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- PDB-1ubs: TRYPTOPHAN SYNTHASE (E.C.4.2.1.20) WITH A MUTATION OF LYS 87->THR... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ubs | ||||||
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Title | TRYPTOPHAN SYNTHASE (E.C.4.2.1.20) WITH A MUTATION OF LYS 87->THR IN THE B SUBUNIT AND IN THE PRESENCE OF LIGAND L-SERINE | ||||||
![]() | (TRYPTOPHAN SYNTHASE) x 2 | ||||||
![]() | LYASE/PEPTIDE / LYASE-PEPTIDE complex | ||||||
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.A. / Miles, E.W. / Davies, D.R. | ||||||
![]() | ![]() 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. #1: ![]() Title: Lysine87 in the B Subunit of Tryptophan Synthase that Forms an Internal Aldimine with Pyridoxal Phosphate Serves Critical Roles in Transimination, Catalysis, and Product Release Authors: Lu, Z. / Nagata, S. / Mcphie, P. / Miles, E.W. #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 Alpha2Beta2 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 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 | ![]() | 141.3 KB | Display | ![]() |
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PDB format | ![]() | 109.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 464.4 KB | Display | ![]() |
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Full document | ![]() | 492.5 KB | Display | |
Data in XML | ![]() | 30.6 KB | Display | |
Data in CIF | ![]() | 43.3 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: CIS PROLINE - PRO B 56 / 3: CIS PROLINE - PRO B 196 |
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Components
-Protein , 2 types, 2 molecules AB
#1: Protein | Mass: 28698.797 Da / Num. of mol.: 1 / Mutation: CHAIN B, K87T Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 42944.965 Da / Num. of mol.: 1 / Mutation: CHAIN B, K87T Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P00933, UniProt: P0A2K1*PLUS, tryptophan synthase |
-Non-polymers , 4 types, 257 molecules ![](data/chem/img/NA.gif)
![](data/chem/img/SER.gif)
![](data/chem/img/PLP.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/SER.gif)
![](data/chem/img/PLP.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-NA / |
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#4: Chemical | ChemComp-SER / |
#5: Chemical | ChemComp-PLP / |
#6: Water | ChemComp-HOH / |
-Details
Nonpolymer details | PLP FORMS THE EXTERNAL ALDIMINE WITH THE AMINO GROUP OF BOUND L-SERINE IN THE BETA SUBUNIT. |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.68 Å3/Da / Density % sol: 54.15 % |
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Crystal grow | pH: 7.8 / Details: pH 7.8 |
Crystal | *PLUS Density % sol: 48 % |
Crystal grow | *PLUS Temperature: 295 K / Method: unknown |
-Data collection
Diffraction | Mean temperature: 295 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: May 19, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→20 Å / Num. obs: 56520 / % possible obs: 89.8 % / Observed criterion σ(I): 0 / Redundancy: 2.5 % / Rmerge(I) obs: 0.079 |
Reflection | *PLUS Rmerge(I) obs: 0.079 |
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Processing
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Refinement | Resolution: 1.9→8 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 1.9→8 Å
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Refine LS restraints |
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