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- PDB-1tdc: STRUCTURES OF THYMIDYLATE SYNTHASE WITH A C-TERMINAL DELETION: RO... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1tdc | ||||||
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Title | STRUCTURES OF THYMIDYLATE SYNTHASE WITH A C-TERMINAL DELETION: ROLE OF THE C-TERMINUS IN ALIGNMENT OF D/UMP AND CH2H4FOLATE | ||||||
![]() | THYMIDYLATE SYNTHASE | ||||||
![]() | TRANSFERASE (METHYLTRANSFERASE) | ||||||
Function / homology | ![]() thymidylate synthase / thymidylate synthase activity / dTMP biosynthetic process / dTTP biosynthetic process / methylation / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Perry, K.M. / Carreras, C.W. / Chang, L.C. / Santi, D.V. / Stroud, R.M. | ||||||
![]() | ![]() Title: Structures of thymidylate synthase with a C-terminal deletion: role of the C-terminus in alignment of 2'-deoxyuridine 5'-monophosphate and 5,10-methylenetetrahydrofolate. Authors: Perry, K.M. / Carreras, C.W. / Chang, L.C. / Santi, D.V. / Stroud, R.M. #1: ![]() Title: Atomic Structure of Thymidylate Synthase: Target for Rational Drug Design Authors: Hardy, L.W. / Finer-Moore, J.S. / Montfort, W.R. / Jones, M.O. / Santi, D.V. / Stroud, R.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 | ![]() | 76.6 KB | Display | ![]() |
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PDB format | ![]() | 57.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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
#1: Protein | Mass: 36531.324 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#2: Chemical | ChemComp-UMP / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.98 Å3/Da / Density % sol: 58.75 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.65 Å / Lowest resolution: 9999 Å / Num. obs: 13210 / % possible obs: 96 % / Redundancy: 5.3 % / Rmerge(I) obs: 0.088 |
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Processing
Software |
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Refinement | Rfactor Rwork: 0.21 / Highest resolution: 2.65 Å Details: THE ELECTRON DENSITY FOR THIS STRUCTURE IS POOR IN REGIONS CORRESPONDING TO RESIDUES 21 - 26 AND 90 - 139. | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.65 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.65 Å / Rfactor obs: 0.213 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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