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- PDB-1cw2: CRYSTAL STRUCTURE OF THE COMPLEX OF BACTERIAL TRYPTOPHAN SYNTHASE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1cw2 | ||||||
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Title | CRYSTAL STRUCTURE OF THE COMPLEX OF BACTERIAL TRYPTOPHAN SYNTHASE WITH THE TRANSITION STATE ANALOGUE INHIBITOR 4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID | ||||||
![]() | (TRYPTOPHAN SYNTHASE ...) x 2 | ||||||
![]() | LYASE / 8-FOLD ALPHA-BETA BARREL / ENZYME-INHIBITOR COMPLEX | ||||||
Function / homology | ![]() tryptophan synthase / tryptophan synthase activity / tryptophan biosynthetic process / identical protein binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Sachpatzidis, A. / Dealwis, C. / Lubetsky, J.B. / Liang, P.H. / Anderson, K.S. / Lolis, E. | ||||||
![]() | ![]() Title: Crystallographic studies of phosphonate-based alpha-reaction transition-state analogues complexed to tryptophan synthase. Authors: Sachpatzidis, A. / Dealwis, C. / Lubetsky, J.B. / Liang, P.H. / Anderson, K.S. / Lolis, E. #1: ![]() 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. #2: ![]() Title: Loop Closure and Intersubunit Communication in Tryptophan Synthase Authors: Schneider, T.R. / Gerhardt, E. / Lee, M. / Liang, P.H. / Anderson, K.S. / Schlichting, I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 137.9 KB | Display | ![]() |
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PDB format | ![]() | 106.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 771.1 KB | Display | ![]() |
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Full document | ![]() | 785 KB | Display | |
Data in XML | ![]() | 27.2 KB | Display | |
Data in CIF | ![]() | 38.3 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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Components
-TRYPTOPHAN SYNTHASE ... , 2 types, 2 molecules AB
#1: Protein | Mass: 28698.797 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source 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 Source: (gene. exp.) ![]() ![]() ![]() |
-Non-polymers , 4 types, 187 molecules ![](data/chem/img/HSP.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/PLP.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/PLP.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-HSP / |
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#4: Chemical | ChemComp-NA / |
#5: Chemical | ChemComp-PLP / |
#6: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.58 Å3/Da / Density % sol: 52.41 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7.8 Details: 12% PEG 4000, 0.75MM SPERMINE, 50MM SODIUM BICINE, 1MM EDTA, 5MM DTT, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 295K | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 0 K / Method: vapor diffusion | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 140 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Feb 2, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→45.7 Å / Num. all: 47428 / Num. obs: 47428 / % possible obs: 95.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.8 % / Biso Wilson estimate: 14.19 Å2 / Rmerge(I) obs: 0.054 / Net I/σ(I): 15.37 |
Reflection shell | Resolution: 2→2.1 Å / Redundancy: 2.4 % / Rmerge(I) obs: 0.159 / % possible all: 86.8 |
Reflection | *PLUS Num. measured all: 238914 |
Reflection shell | *PLUS % possible obs: 91.8 % / Rmerge(I) obs: 0.134 / Mean I/σ(I) obs: 5.9 |
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Processing
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Refinement | Resolution: 2→30 Å / σ(F): 2 / σ(I): 0 / Stereochemistry target values: ENGH & HUBER Details: RESTRAINED LEAST SQUARES REFINEMENT. CONJUGATE GRADIENT MINIMIZATION AND SIMULATED ANNEALING PROTOCOLS IMPLEMENTED IN XPLOR.
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Refinement step | Cycle: LAST / Resolution: 2→30 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 30 Å / σ(F): 2 / Rfactor Rfree: 0.25 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |