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Open data
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Basic information
| Entry | Database: PDB / ID: 8yfh | ||||||
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| Title | Structure of alpha-1,3-glucanase agn1 | ||||||
Components | Glucan endo-1,3-alpha-glucosidase agn1 | ||||||
Keywords | HYDROLASE / glucanase | ||||||
| Function / homology | Function and homology informationcell septum edging catabolic process / glucan endo-1,3-alpha-glucosidase / glucan endo-1,3-alpha-glucosidase activity / fungal-type cell wall disassembly involved in conjugation with cellular fusion / mating projection actin fusion focus / mating projection tip / extracellular region Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||
Authors | Horaguch, Y. / Yano, S. / Makabe, K. | ||||||
| Funding support | 1items
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Citation | Journal: To Be PublishedTitle: Structure of alpha-1,3-glucanase agn1 Authors: Horaguchi, Y. / Yano, S. / Makabe, K. | ||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8yfh.cif.gz | 308.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8yfh.ent.gz | 212.1 KB | Display | PDB format |
| PDBx/mmJSON format | 8yfh.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8yfh_validation.pdf.gz | 426.8 KB | Display | wwPDB validaton report |
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| Full document | 8yfh_full_validation.pdf.gz | 428.5 KB | Display | |
| Data in XML | 8yfh_validation.xml.gz | 59.8 KB | Display | |
| Data in CIF | 8yfh_validation.cif.gz | 85.2 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yf/8yfh ftp://data.pdbj.org/pub/pdb/validation_reports/yf/8yfh | HTTPS FTP |
-Related structure data
| Similar structure data | Similarity search - Function & homology F&H Search |
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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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| Unit cell |
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Components
| #1: Protein | Mass: 44534.848 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: agn1, SPAC14C4.09 / Production host: ![]() References: UniProt: O13716, glucan endo-1,3-alpha-glucosidase #2: Water | ChemComp-HOH / | Has protein modification | N | |
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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: 3.15 Å3/Da / Density % sol: 60.97 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / Details: 0.9M Disodium Malonate, 0.1M HEPES pH 7.0 |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: BL-5A / Wavelength: 1 Å |
| Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jun 24, 2022 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
| Reflection | Resolution: 1.78→48.01 Å / Num. obs: 158150 / % possible obs: 100 % / Redundancy: 5.2 % / Biso Wilson estimate: 24.34 Å2 / CC1/2: 0.999 / Net I/σ(I): 21.3 |
| Reflection shell | Resolution: 1.78→1.81 Å / Num. unique obs: 7813 / CC1/2: 0.791 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.8→19.99 Å / SU ML: 0.1602 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 19.0924 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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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 mean: 28.01 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 1.8→19.99 Å
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| Refine LS restraints |
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| LS refinement shell |
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