[English] 日本語
![](img/lk-miru.gif)
- PDB-3sft: Crystal structure of Thermotoga maritima CheB methylesterase cata... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 3sft | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of Thermotoga maritima CheB methylesterase catalytic domain | ||||||
![]() | Chemotaxis response regulator protein-glutamate methylesterase | ||||||
![]() | HYDROLASE / modified doubly-wound/fold / Methylesterase / chemoreceptor | ||||||
Function / homology | ![]() protein-glutamate methylesterase / protein-glutamate methylesterase activity / protein-glutamine glutaminase activity / protein-glutamine glutaminase / phosphorelay response regulator activity / chemotaxis / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Park, S.Y. / Crane, B.R. | ||||||
![]() | ![]() Title: An insight into the interaction mode between CheB and chemoreceptor from two crystal structures of CheB methylesterase catalytic domain Authors: Cho, K.H. / Crane, B.R. / Park, S.Y. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 50.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 35.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 419.3 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 419.7 KB | Display | |
Data in XML | ![]() | 9.9 KB | Display | |
Data in CIF | ![]() | 13.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1chdS S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 20895.289 Da / Num. of mol.: 1 / Fragment: CheB methylesterase catalytic domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q9WYN9, protein-glutamate methylesterase |
---|---|
#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.27 Å3/Da / Density % sol: 62.33 % |
---|---|
Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 0.2M ammonium sulfate, 0.1M cacodylate, 30%(w/v) PEG 8K, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jan 23, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.15→30 Å / Num. obs: 13555 |
-
Processing
Software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: 1CHD Resolution: 2.15→30 Å
| ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.15→30 Å
|