+
Open data
-
Basic information
Entry | Database: PDB / ID: 1gz5 | ||||||
---|---|---|---|---|---|---|---|
Title | Trehalose-6-phosphate synthase. OtsA | ||||||
![]() | ALPHA-TREHALOSE-PHOSPHATE SYNTHASE | ||||||
![]() | SYNTHASE / TREHALOSE / GLYCOSYLTRANSFERASE / ROSSMANN-FOLD / GLUCOSE-6-PHOSPHATE / TREHALOSE-6-PHOSPHATE | ||||||
Function / homology | ![]() trehalose metabolism in response to cold stress / alpha,alpha-trehalose-phosphate synthase (UDP-forming) / alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity / alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) / trehalose-phosphatase activity / trehalose biosynthetic process / response to osmotic stress / cellular response to heat / DNA damage response / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gibson, R.P. / Turkenburg, J.P. / Davies, G.J. | ||||||
![]() | ![]() Title: Insights Into Trehalose Synthesis Provided by the Structure of the Retaining Glycosyltransferase Otsa Authors: Gibson, R.P. / Turkenburg, J.P. / Charnock, S.J. / Lloyd, R. / Davies, G.J. #1: Journal: Acta Crystallogr.,Sect.D / Year: 2002 Title: Characterization of Escherichia Coli Otsa, a Trehalose-6-Phosphate Synthase from Glycosyltransferase Family 20 Authors: Gibson, R.P. / Lloyd, R.M. / Charnock, S.J. / Davies, G.J. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 362.6 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 300.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 813 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 877.4 KB | Display | |
Data in XML | ![]() | 43.3 KB | Display | |
Data in CIF | ![]() | 63.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Unit cell |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS ensembles :
NCS oper:
|
-
Components
#1: Protein | Mass: 51871.273 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P31677, alpha,alpha-trehalose-phosphate synthase (UDP-forming) #2: Chemical | ChemComp-UDP / #3: Sugar | ChemComp-G6P / #4: Chemical | ChemComp-IMD / #5: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 53.3 % Description: THESE STATISTICS REFLECT SEPARATE TREATMENT OF FREIDEL MATES DURING SCALING PROCEDURE. TRUE MULTIPLICITY IS THUS APPROXIMATALY TWICE THE VALUE GIVEN | |||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | pH: 7.5 Details: 14% PEG4000, 0.15M NAAC, 0.1M IMIDAZOLE PH 7.5, 10MM MG-UDP, 10MM G6P | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: unknown | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Nov 15, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9392 Å / Relative weight: 1 |
Reflection | Resolution: 2.45→20 Å / Num. obs: 86205 / % possible obs: 99.9 % / Redundancy: 2.8 % / Rmerge(I) obs: 0.056 / Net I/σ(I): 17 |
Reflection shell | Resolution: 2.45→2.54 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.436 / Mean I/σ(I) obs: 2.4 / % possible all: 99.5 |
Reflection | *PLUS Lowest resolution: 20 Å |
Reflection shell | *PLUS % possible obs: 99.5 % / Rmerge(I) obs: 0.43 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES Details: TLS REFINEMENT USED THROUGHOUT. MOLECULE C SHOWS LARGE DISORDER IN ITS N-TERMINAL DOMAIN REFLECTED IN LARGE TLS VALUES AND POOR ELECTRON DENSITY. RESIDUES ALA 208 B AND ALA 208 D COULD NOT ...Details: TLS REFINEMENT USED THROUGHOUT. MOLECULE C SHOWS LARGE DISORDER IN ITS N-TERMINAL DOMAIN REFLECTED IN LARGE TLS VALUES AND POOR ELECTRON DENSITY. RESIDUES ALA 208 B AND ALA 208 D COULD NOT BE BUILT INTO THE ELECTRON DENSITY DUE TO LARGE DISORDER FOUND IN THESE LOOP REGIONS.
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 34.54 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.43→100 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|