+Open data
-Basic information
Entry | Database: PDB / ID: 6a1x | ||||||
---|---|---|---|---|---|---|---|
Title | Charcot-Leyden crystal protein/Galectin-10 variant W127A | ||||||
Components | Galectin-10 | ||||||
Keywords | PROTEIN BINDING | ||||||
Function / homology | Function and homology information regulation of activated T cell proliferation / regulation of T cell cytokine production / T cell apoptotic process / regulation of T cell anergy / cysteine-type endopeptidase activity involved in apoptotic process / carbohydrate binding / collagen-containing extracellular matrix / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.99 Å | ||||||
Authors | Su, J. | ||||||
Funding support | China, 1items
| ||||||
Citation | Journal: Glycobiology / Year: 2019 Title: Identification of key amino acid residues determining ligand binding specificity, homodimerization and cellular distribution of human galectin-10 Authors: Su, J. / Song, C. / Si, Y. / Cui, L. / Yang, T. / Li, Y. / Wang, H. / Tai, G. / Zhou, Y. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 6a1x.cif.gz | 44.3 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb6a1x.ent.gz | 29.9 KB | Display | PDB format |
PDBx/mmJSON format | 6a1x.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6a1x_validation.pdf.gz | 423.8 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 6a1x_full_validation.pdf.gz | 424.8 KB | Display | |
Data in XML | 6a1x_validation.xml.gz | 8.8 KB | Display | |
Data in CIF | 6a1x_validation.cif.gz | 11.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a1/6a1x ftp://data.pdbj.org/pub/pdb/validation_reports/a1/6a1x | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
Unit cell |
| |||||||||
Components on special symmetry positions |
|
-Components
#1: Protein | Mass: 16638.979 Da / Num. of mol.: 1 / Fragment: UNP residues 1-142 / Mutation: W127A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CLC / Production host: Escherichia coli (E. coli) / References: UniProt: Q05315 |
---|---|
#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.72 Å3/Da / Density % sol: 54.75 % |
---|---|
Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / Details: Bistris |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL18U1 / Wavelength: 0.98 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Nov 11, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 1.99→19.472 Å / Num. obs: 13492 / % possible obs: 99.9 % / Redundancy: 17.9 % / Net I/σ(I): 15.8 |
Reflection shell | Resolution: 1.99→2.04 Å |
-Processing
Software | Name: PHENIX / Classification: refinement | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.99→19.472 Å / SU ML: 0.19 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 17.88 / Stereochemistry target values: ML
| ||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||
Displacement parameters | Biso max: 57.45 Å2 / Biso mean: 18.8825 Å2 / Biso min: 5.39 Å2 | ||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 1.99→19.472 Å
|