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Open data
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Basic information
Entry | Database: PDB / ID: 2csm | ||||||
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Title | TYR-BOUND T-STATE OF YEAST CHORISMATE MUTASE | ||||||
![]() | CHORISMATE MUTASE | ||||||
![]() | COMPLEX (ISOMERASE/PEPTIDE) / ALLOSTERIC PROTEIN / COMPLEX (ISOMERASE-PEPTIDE) / COMPLEX (ISOMERASE-PEPTIDE) complex | ||||||
Function / homology | ![]() tryptophan binding / L-tyrosine binding / tyrosine biosynthetic process / chorismate metabolic process / chorismate mutase / chorismate mutase activity / L-phenylalanine biosynthetic process / aromatic amino acid family biosynthetic process / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Straeter, N. / Hakansson, K. / Lipscomb, W.N. | ||||||
![]() | ![]() Title: Crystal structure of the T state of allosteric yeast chorismate mutase and comparison with the R state. Authors: Strater, N. / Hakansson, K. / Schnappauf, G. / Braus, G. / Lipscomb, W.N. #1: ![]() Title: Location of the Active Site of Allosteric Chorismate Mutase from Saccharomyces Cerevisiae, and Comments on the Catalytic and Regulatory Mechanisms Authors: Xue, Y. / Lipscomb, W.N. #2: ![]() Title: The Crystal Structure of Allosteric Chorismate Mutase at 2.2-A Resolution Authors: Xue, Y. / Lipscomb, W.N. / Graf, R. / Schnappauf, G. / Braus, G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 60.7 KB | Display | ![]() |
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PDB format | ![]() | 45.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 383.8 KB | Display | ![]() |
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Full document | ![]() | 386.5 KB | Display | |
Data in XML | ![]() | 6.6 KB | Display | |
Data in CIF | ![]() | 9.5 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: 29789.172 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Chemical | ChemComp-TYR / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.01 Å3/Da / Density % sol: 59.11 % | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 123 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: SIEMENS / Date: Oct 10, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→20 Å / Num. obs: 9401 / % possible obs: 99.1 % / Observed criterion σ(I): 0 / Redundancy: 3.1 % / Rmerge(I) obs: 0.069 |
Reflection | *PLUS Num. measured all: 29418 |
Reflection shell | *PLUS % possible obs: 97.3 % / Rmerge(I) obs: 0.28 |
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Processing
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Refinement | Resolution: 2.8→7 Å / σ(F): 2
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Displacement parameters | Biso mean: 22.4 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.35 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→7 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 2.9 Å |