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Open data
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Basic information
Entry | Database: PDB / ID: 1tis | ||||||
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Title | CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE FROM T4 PHAGE | ||||||
![]() | THYMIDYLATE SYNTHASE | ||||||
![]() | TRANSFERASE(METHYLTRANSFERASE) | ||||||
Function / homology | ![]() thymidylate synthase / thymidylate synthase activity / dTMP biosynthetic process / dTTP biosynthetic process / methylation Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Finer-Moore, J. / Stroud, R. | ||||||
![]() | ![]() Title: Crystal structure of thymidylate synthase from T4 phage: component of a deoxynucleoside triphosphate-synthesizing complex. Authors: Finer-Moore, J.S. / Maley, G.F. / Maley, F. / Montfort, W.R. / Stroud, R.M. #1: ![]() Title: Crystal Structure of a Misfolded Protein: Human Thymidylate Synthase Authors: Schiffer, C.A. / Clifton, I.J. / Davisson, V.J. / Hadju, J. / Santi, D.V. / Stroud, R.M. #2: ![]() 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. #3: ![]() 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 | ![]() | 69.8 KB | Display | ![]() |
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PDB format | ![]() | 53.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 379.2 KB | Display | ![]() |
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Full document | ![]() | 396.7 KB | Display | |
Data in XML | ![]() | 9.5 KB | Display | |
Data in CIF | ![]() | 13.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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: 33116.211 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#2: Chemical | ChemComp-PO4 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 49.96 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 9999 Å / Num. obs: 6186 / % possible obs: 65 % / Num. measured all: 30518 / Rmerge(I) obs: 0.068 |
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Reflection shell | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 2.9 Å / % possible obs: 12 % / Num. unique obs: 192 / Num. measured obs: 227 / Rmerge(I) obs: 0.257 |
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Processing
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Refinement | Resolution: 2.7→50 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 2.7→50 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.199 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 28 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 3.8 |