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- PDB-1esq: CRYSTAL STRUCTURE OF THIAZOLE KINASE MUTANT (C198S) WITH ATP AND ... -
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Basic information
Entry | Database: PDB / ID: 1esq | ||||||
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Title | CRYSTAL STRUCTURE OF THIAZOLE KINASE MUTANT (C198S) WITH ATP AND THIAZOLE PHOSPHATE. | ||||||
![]() | HYDROXYETHYLTHIAZOLE KINASE | ||||||
![]() | TRANSFERASE / trimer / alpha-beta protein | ||||||
Function / homology | ![]() hydroxyethylthiazole kinase / hydroxyethylthiazole kinase activity / phosphomethylpyrimidine kinase activity / hydroxymethylpyrimidine kinase activity / thiamine diphosphate biosynthetic process / thiamine biosynthetic process / phosphorylation / magnesium ion binding / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Campobasso, N. / Mathews, I.I. / Begley, T.P. / Ealick, S.E. | ||||||
![]() | ![]() Title: Crystal structure of 4-methyl-5-beta-hydroxyethylthiazole kinase from Bacillus subtilis at 1.5 A resolution. Authors: Campobasso, N. / Mathews, I.I. / Begley, T.P. / Ealick, S.E. #1: ![]() Title: Thiamin Biosynthesis in Prokaryotes. Authors: Begley, T.P. / Downs, D. / Ealick, S. / McLafferty, F. / Van Loon, D. / Taylor, S. / Campobasso, N. / Chiu, H.J. / Kinsland, C. / Reddick, J.J. / Xi, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 161.8 KB | Display | ![]() |
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PDB format | ![]() | 126.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.3 MB | Display | ![]() |
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Full document | ![]() | 1.3 MB | Display | |
Data in XML | ![]() | 35.3 KB | Display | |
Data in CIF | ![]() | 46.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Protein , 1 types, 3 molecules ABC
#1: Protein | Mass: 29629.633 Da / Num. of mol.: 3 / Mutation: C198S Source method: isolated from a genetically manipulated source Details: N-TERMINAL HIS TAG / Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 5 types, 192 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/ATP.gif)
![](data/chem/img/TZP.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/ATP.gif)
![](data/chem/img/TZP.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-MG / #3: Chemical | #4: Chemical | #5: Chemical | ChemComp-SO4 / | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.21 Å3/Da / Density % sol: 44.47 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.6 Details: 21%PEG4K, 0.1M Ammonium sulfate, 0.1M Tris. HCl, pH 7.6, VAPOR DIFFUSION, HANGING DROP, temperature 18K | ||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 44 % | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8.6 / Method: vapor diffusion, sitting dropDetails: drop consists of equal volume of protein and reservoir solutions | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ![]() ![]() |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0332 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→20 Å / Num. all: 26976 / Num. obs: 26796 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.1 % / Biso Wilson estimate: 37.3 Å2 / Rmerge(I) obs: 0.068 / Net I/σ(I): 7.9 |
Reflection shell | Resolution: 2.5→2.59 Å / Redundancy: 4 % / Rmerge(I) obs: 0.258 / Num. unique all: 2710 / % possible all: 100 |
Reflection | *PLUS Num. measured all: 111367 |
Reflection shell | *PLUS % possible obs: 100 % / Mean I/σ(I) obs: 4.3 |
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Processing
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Refinement | Resolution: 2.5→20 Å / σ(F): 1 / σ(I): 0.5 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.5→20 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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