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- PDB-4x8x: Crystal structure of Dscam1 isoform 1.9, N-terminal four Ig domains -
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Open data
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Basic information
Entry | Database: PDB / ID: 4x8x | |||||||||
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Title | Crystal structure of Dscam1 isoform 1.9, N-terminal four Ig domains | |||||||||
![]() | Down Syndrome cell adhesion molecule isoform 1.9 | |||||||||
![]() | CELL ADHESION / Ig fold | |||||||||
Function / homology | ![]() detection of molecule of bacterial origin / mushroom body development / detection of mechanical stimulus involved in sensory perception of touch / central nervous system morphogenesis / ventral cord development / axon extension involved in axon guidance / axon guidance receptor activity / dendrite self-avoidance / peripheral nervous system development / axonal fasciculation ...detection of molecule of bacterial origin / mushroom body development / detection of mechanical stimulus involved in sensory perception of touch / central nervous system morphogenesis / ventral cord development / axon extension involved in axon guidance / axon guidance receptor activity / dendrite self-avoidance / peripheral nervous system development / axonal fasciculation / regulation of dendrite morphogenesis / regulation of axonogenesis / plasma membrane => GO:0005886 / neuron development / phagocytosis / antigen binding / axon guidance / cell adhesion / neuron projection / axon / neuronal cell body / dendrite / protein homodimerization activity / identical protein binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Chen, Q. | |||||||||
![]() | ![]() Title: Structural basis of Dscam1 homodimerization: Insights into context constraint for protein recognition Authors: Li, S.A. / Cheng, L. / Yu, Y. / Chen, Q. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 174.9 KB | Display | ![]() |
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PDB format | ![]() | 136.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
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Full document | ![]() | 1.5 MB | Display | |
Data in XML | ![]() | 30.1 KB | Display | |
Data in CIF | ![]() | 42 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4wvrC ![]() 4x5lC ![]() 4x83C ![]() 4x9bC ![]() 4x9fC ![]() 4x9gC ![]() 4x9hC ![]() 4x9iC ![]() 4xb7C ![]() 4xb8C ![]() 4xhqC ![]() 2v5mS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 43584.102 Da / Num. of mol.: 2 / Fragment: N-terminal four Ig domains Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Polysaccharide | alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #4: Chemical | ChemComp-GOL / | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.98 Å3/Da / Density % sol: 58.7 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop Details: 0.1M Bistris pH 5.5, 0.1M Ammonium Acetate, 20% (w/v) PEG 10000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Jul 3, 2014 |
Radiation | Monochromator: SiIII double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→50 Å / Num. obs: 35836 / % possible obs: 99.4 % / Redundancy: 4.5 % / Net I/σ(I): 18.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2V5M Resolution: 2.5→46.744 Å / SU ML: 0.35 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 28.33 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→46.744 Å
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Refine LS restraints |
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LS refinement shell |
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