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Yorodumi- PDB-1h5t: Thymidylyltransferase complexed with Thymidylyldiphosphate-glucose -
+Open data
-Basic information
Entry | Database: PDB / ID: 1h5t | |||||||||
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Title | Thymidylyltransferase complexed with Thymidylyldiphosphate-glucose | |||||||||
Components | (Glucose-1-phosphate thymidylyltransferase ...) x 2 | |||||||||
Keywords | TRANSFERASE / PYROPHOSPHATASE / NUCLEOTIDE SUGAR METHABOLISM | |||||||||
Function / homology | Function and homology information 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 | Escherichia coli (E. coli) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | |||||||||
Authors | Rosano, C. / Zuccotti, S. / Bolognesi, M. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 2001 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1h5t.cif.gz | 246 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1h5t.ent.gz | 207.8 KB | Display | PDB format |
PDBx/mmJSON format | 1h5t.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h5/1h5t ftp://data.pdbj.org/pub/pdb/validation_reports/h5/1h5t | 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
-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.) Escherichia coli (E. coli) / Gene: rfbA, rmlA, rmlA1, b2039, JW2024 / Production host: Escherichia coli (E. coli) 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.) Escherichia coli (E. coli) / Gene: rfbA, rmlA, rmlA1, b2039, JW2024 / Production host: Escherichia coli (E. coli) References: UniProt: P37744, glucose-1-phosphate thymidylyltransferase |
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-Non-polymers , 4 types, 510 molecules
#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: X-RAY DIFFRACTION / Number of used crystals: 1 |
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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: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.933 |
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 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.9→12 Å / SU ML: 0.1019 / ESU R Free: 0.1449 / Details: PROLINE 19 IS IN CIS CONFORMATION
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Refinement step | Cycle: LAST / Resolution: 1.9→12 Å
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