatidylinositol phosphate binding / bone mineralization involved in bone maturation / vesicle organization / ruffle assembly / endosome organization / protein localization to cilium / cellular homeostasis / protein localization to centrosome / cilium assembly / bone resorption / calcium ion homeostasis / osteoclast differentiation / secretory granule / cellular response to leukemia inhibitory factor / intracellular protein transport / endocytosis / ATPase binding / endosome / centrosome / endoplasmic reticulum / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å | ||||||
Authors | Xu, T. / Xu, J. / Wang, Q. / Liu, J. | ||||||
Citation | Journal: Proteins / Year: 2014 Title: Structure of human SNX10 reveals insights into its role in human autosomal recessive osteopetrosis. Authors: Xu, T. / Xu, J. / Ye, Y. / Wang, Q. / Shu, X. / Pei, D. / Liu, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4pzg.cif.gz | 78 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4pzg.ent.gz | 62.2 KB | Display | PDB format |
PDBx/mmJSON format | 4pzg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4pzg_validation.pdf.gz | 1.8 MB | Display | wwPDB validaton report |
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Full document | 4pzg_full_validation.pdf.gz | 1.8 MB | Display | |
Data in XML | 4pzg_validation.xml.gz | 14.7 KB | Display | |
Data in CIF | 4pzg_validation.cif.gz | 19 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pz/4pzg ftp://data.pdbj.org/pub/pdb/validation_reports/pz/4pzg | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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Unit cell |
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Components on special symmetry positions |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
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-Components
#1: Protein | Mass: 24701.484 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SNX10 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9Y5X0 #2: Chemical | ChemComp-NO3 / #3: Chemical | ChemComp-PE5 / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 5.24 Å3/Da / Density % sol: 76.53 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion / pH: 7 Details: 4 M sodium nitrate, 0.1 M BIS-TRIS propane pH 7.0, vapor diffusion, temperature 293K |
-Data collection
Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.9792 Å | |||||||||||||||||||||
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Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Mar 13, 2014 | |||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||
Radiation wavelength | Wavelength: 0.9792 Å / Relative weight: 1 | |||||||||||||||||||||
Reflection | Resolution: 2.8→49.45 Å / Num. obs: 25144 / % possible obs: 98.7 % / Redundancy: 6.5 % / Rmerge(I) obs: 0.136 / Net I/σ(I): 10.5 / Scaling rejects: 121 | |||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.8→49.45 Å / Cor.coef. Fo:Fc: 0.929 / Cor.coef. Fo:Fc free: 0.894 / SU B: 8.622 / SU ML: 0.164 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.25 / ESU R Free: 0.227 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES: REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 152.81 Å2 / Biso mean: 42.045 Å2 / Biso min: 10.03 Å2
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Refinement step | Cycle: LAST / Resolution: 2.8→49.45 Å
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Refine LS restraints |
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Refine LS restraints NCS | Ens-ID: 1 / Number: 8806 / Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Rms dev position: 0.15 Å / Weight position: 0.05
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LS refinement shell | Resolution: 2.8→2.873 Å / Total num. of bins used: 20
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