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- PDB-5duw: Crystal structure of the human galectin-4 N-terminal carbohydrate... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5duw | |||||||||
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Title | Crystal structure of the human galectin-4 N-terminal carbohydrate recognition domain in complex with lactose-3'-sulfate | |||||||||
![]() | Galectin-4![]() | |||||||||
![]() | SUGAR BINDING PROTEIN / ![]() ![]() ![]() | |||||||||
Function / homology | ![]() antibacterial peptide biosynthetic process / ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Bum-Erdene, K. / Blanchard, H. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural characterisation of human galectin-4 N-terminal carbohydrate recognition domain in complex with glycerol, lactose, 3'-sulfo-lactose, and 2'-fucosyllactose. Authors: Bum-Erdene, K. / Leffler, H. / Nilsson, U.J. / Blanchard, H. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 138.1 KB | Display | ![]() |
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PDB format | ![]() | 107.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5duuC ![]() 5duvC ![]() 5duxC ![]() 3i8tS 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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1 | ![]()
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2 | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Components
#1: Protein | ![]() Mass: 17473.912 Da / Num. of mol.: 4 Fragment: N-terminal carbohydrate recognition domain (UNP residues 1-155) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() #2: Polysaccharide | 3-O-sulfo-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose / lactose-3'-sulfate #3: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.87 Å3/Da / Density % sol: 34.27 % |
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Crystal grow![]() | Temperature: 293.15 K / Method: vapor diffusion, hanging drop / pH: 8 / Details: 3.5 M sodium formate, 0.1 M Tris |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jul 1, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.7→64.64 Å / Num. obs: 56576 / % possible obs: 99.5 % / Redundancy: 4 % / Rmerge(I) obs: 0.072 / Net I/σ(I): 13.7 |
Reflection shell | Resolution: 1.7→1.73 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.369 / Mean I/σ(I) obs: 3.4 / % possible all: 98.5 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: 3I8T Resolution: 1.7→64.64 Å / SU B: 2.102 / SU ML: 0.068 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.101 / ESU R Free: 0.097 Details: The authors state that the electron density currently modelled as water molecules A304, B302, C301 and D301, which are coordinated by residues ASP72, GLY70 and PHE68 shows potential for ...Details: The authors state that the electron density currently modelled as water molecules A304, B302, C301 and D301, which are coordinated by residues ASP72, GLY70 and PHE68 shows potential for occupation by NA+ ions, which is present in the crystallisation conditions.
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Displacement parameters | Biso mean: 16.73 Å2
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Refinement step | Cycle: LAST / Resolution: 1.7→64.64 Å
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LS refinement shell | Resolution: 1.7→1.744 Å / Rfactor Rfree error: 0.015
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