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- PDB-1tkc: SPECIFICITY OF COENZYME BINDING IN THIAMIN DIPHOSPHATE DEPENDENT ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1tkc | ||||||
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Title | SPECIFICITY OF COENZYME BINDING IN THIAMIN DIPHOSPHATE DEPENDENT ENZYMES: CRYSTAL STRUCTURES OF YEAST TRANSKETOLASE IN COMPLEX WITH ANALOGS OF THIAMIN DIPHOSPHATE | ||||||
![]() | TRANSKETOLASE![]() | ||||||
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Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Schneider, G. / Koenig, S. | ||||||
![]() | ![]() Title: Specificity of coenzyme binding in thiamin diphosphate-dependent enzymes. Crystal structures of yeast transketolase in complex with analogs of thiamin diphosphate. Authors: Konig, S. / Schellenberger, A. / Neef, H. / Schneider, G. #1: ![]() Title: Refined Structure of Transketolase from Saccharomyces Cerevisae at 2.0 Angstrom Resolution Authors: Nikkola, M. / Lindqvist, Y. / Schneider, G. #2: ![]() Title: Yeast Tkl1 Gene Encodes a Transketolase that is Required for Efficient Glycolysis and Biosynthesis of Aromatic Amino Acids Authors: Sundstrom, M. / Lindqvist, Y. / Schneider, G. / Hellman, U. / Ronne, H. #3: ![]() Title: Three-Dimensional Structure of Transketolase, a Thiamine Diphosphate Dependent Enzyme, at 2.5 Angstroms Resolution Authors: Lindqvist, Y. / Schneider, G. / Ermler, U. / Sundstrom, M. #4: ![]() Title: Preliminary Crystallographic Data for Transketolase from Yeast Authors: Schneider, G. / Sundstrom, M. / Lindqvist, Y. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 265.2 KB | Display | ![]() |
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PDB format | ![]() | 211.9 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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.784, 0.001, -0.621), Vector ![]() Details | THE TRANSFORMATION PRESENTED ON MTRIX RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO CHAIN *A*. | |
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Components
#1: Protein | ![]() Mass: 73655.094 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P23254, ![]() #2: Chemical | #3: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 47.87 % | |||||||||||||||||||||||||||||||||||
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Crystal grow![]() | *PLUS Temperature: 4 ℃ / pH: 7.6 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.7 Å / Num. obs: 24737 / % possible obs: 72.5 % / Num. measured all: 56543 / Rmerge(I) obs: 0.053 |
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Processing
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Refinement | Resolution: 2.7→15 Å / σ(F): 1 /
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Refinement step | Cycle: LAST / Resolution: 2.7→15 Å
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.152 / Rfactor Rwork![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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