[English] 日本語
![](img/lk-miru.gif)
- PDB-1cx9: CRYSTAL STRUCTURE OF THE COMPLEX OF BACTERIAL TRYPTOPHAN SYNTHASE... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1cx9 | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF THE COMPLEX OF BACTERIAL TRYPTOPHAN SYNTHASE WITH THE TRANSITION STATE ANALOGUE INHIBITOR 4-(2-AMINOPHENYLTHIO)-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 / cytosol / cytoplasm 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. / Anderson, K.S. / Schlichting, I. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 137.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 106.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
Unit cell |
|
-
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.) ![]() ![]() ![]() |
---|---|
#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, 160 molecules ![](data/chem/img/NHP.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-NHP / |
---|---|
#4: Chemical | ChemComp-NA / |
#5: Chemical | ChemComp-PLP / |
#6: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.53 Å3/Da / Density % sol: 51.47 % | |||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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 / Details: pH was adjusted with NaOH | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 140 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: May 28, 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: 2.3→44.2 Å / Num. all: 30288 / Num. obs: 30288 / % possible obs: 94 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2 % / Biso Wilson estimate: 12.8 Å2 / Rmerge(I) obs: 0.125 / Net I/σ(I): 10.5 |
Reflection shell | Resolution: 2.3→2.4 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.32 / % possible all: 80.8 |
Reflection | *PLUS Num. measured all: 110360 |
Reflection shell | *PLUS % possible obs: 80.8 % |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.3→30 Å / σ(F): 2 / Stereochemistry target values: ENGH & HUBER Details: RESTRAINED LEAST SQUARES REFINEMENT. CONJUGATE GRADIENT MINIMIZATION AND SIMULATED ANNEALING PROTOCOLS IMPLEMENTED IN XPLOR.
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→30 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |