[English] 日本語
![](img/lk-miru.gif)
- PDB-2jg0: Family 37 trehalase from Escherichia coli in complex with 1- thia... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2jg0 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Family 37 trehalase from Escherichia coli in complex with 1- thiatrehazolin | |||||||||
![]() | PERIPLASMIC TREHALASE | |||||||||
![]() | HYDROLASE / FAMILY 37 / INHIBITOR / TREHALASE / GLYCOSIDE HYDROLASE / PERIPLASMIC / GLYCOSIDASE / 1-THIATREHAZOLIN | |||||||||
Function / homology | ![]() alpha,alpha-trehalase / trehalose catabolic process / alpha,alpha-trehalase activity / cellular hyperosmotic response / outer membrane-bounded periplasmic space / DNA damage response Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Gibson, R.P. / Gloster, T.M. / Roberts, S. / Warren, R.A.J. / Storch De Gracia, I. / Garcia, A. / Chiara, J.L. / Davies, G.J. | |||||||||
![]() | ![]() Title: Molecular Basis for Trehalase Inhibition Revealed by the Structure of Trehalase in Complex with Potent Inhibitors. Authors: Gibson, R.P. / Gloster, T.M. / Roberts, S. / Warren, R.A.J. / Storch De Gracia, I. / Garcia, A. / Chiara, J.L. / Davies, G.J. | |||||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 247.6 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 195.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 796.2 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 805 KB | Display | |
Data in XML | ![]() | 27.1 KB | Display | |
Data in CIF | ![]() | 43.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2jf4SC S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 60526.531 Da / Num. of mol.: 1 / Fragment: RESIDUES 31-565 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
---|---|
#2: Sugar | ChemComp-TTZ / |
#3: Water | ChemComp-HOH / |
Sequence details | THE FIRST 30 RESIDUES CORRESPOND TO A SIGNAL PEPTIDE THAT IS PREDICTED TO HAVE CLEAVED DURING ...THE FIRST 30 RESIDUES CORRESPOND |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 43 % |
---|---|
Crystal grow | pH: 6.5 Details: 15 MG/ML PROTEIN, 25% PEG3350 AND 0.1 M BIS-TRIS HCL, PH 6.5. |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Details: TOROIDAL MIRROR |
Radiation | Monochromator: SI(311) AND SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97377 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→30 Å / Num. obs: 83167 / % possible obs: 100 % / Redundancy: 5.3 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 12.6 |
Reflection shell | Resolution: 1.5→1.58 Å / Redundancy: 5.3 % / Rmerge(I) obs: 0.35 / Mean I/σ(I) obs: 4 / % possible all: 100 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PBD ENTRY 2JF4 Resolution: 1.5→28.36 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.942 / SU B: 2.372 / SU ML: 0.042 / Cross valid method: THROUGHOUT / ESU R: 0.086 / ESU R Free: 0.072 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. NO ELECTRON DENSITY CAN BE OBSERVED FOR THE CHAIN BETWEEN 102 AND 107. THERE IS DISORDERED DENSITY IN THE REGION OF 478,546,547 WHICH HAS ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. NO ELECTRON DENSITY CAN BE OBSERVED FOR THE CHAIN BETWEEN 102 AND 107. THERE IS DISORDERED DENSITY IN THE REGION OF 478,546,547 WHICH HAS BEEN MODELLED AS BEST AS POSSIBLE.
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 8.5 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.5→28.36 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|