[English] 日本語
![](img/lk-miru.gif)
- PDB-1gts: STRUCTURAL BASIS FOR TRANSFER RNA AMINOACEYLATION BY ESCHERICHIA ... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1gts | ||||||
---|---|---|---|---|---|---|---|
Title | STRUCTURAL BASIS FOR TRANSFER RNA AMINOACEYLATION BY ESCHERICHIA COLI GLUTAMINYL-TRNA SYNTHETASE | ||||||
![]() |
| ||||||
![]() | LIGASE/RNA / PROTEIN-RNA COMPLEX / LIGASE-RNA COMPLEX | ||||||
Function / homology | ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Perona, J.J. / Steitz, T.A. / Rould, M.A. | ||||||
![]() | ![]() Title: Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase. Authors: Perona, J.J. / Rould, M.A. / Steitz, T.A. #1: ![]() Title: Structural Basis of Anticodon Loop Recognition by Glutaminyl-tRNA Synthetase Authors: Rould, M.A. / Perona, J.J. / Steitz, T.A. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 159.8 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 126.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: RNA chain | Mass: 23754.121 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() ![]() |
---|---|
#2: Protein | Mass: 63434.641 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() ![]() |
#3: Chemical | ChemComp-AMP / ![]() |
#4: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.77 Å3/Da / Density % sol: 67.37 % | ||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow![]() | *PLUS Temperature: 17 ℃ / Method: vapor diffusion, hanging drop / Details: referred to J.Mol.Biol. 202.121 1988 / PH range low: 7.2 / PH range high: 6.8 | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
-
Processing
Software | Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Rfactor Rwork![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.8 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 6 Å / Rfactor obs: 0.199 / Rfactor Rwork![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 3.4 |