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Open data
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Basic information
Entry | Database: PDB / ID: 1e9f | ||||||
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Title | Mutant human thymidylate kinase complexed with TMP and ADP | ||||||
![]() | THYMIDYLATE KINASE![]() | ||||||
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Function / homology | ![]() thymidine biosynthetic process / dUDP biosynthetic process / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Ostermann, N. / Lavie, A. / Padiyar, S. / Brundiers, R. / Veit, T. / Reinstein, J. / Goody, R.S. / Konrad, M. / Schlichting, I. | ||||||
![]() | ![]() Title: Potentiating Azt Activation: Structures of Wildtype and Mutant Human Thymidylate Kinase Suggest Reasons for the Mutants' Improved Kinetics with the HIV Prodrug Metabolite Aztmp Authors: Ostermann, N. / Lavie, A. / Padiyar, S. / Brundiers, R. / Veit, T. / Reintein, J. / Goody, R.S. / Konrad, M. / Schlichting, I. #1: ![]() Title: Insights Into the Phosphoryltransfer Mechanism of Human Thymidylate Kinase Gained from Crystal Structures of Enzyme Complexes Along the Reaction Coordinate. Authors: Ostermann, N. / Schlichting, I. / Brundiers, R. / Konrad, M. / Reinstein, J. / Veit, T. / Goody, R.S. / Lavie, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 61.2 KB | Display | ![]() |
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PDB format | ![]() | 43.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1e98C ![]() 1e99C ![]() 1e9aC ![]() 1e9bC ![]() 1e9cC ![]() 1e9dC ![]() 1e9eC C: citing same article ( |
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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 on special symmetry positions |
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Components
#1: Protein | ![]() Mass: 24223.729 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() Production host: ![]() ![]() ![]() ![]() | ||||||
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#2: Chemical | ChemComp-TMP / | ||||||
#3: Chemical | ChemComp-ADP / ![]() | ||||||
#4: Chemical | #5: Water | ChemComp-HOH / | ![]() Compound details | CHAIN A - ENGINEERED MUTATION ARG200ALA, ARG16GLY CHAIN A - (GLY SER HIS) INSERTED AT THE N- ...CHAIN A - ENGINEERED | Sequence details | SAMPLE COMTAINS SER183, ILE184, ASP190, AND A ILE191 (CONFIRMED BY THE DNA SEQUENCE AND ELECTRON ...SAMPLE COMTAINS SER183, ILE184, ASP190, AND A ILE191 (CONFIRMED BY THE DNA SEQUENCE AND ELECTRON DENSITY OF SIDE-CHAINS). POSSIBLE ERROR IN SWISSPROT ENTRY. | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.55 Å3/Da / Density % sol: 51.75 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | Temperature: 293 K / Method: vapor diffusion / pH: 8 Details: VAPOR DIFFUSION AT 293 K MIXING 2 MICROLITERS OF A SOLUTION CONTAINING THE ENZYME, NUCLEOTIDES, AND 50 MM MGCL2 WITH 2 MICROLITERS OF A SOLUTION CONTAINING 21% PEG 3350, 100 MM TRIS HCL PH 8. ...Details: VAPOR DIFFUSION AT 293 K MIXING 2 MICROLITERS OF A SOLUTION CONTAINING THE ENZYME, NUCLEOTIDES, AND 50 MM MGCL2 WITH 2 MICROLITERS OF A SOLUTION CONTAINING 21% PEG 3350, 100 MM TRIS HCL PH 8.0 AND 50 MICROLITERS OF DEAD SEA WATER. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, hanging drop / Details: Ostermann, N., (2000) Structure (London), 8, 629. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Radiation | Monochromator: YES / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.9→70 Å / Num. obs: 19646 / % possible obs: 96.8 % / Redundancy: 4.9 % / Rsym value: 0.054 / Net I/σ(I): 17 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 4.3 % / Mean I/σ(I) obs: 3.2 / Rsym value: 0.144 / % possible all: 97.3 |
Reflection | *PLUS Lowest resolution: 70 Å / Num. measured all: 96858 / Rmerge(I) obs: 0.054 |
Reflection shell | *PLUS % possible obs: 97.3 % / Rmerge(I) obs: 0.144 |
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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→70 Å
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 70 Å / Rfactor obs: 0.226 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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