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Open data
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Basic information
Entry | Database: PDB / ID: 5csm | ||||||
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Title | YEAST CHORISMATE MUTASE, T226S MUTANT, COMPLEX WITH TRP | ||||||
![]() | CHORISMATE MUTASE | ||||||
![]() | COMPLEX (ISOMERASE/PEPTIDE) / CHORISMATE PYRUVATEMUTASE / ALLOSTERIC PROTEIN / COMPLEX (ISOMERASE-PEPTIDE) / TRANSITION STATE ANALOG / 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. / Schnappauf, G. / Braus, G. / Lipscomb, W.N. | ||||||
![]() | ![]() Title: Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures. Authors: Strater, N. / Schnappauf, G. / Braus, G. / Lipscomb, W.N. #1: ![]() 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. #2: ![]() 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. #3: ![]() 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 | ![]() | 64.6 KB | Display | ![]() |
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PDB format | ![]() | 47.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 379.2 KB | Display | ![]() |
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Full document | ![]() | 380.9 KB | Display | |
Data in XML | ![]() | 6.3 KB | Display | |
Data in CIF | ![]() | 9.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3csmC ![]() 4csmC ![]() 1csmS S: Starting model for refinement 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
#1: Protein | Mass: 29944.457 Da / Num. of mol.: 1 / Mutation: T226S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: RH1242 / Plasmid: PME605 / Production host: ![]() ![]() |
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#2: Chemical | ChemComp-TRP / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 49.25 % | ||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 5 Details: HANGING DROP, 19 % PEG 3350, 3 MM DTT, 0.16 M SODIUM ACETATE PH 5.0, 16 MM TRYPTOPHAN, 10 MG/ML PROTEIN, vapor diffusion - hanging drop | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: SIEMENS-NICOLET X100 / Detector: AREA DETECTOR / Date: Jun 27, 1996 / Details: SUPPER DOUBLE-MIRROR, NI-COATED |
Radiation | Monochromator: DOUBLE CRYSTAL SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. obs: 18951 / % possible obs: 96.6 % / Observed criterion σ(I): 0 / Redundancy: 2.2 % / Rmerge(I) obs: 0.055 |
Reflection shell | Resolution: 2→2.1 Å / Rmerge(I) obs: 0.196 / % possible all: 88.8 |
Reflection | *PLUS Num. measured all: 40918 |
Reflection shell | *PLUS % possible obs: 88.8 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1CSM Resolution: 2→7 Å / σ(F): 2 Details: RESIDUES THR 218 - GLU 223 ARE NOT VISIBLE IN THE ELECTRON DENSITY MAPS (LOOP REGION). RESIDUES THR 218 - GLU 223 ARE NOT VISIBLE IN THE ELECTRON DENSITY MAPS (LOOP REGION).
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Displacement parameters | Biso mean: 26.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→7 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.09 Å / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Lowest resolution: 2.1 Å / Rfactor obs: 0.255 |