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Yorodumi- PDB-3asz: CMP-complex structure of uridine kinase from Thermus thermophilus HB8 -
+Open data
-Basic information
Entry | Database: PDB / ID: 3asz | ||||||
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Title | CMP-complex structure of uridine kinase from Thermus thermophilus HB8 | ||||||
Components | Uridine kinase | ||||||
Keywords | TRANSFERASE / cytidine phosphorylation | ||||||
Function / homology | Function and homology information uridine/cytidine kinase / CTP salvage / uridine kinase activity / cytidine kinase activity / UMP salvage / phosphorylation / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | Thermus thermophilus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.25 Å | ||||||
Authors | Tomoike, F. / Nakagawa, N. / Kuramitsu, S. / Masui, R. | ||||||
Citation | Journal: Biochemistry / Year: 2011 Title: A Single Amino Acid Limits the Substrate Specificity of Thermus thermophilus Uridine-Cytidine Kinase to Cytidine Authors: Tomoike, F. / Nakagawa, N. / Kuramitsu, S. / Masui, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3asz.cif.gz | 96 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3asz.ent.gz | 73.7 KB | Display | PDB format |
PDBx/mmJSON format | 3asz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/as/3asz ftp://data.pdbj.org/pub/pdb/validation_reports/as/3asz | 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: 23709.723 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermus thermophilus (bacteria) / Strain: HB8 / Gene: udk, TTHA0578 / Plasmid: pET11a / Production host: Escherichia coli (E. coli) / References: UniProt: Q5SKR5, uridine/cytidine kinase #2: Chemical | #3: Water | ChemComp-HOH / | |
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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: 2.81 Å3/Da / Density % sol: 56.16 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion / pH: 8 Details: 50%(w/v) PEG 200, 0.1M Tris-HCl, pH 8.0, VAPOR DIFFUSION, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL26B1 / Wavelength: 1 Å |
Detector | Type: RIGAKU JUPITER 210 / Detector: CCD / Date: Feb 22, 2008 |
Radiation | Monochromator: transparent diamond double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.15→50 Å / Num. obs: 29582 / Observed criterion σ(F): 0 |
Reflection shell | Resolution: 2.15→2.23 Å / Redundancy: 5.6 % / Rmerge(I) obs: 0.858 / Mean I/σ(I) obs: 7.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: uridine cytidine kinase2 from Homo Sapiens Resolution: 2.25→50 Å / σ(F): 0
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Solvent computation | Bsol: 54.1722 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 34.0823 Å2
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Refinement step | Cycle: LAST / Resolution: 2.25→50 Å
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Refine LS restraints |
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Xplor file |
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