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Yorodumi- PDB-3lfi: Crystal structure of fructosyltransferase (wild-type) from A. jap... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3lfi | ||||||
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Title | Crystal structure of fructosyltransferase (wild-type) from A. japonicus in complex with glucose | ||||||
Components | Fructosyltransferase | ||||||
Keywords | HYDROLASE / Protein-oligosaccharide complex / Five bladed beta-propeller fold | ||||||
Function / homology | Function and homology information sucrose alpha-glucosidase activity / sucrose catabolic process / cytoplasm Similarity search - Function | ||||||
Biological species | Aspergillus japonicus (mold) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Chuankhayan, P. / Chen, C.J. / Chiang, C.M. | ||||||
Citation | Journal: To be Published Title: Crystal structure of Aspergillus japonicus fructosyltransferase complex with donor/acceptor substrates reveal complete sbusites in the active site for catalysis Authors: Chuankhayan, P. / Hsieh, C.Y. / Huang, Y.C. / Hsieh, Y.Y. / Guan, H.H. / Hsieh, Y.C. / Tien, Y.C. / Chen, C.D. / Chaing, C.M. / Chen, C.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3lfi.cif.gz | 255.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3lfi.ent.gz | 205.9 KB | Display | PDB format |
PDBx/mmJSON format | 3lfi.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lf/3lfi ftp://data.pdbj.org/pub/pdb/validation_reports/lf/3lfi | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 68986.570 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aspergillus japonicus (mold) / Production host: Escherichia coli (E. coli) / References: UniProt: Q1W3Z7*PLUS #2: Sugar | #3: Water | ChemComp-HOH / | Sequence details | A SEQUENCE DATABASE REFERENCE FOR THIS PROTEIN DOES NOT CURRENTLY EXIST. THE AUTHOR HAS ALREADY ...A SEQUENCE DATABASE REFERENCE FOR THIS PROTEIN DOES NOT CURRENTLY EXIST. THE AUTHOR HAS ALREADY DEPOSITED THE DNA SEQUENCE OF THIS PROTEIN IN GENBANK DATABASES, THE ACCESS NUMBER IS GU356596. | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 2.54 Å3/Da / Density % sol: 51.61 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: 8% PEG 3350, 0.1M Sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation |
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Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | ||||||||||||||||||
Reflection | Resolution: 2→30 Å / Num. all: 101087 / Num. obs: 91860 / % possible obs: 98 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.7 % / Rmerge(I) obs: 0.073 / Rsym value: 0.073 / Net I/σ(I): 23.1 | ||||||||||||||||||
Reflection shell | Resolution: 2→2.1 Å / Redundancy: 5.9 % / Rmerge(I) obs: 0.357 / Mean I/σ(I) obs: 4.4 / Num. unique all: 9602 / Rsym value: 0.357 / % possible all: 94 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→30 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2→30 Å
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Refine LS restraints |
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