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Open data
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Basic information
Entry | Database: PDB / ID: 1bks | |||||||||
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Title | TRYPTOPHAN SYNTHASE (E.C.4.2.1.20) FROM SALMONELLA TYPHIMURIUM | |||||||||
![]() | (TRYPTOPHAN SYNTHASE) x 2 | |||||||||
![]() | LYASE / MULTIENZYME COMPLEX / TIM BARREL / PYRIDOXAL PHOSPHATE | |||||||||
Function / homology | ![]() tryptophan synthase / tryptophan synthase activity / tryptophan biosynthetic process / identical protein binding / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Hyde, C.C. | |||||||||
![]() | ![]() Title: Exchange of K+ or Cs+ for Na+ induces local and long-range changes in the three-dimensional structure of the tryptophan synthase alpha2beta2 complex. Authors: Rhee, S. / Parris, K.D. / Ahmed, S.A. / Miles, E.W. / Davies, D.R. #1: ![]() Title: Crystal Structures of a Mutant (Betak87T) Tryptophan Synthase Alpha2Beta2 Complex with Ligands Bound to the Active Sites of the Alpha-and Beta-Subunits Reveal Ligand-Induced Conformational Changes Authors: Rhee, S. / Parris, K.D. / Hyde, C.C. / Ahmed, S.A. / Miles, E.W. / Davies, D.R. #2: ![]() Title: The Tryptophan Synthase Multienzyme Complex: Exploring Structure-Function Relationships with X-Ray Crystallography and Mutagenesis Authors: Hyde, C.C. / Miles, E.W. #3: ![]() Title: Three-Dimensional Structure of the Tryptophan Synthase Alpha 2 Beta 2 Multienzyme Complex from Salmonella Typhimurium Authors: Hyde, C.C. / Ahmed, S.A. / Padlan, E.A. / Miles, E.W. / Davies, D.R. #4: ![]() Title: Crystallization and Preliminary X-Ray Crystallographic Data of the Tryptophan Synthase Alpha 2 Beta 2 Complex from Salmonella Typhimurium Authors: Ahmed, S.A. / Miles, E.W. / Davies, D.R. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 137 KB | Display | ![]() |
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PDB format | ![]() | 109.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 394.9 KB | Display | ![]() |
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Full document | ![]() | 406.8 KB | Display | |
Data in XML | ![]() | 15.3 KB | Display | |
Data in CIF | ![]() | 24.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ttpC ![]() 1ttqC ![]() 1wsy 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: 28698.797 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: STRUCTURE OF WILD TYPE, HOLO-ENZYME / Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 42988.996 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: STRUCTURE OF WILD TYPE, HOLO-ENZYME / Source: (gene. exp.) ![]() ![]() ![]() |
#3: Chemical | ChemComp-NA / |
#4: Chemical | ChemComp-PLP / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54 % |
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Crystal grow | pH: 7.8 / Details: pH 7.8 |
-Data collection
Diffraction | Mean temperature: 300 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Oct 1, 1996 / Details: MIRRORS |
Radiation | Monochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 2.2 Å |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||
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Refinement | Starting model: 1WSY![]() 1wsy Highest resolution: 2.2 Å Details: THE AUTHORS OF THIS ENTRY HAVE NOT PROVIDED REFINEMENT DETAILS. | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.2 Å
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