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- PDB-2wvj: Mutation of Thr163 to Ser in Human Thymidine Kinase Shifts the Sp... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2wvj | ||||||
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Title | Mutation of Thr163 to Ser in Human Thymidine Kinase Shifts the Specificity from Thymidine towards the Nucleoside Analogue Azidothymidine | ||||||
![]() | THYMIDINE KINASE, CYTOSOLIC | ||||||
![]() | TRANSFERASE / ZINC-BINDING DOMAIN / DEOXYRIBONUCLEOSIDE KINASE / FEEDBACK INHIBITOR / NUCLEOTIDE-BINDING / KINASE / CYTOPLASM / ATP-BINDING / DNA SYNTHESIS / PHOSPHOPROTEIN / PHOSPHORYLATION | ||||||
Function / homology | ![]() DNA synthesis involved in mitotic DNA replication / thymidine biosynthetic process / thymidine metabolic process / thymidine kinase / thymidine kinase activity / Pyrimidine salvage / nucleobase-containing compound metabolic process / G1/S-Specific Transcription / protein homotetramerization / phosphorylation ...DNA synthesis involved in mitotic DNA replication / thymidine biosynthetic process / thymidine metabolic process / thymidine kinase / thymidine kinase activity / Pyrimidine salvage / nucleobase-containing compound metabolic process / G1/S-Specific Transcription / protein homotetramerization / phosphorylation / zinc ion binding / ATP binding / identical protein binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Skovgaard, T. / Uhlin, U. / Munch-Petersen, B. | ||||||
![]() | ![]() Title: Comparative Active-Site Mutation Study of Human and Caenorhabditis Elegans Thymidine Kinase 1. Authors: Skovgaard, T. / Uhlin, U. / Munch-Petersen, B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 289.6 KB | Display | ![]() |
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PDB format | ![]() | 233.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.7 MB | Display | ![]() |
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Full document | ![]() | 2.8 MB | Display | |
Data in XML | ![]() | 62.8 KB | Display | |
Data in CIF | ![]() | 86.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1xbtS S: Starting model for refinement |
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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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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 21312.975 Da / Num. of mol.: 8 / Fragment: RESIDUES 1-193 / Mutation: YES Source method: isolated from a genetically manipulated source Details: TTP FEEDBACK INHIBITOR / Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-TTP / #3: Chemical | ChemComp-ZN / #4: Chemical | #5: Water | ChemComp-HOH / | Compound details | ENGINEERED RESIDUE IN CHAIN A, THR 163 TO SER ENGINEERED RESIDUE IN CHAIN B, THR 163 TO SER ...ENGINEERED | Nonpolymer details | THYMIDINE 5' TRIPHOSPHATE (TTP): TTP HAS TWO CONFORMATIONS IN EACH SITE. IN PROTEIN CHAINS A,B,C,E ...THYMIDINE 5' TRIPHOSPHA | Sequence details | TRUNCATION | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 43 % / Description: NONE |
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 5.6 Details: HANGING DROPS WITH EQUAL AMOUNTS OF PROTEIN, 10 MG PER ML CONTAINING 5 MM TTP AND TRAY SOLUTION COMPOSED OF SODIUM CITRATE PH 5.6, 2-PROPANOL AND PEG 4000. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Apr 23, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8726 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→88.39 Å / Num. obs: 85203 / % possible obs: 99.9 % / Observed criterion σ(I): -3.7 / Redundancy: 3.7 % / Biso Wilson estimate: 24.5 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 10.56 |
Reflection shell | Resolution: 2.2→2.22 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.37 / Mean I/σ(I) obs: 3.4 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1XBT Resolution: 2.2→49.814 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.917 / SU B: 4.75 / SU ML: 0.123 / Cross valid method: THROUGHOUT / ESU R: 0.218 / ESU R Free: 0.185 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. LOOP CONTAINING RESIDUES 64 TO 73 IS MISSING IN THE STRUCTURE AS ARE RESIDUES BEFORE AMINO ACID 18 AND AFTER 192.
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Solvent computation | Ion probe radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 21.101 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→49.814 Å
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Refine LS restraints |
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