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- PDB-1h5t: Thymidylyltransferase complexed with Thymidylyldiphosphate-glucose -
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Open data
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Basic information
Entry | Database: PDB / ID: 1h5t | |||||||||
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Title | Thymidylyltransferase complexed with Thymidylyldiphosphate-glucose | |||||||||
![]() | (Glucose-1-phosphate thymidylyltransferase ...) x 2 | |||||||||
![]() | TRANSFERASE / PYROPHOSPHATASE / NUCLEOTIDE SUGAR METHABOLISM | |||||||||
Function / homology | ![]() glucose-1-phosphate thymidylyltransferase / glucose-1-phosphate thymidylyltransferase activity / O antigen biosynthetic process / dTDP-rhamnose biosynthetic process / extracellular polysaccharide biosynthetic process / protein homotetramerization / identical protein binding / metal ion binding / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Rosano, C. / Zuccotti, S. / Bolognesi, M. | |||||||||
![]() | ![]() Title: Kinetic and Crystallographic Analyses Support a Sequential-Ordered Bi Bi Catalytic Mechanism for Escherichia Coli Glucose-1-Phosphate Thymidylyltransferase Authors: Zuccotti, S. / Zanardi, D. / Rosano, C. / Sturla, L. / Tonetti, M. / Bolognesi, M. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 246 KB | Display | ![]() |
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PDB format | ![]() | 207.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 903.5 KB | Display | ![]() |
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Full document | ![]() | 941.6 KB | Display | |
Data in XML | ![]() | 31.3 KB | Display | |
Data in CIF | ![]() | 46.4 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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1 |
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Unit cell |
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Components
-Glucose-1-phosphate thymidylyltransferase ... , 2 types, 4 molecules ACDB
#1: Protein | Mass: 32726.465 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P37744, glucose-1-phosphate thymidylyltransferase #2: Protein | | Mass: 32705.363 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P37744, glucose-1-phosphate thymidylyltransferase |
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-Non-polymers , 4 types, 510 molecules ![](data/chem/img/TYD.gif)
![](data/chem/img/DAU.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/DAU.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-TYD / #4: Chemical | ChemComp-DAU / #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: 2.48 Å3/Da / Density % sol: 50.4 % |
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Crystal grow | pH: 5.5 / Details: pH 5.50 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Date: Jun 15, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→30 Å / Num. obs: 98078 / % possible obs: 97.5 % / Observed criterion σ(I): 3 / Redundancy: 4.3 % / Rmerge(I) obs: 0.048 / Net I/σ(I): 14.7 |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 1.9→12 Å
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