[English] 日本語
![](img/lk-miru.gif)
- PDB-7ehr: Levansucrase from Brenneria sp. EniD 312 at 1.33 angstroms resolution -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 7ehr | ||||||
---|---|---|---|---|---|---|---|
Title | Levansucrase from Brenneria sp. EniD 312 at 1.33 angstroms resolution | ||||||
![]() | Levansucrase | ||||||
![]() | TRANSFERASE / Levansucrase / fructosyltransferase / levan synthesis | ||||||
Function / homology | ![]() levansucrase / levansucrase activity / carbohydrate utilization / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Xu, W. / Ni, D.W. / Hou, X.D. / Rao, Y.J. / Pijning, T. / Guskov, A. / Mu, W.M. | ||||||
Funding support | ![]()
| ||||||
![]() | ![]() Title: Crystal Structure of Levansucrase from the Gram-Negative Bacterium Brenneria Provides Insights into Its Product Size Specificity. Authors: Xu, W. / Ni, D. / Hou, X. / Pijning, T. / Guskov, A. / Rao, Y. / Mu, W. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 214.3 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 168.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 838 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 842 KB | Display | |
Data in XML | ![]() | 23.2 KB | Display | |
Data in CIF | ![]() | 35.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7ehsC ![]() 7ehtC ![]() 7fdzC ![]() 4d47S S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data | Similarity search - Function & homology ![]() |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||||
Unit cell |
| ||||||||||||
Components on special symmetry positions |
|
-
Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 49397.855 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|
-Non-polymers , 7 types, 508 molecules ![](data/chem/img/PGE.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/1PE.gif)
![](data/chem/img/PE4.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/1PE.gif)
![](data/chem/img/PE4.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-PGE / #3: Chemical | #4: Chemical | ChemComp-1PE / | #5: Chemical | ChemComp-PE4 / | #6: Chemical | ChemComp-GOL / #7: Chemical | ChemComp-PO4 / #8: Water | ChemComp-HOH / | |
---|
-Details
Has ligand of interest | N |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.14 Å3/Da / Density % sol: 60.86 % |
---|---|
Crystal grow | Temperature: 298.15 K / Method: vapor diffusion, hanging drop / pH: 7.5 / Details: Ammonium sulfate, PEG 400 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Dec 10, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97853 Å / Relative weight: 1 |
Reflection | Resolution: 1.33→84.87 Å / Num. obs: 138038 / % possible obs: 90.3 % / Redundancy: 36.8 % / CC1/2: 0.999 / Rpim(I) all: 0.019 / Net I/σ(I): 20.1 |
Reflection shell | Resolution: 1.33→1.4 Å / Redundancy: 16.1 % / Num. unique obs: 6204 / CC1/2: 0.706 / Rpim(I) all: 0.012 / % possible all: 34.5 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: 4D47 Resolution: 1.33→84.8 Å / Cross valid method: THROUGHOUT
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 99.48 Å2 / Biso min: 8.09 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.33→84.8 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 1.332→1.367 Å /
|