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Yorodumi- PDB-2tsc: STRUCTURE, MULTIPLE SITE BINDING, AND SEGMENTAL ACCOMODATION IN T... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2tsc | ||||||
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Title | STRUCTURE, MULTIPLE SITE BINDING, AND SEGMENTAL ACCOMODATION IN THYMIDYLATE SYNTHASE ON BINDING D/UMP AND AN ANTI-FOLATE | ||||||
Components | THYMIDYLATE SYNTHASE | ||||||
Keywords | TRANSFERASE (METHYLTRANSFERASE) | ||||||
Function / homology | Function and homology information thymidylate synthase / thymidylate synthase activity / dTMP biosynthetic process / dTTP biosynthetic process / response to radiation / regulation of translation / methylation / magnesium ion binding / protein homodimerization activity / RNA binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.97 Å | ||||||
Authors | Montfort, W.R. / Stroud, R.M. | ||||||
Citation | Journal: Biochemistry / Year: 1990 Title: Structure, multiple site binding, and segmental accommodation in thymidylate synthase on binding dUMP and an anti-folate. Authors: Montfort, W.R. / Perry, K.M. / Fauman, E.B. / Finer-Moore, J.S. / Maley, G.F. / Hardy, L. / Maley, F. / Stroud, R.M. #1: Journal: Biochemistry / Year: 1990 Title: Pairwise Specificity and Sequential Binding in Enzyme Catalysis: Thymidylate Synthase Authors: Finer-Moore, J.S. / Montfort, W.R. / Stroud, R.M. #2: Journal: Proteins / Year: 1990 Title: Plastic Adaptation Toward Mutations in Proteins: Structural Comparison of Thymidylate Synthases Authors: Perry, K.M. / Fauman, E.B. / Finer-Moore, J.S. / Montfort, W.R. / Maley, G.F. / Maley, F. / Stroud, R.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2tsc.cif.gz | 120.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2tsc.ent.gz | 98.6 KB | Display | PDB format |
PDBx/mmJSON format | 2tsc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ts/2tsc ftp://data.pdbj.org/pub/pdb/validation_reports/ts/2tsc | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 30457.553 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: P0A884, thymidylate synthase #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.65 % | |||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion / pH: 8 | |||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.97 Å / Rmerge(I) obs: 0.18 |
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-Processing
Software | Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.97→7.5 Å / Rfactor obs: 0.18 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.97→7.5 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.18 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |