+Open data
-Basic information
Entry | Database: PDB / ID: 5dg1 | |||||||||
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Title | Sugar binding protein - human galectin-2 | |||||||||
Components | Galectin-2 | |||||||||
Keywords | SUGAR BINDING PROTEIN / Galectin-2 | |||||||||
Function / homology | Function and homology information galectin complex / galactoside binding / T cell homeostasis / cell-cell adhesion / positive regulation of inflammatory response / carbohydrate binding / positive regulation of apoptotic process Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 3.2 Å | |||||||||
Authors | Su, J.Y. / Si, Y.L. | |||||||||
Citation | Journal: Acta Biochim.Biophys.Sin. / Year: 2016 Title: Human galectin-2 interacts with carbohydrates and peptides non-classically: new insight from X-ray crystallography and hemagglutination. Authors: Si, Y. / Feng, S. / Gao, J. / Wang, Y. / Zhang, Z. / Meng, Y. / Zhou, Y. / Tai, G. / Su, J. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5dg1.cif.gz | 307.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5dg1.ent.gz | 252.1 KB | Display | PDB format |
PDBx/mmJSON format | 5dg1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5dg1_validation.pdf.gz | 1.3 MB | Display | wwPDB validaton report |
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Full document | 5dg1_full_validation.pdf.gz | 1.3 MB | Display | |
Data in XML | 5dg1_validation.xml.gz | 31.7 KB | Display | |
Data in CIF | 5dg1_validation.cif.gz | 41.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dg/5dg1 ftp://data.pdbj.org/pub/pdb/validation_reports/dg/5dg1 | HTTPS FTP |
-Related structure data
Related structure data | 5dg2C 5ewsC 1hlcS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
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-Components
#1: Protein | Mass: 14945.729 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: LGALS2 / Production host: Escherichia coli (E. coli) / References: UniProt: P05162 #2: Polysaccharide | |
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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: 2.16 Å3/Da / Density % sol: 43.1 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / Details: Sodium citrate, Amino Sulfate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SEALED TUBE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Apr 23, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 3.2→46.06 Å / Num. obs: 13129 / % possible obs: 100 % / Redundancy: 6.9 % / Net I/σ(I): 10.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1HLC Resolution: 3.2→46.057 Å / SU ML: 0.42 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 33.01 / 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 | |||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 172.84 Å2 / Biso mean: 50.6661 Å2 / Biso min: 12.67 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 3.2→46.057 Å
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Refine LS restraints NCS |
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