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Yorodumi- PDB-1qkj: T4 Phage B-Glucosyltransferase, Substrate Binding and Proposed Ca... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1qkj | ||||||
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Title | T4 Phage B-Glucosyltransferase, Substrate Binding and Proposed Catalytic Mechanism | ||||||
Components | BETA-GLUCOSYLTRANSFERASE | ||||||
Keywords | TRANSFERASE (GLUCOSYLTRANSFERASE) / TRANSFERASE(GLUCOSYLTRANSFERASE) | ||||||
Function / homology | Function and homology information DNA beta-glucosyltransferase / DNA beta-glucosyltransferase activity / symbiont-mediated evasion of host restriction-modification system / DNA modification Similarity search - Function | ||||||
Biological species | BACTERIOPHAGE T4 (virus) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Morera, S. / Imberty, I. / Aschke-Sonnenborn, U. / Ruger, W. / Freemont, P.S. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1999 Title: T4 Phage Beta-Glucosyltransferase: Substrate Binding and Proposed Catalytic Mechanism Authors: Morera, S. / Imberty, A. / Aschke-Sonnenborn, U. / Ruger, W. / Freemont, P.S. #1: Journal: Embo J. / Year: 1994 Title: Crystal Structure of the DNA Modifying Enzyme Beta-Glucosyltransferase in the Presence and Absence of the Substrate Uridine Diphosphoglucose Authors: Vrielink, A. / Rueger, W. / Driessen, H.P.C. / Freemont, P.S. #2: Journal: J.Mol.Biol. / Year: 1988 Title: Crystallization and Preliminary X-Ray Studies of T4 Phage Beta-Glucosyltransferase Authors: Freemont, P.S. / Rueger, W. #3: Journal: Nucleic Acids Res. / Year: 1985 Title: T4-Induced Alpha- and Beta-Glucosyltransferase: Cloning of the Genes and a Comparison of Their Products Based on Sequencing Data Authors: Tomaschewski, J. / Gram, H. / Crabb, J.W. / Ruger, W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qkj.cif.gz | 87.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qkj.ent.gz | 64.5 KB | Display | PDB format |
PDBx/mmJSON format | 1qkj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qk/1qkj ftp://data.pdbj.org/pub/pdb/validation_reports/qk/1qkj | HTTPS FTP |
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-Related structure data
Related structure data | 1c3jC 1bguS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | BIOLOGICAL_UNIT: MONOMER |
-Components
#1: Protein | Mass: 40719.879 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) BACTERIOPHAGE T4 (virus) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P04547, DNA beta-glucosyltransferase |
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#2: Chemical | ChemComp-UDP / |
#3: Water | ChemComp-HOH / |
Compound details | BETA-GLUCOSYLTRANSFERASE TRANSFERS A BETA-D-GLUCOSYL RESIDUE FROM UDP-GLUCOSE TO AN ...BETA-GLUCOSYLTR |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.63 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.4 / Details: pH 7.40 | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM02 / Wavelength: 1 |
Detector | Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→20 Å / Num. obs: 16930 / % possible obs: 96 % / Redundancy: 5 % / Rsym value: 0.41 |
Reflection | *PLUS Num. measured all: 57848 / Rmerge(I) obs: 0.041 |
Reflection shell | *PLUS % possible obs: 78 % / Rmerge(I) obs: 0.23 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1BGU Resolution: 2.3→20 Å / σ(F): 2
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Displacement parameters | Biso mean: 17.49 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→20 Å
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Refine LS restraints |
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Software | *PLUS Version: 3.84 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection obs: 16489 / Rfactor obs: 0.198 / Rfactor Rfree: 0.29 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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