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- PDB-1ttq: TRYPTOPHAN SYNTHASE (E.C.4.2.1.20) IN THE PRESENCE OF POTASSIUM A... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ttq | ||||||
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Title | TRYPTOPHAN SYNTHASE (E.C.4.2.1.20) IN THE PRESENCE OF POTASSIUM AT ROOM TEMPERATURE | ||||||
![]() | (TRYPTOPHAN SYNTHASE) x 2 | ||||||
![]() | CARBON-OXYGEN LYASE | ||||||
Function / homology | ![]() tryptophan synthase / tryptophan synthase activity / tryptophan biosynthetic process / identical protein binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Rhee, S. / Parris, K. / Ahmed, S. / Miles, E.W. / Davies, D.R. | ||||||
![]() | ![]() 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: The Tryptophan Synthase Multienzyme Complex: Exploring Structure-Function Relationships with X-Ray Crystallography and Mutagenesis Authors: Hyde, C.C. / Miles, E.W. #2: ![]() Title: Three-Dimensional Structure of the Tryptophan Synthase Alpha2Beta2 Multienzyme Complex from Salmonella Typhimurium Authors: Hyde, C.C. / Ahmed, S.A. / Padlan, E.A. / Miles, E.W. / Davies, D.R. #3: ![]() Title: Crystallization and Preliminary X-Ray Crystallographic Data of the Tryptophan Synthase Alpha2Beta2 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 | ![]() | 135 KB | Display | ![]() |
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PDB format | ![]() | 104.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 462 KB | Display | ![]() |
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Full document | ![]() | 479 KB | Display | |
Data in XML | ![]() | 26.5 KB | Display | |
Data in CIF | ![]() | 36.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-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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Atom site foot note | 1: CIS PROLINE - PRO A 28 2: SER A 55 - ASP A 56 OMEGA = 148.59 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: GLY A 61 - PRO A 62 OMEGA = 216.22 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 4: SER A 247 - PRO A 248 OMEGA = 216.00 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 5: CIS PROLINE - PRO B 56 / 6: CIS PROLINE - PRO B 196 |
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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 IN THE PRESENCE OF POTASSIUM / 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 IN THE PRESENCE OF POTASSIUM / Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P00933, UniProt: P0A2K1*PLUS, tryptophan synthase |
#3: Chemical | ChemComp-K / |
#4: Chemical | ChemComp-PLP / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.67 Å3/Da / Density % sol: 53.88 % | |||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 48 % | |||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 7.8 / Method: unknown / Details: pH is adjusted to 7.8 with NaOH | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Nov 27, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→40 Å / Num. obs: 39626 / % possible obs: 77.8 % / Observed criterion σ(I): 0 / Redundancy: 2.5 % / Rmerge(I) obs: 0.079 |
Reflection | *PLUS Num. measured all: 322940 / Rmerge(I) obs: 0.079 |
Reflection shell | *PLUS Highest resolution: 2 Å / Lowest resolution: 2.07 Å / % possible obs: 42.4 % |
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Processing
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Refinement | Resolution: 2→8 Å / σ(F): 2
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Refine analyze | Luzzati coordinate error obs: 0.3 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.204 / Rfactor Rfree: 0.289 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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