+
Open data
-
Basic information
Entry | Database: PDB / ID: 1j0h | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of Bacillus stearothermophilus neopullulanase | ||||||
![]() | neopullulanase | ||||||
![]() | HYDROLASE / beta-alpha-barrels | ||||||
Function / homology | ![]() neopullulanase / neopullulanase activity / D-glucose binding / carbohydrate metabolic process / calcium ion binding / protein homodimerization activity / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Hondoh, H. / Kuriki, T. / Matsuura, Y. | ||||||
![]() | ![]() Title: Three-dimensional Structure and Substrate Binding of Bacillus stearothermophilus Neopullulanase Authors: Hondoh, H. / Kuriki, T. / Matsuura, Y. #1: ![]() Title: Action of neopullulanase. neopullulanase catalyzes both hydrolysis and transglycosylation at alpha-(1,4)- and alpha-(1,6)-glucosidic linkages Authors: Takata, H. / Kuriki, T. / Okada, S. / Takesada, Y. / Iizuka, M. / Minamiura, N. / Imanaka, T. #2: ![]() Title: Pattern of action of Bacillus stearothermophilus neopullulanase on pullulan Authors: Imanaka, T. / Kuriki, T. #3: ![]() Title: New type of pullulanase from Bacillus stearothermophilus and molecular cloning and expression of the gene in Bacillus subtilis Authors: Kuriki, T. / Okada, S. / Imanaka, T. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 286.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 228.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 439.4 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 455.9 KB | Display | |
Data in XML | ![]() | 58.7 KB | Display | |
Data in CIF | ![]() | 90.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Details | The biological assembly is a dimer in the assymetric unit. |
-
Components
#1: Protein | Mass: 69142.844 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: pUC129 / Production host: ![]() ![]() #2: Chemical | ChemComp-CL / | #3: Chemical | #4: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 1.94 Å3/Da / Density % sol: 36.08 % | |||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: PEG 8000, sodium chloride, cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K | |||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ | |||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jul 2, 1999 |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→32 Å / Num. obs: 90768 / % possible obs: 94.2 % / Observed criterion σ(F): 2 |
Reflection shell | Resolution: 1.9→2.02 Å / % possible all: 71.9 |
Reflection | *PLUS Num. obs: 90890 / Num. measured all: 321350 / Rmerge(I) obs: 0.059 |
Reflection shell | *PLUS Lowest resolution: 2 Å / % possible obs: 71.1 % / Rmerge(I) obs: 0.187 |
-
Processing
Software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]()
| ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
| ||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||
Software | *PLUS Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 10 Å / % reflection Rfree: 5 % | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS |