[English] 日本語
![](img/lk-miru.gif)
- PDB-1krs: SOLUTION STRUCTURE OF THE ANTICODON BINDING DOMAIN OF ESCHERICHIA... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1krs | ||||||
---|---|---|---|---|---|---|---|
Title | SOLUTION STRUCTURE OF THE ANTICODON BINDING DOMAIN OF ESCHERICHIA COLI LYSYL-TRNA SYNTHETASE AND STUDIES OF ITS INTERACTIONS WITH TRNA-LYS | ||||||
![]() | LYSYL-TRNA SYNTHETASE (PRODUCT OF LYSS GENE) | ||||||
![]() | AMINOACYL-TRNA SYNTHETASE | ||||||
Function / homology | ![]() ATP:ADP adenylyltransferase activity / lysine-tRNA ligase / lysine-tRNA ligase activity / lysyl-tRNA aminoacylation / diadenosine tetraphosphate biosynthetic process / tRNA aminoacylation for protein translation / aminoacyl-tRNA synthetase multienzyme complex / positive regulation of macrophage activation / ligase activity / tRNA binding ...ATP:ADP adenylyltransferase activity / lysine-tRNA ligase / lysine-tRNA ligase activity / lysyl-tRNA aminoacylation / diadenosine tetraphosphate biosynthetic process / tRNA aminoacylation for protein translation / aminoacyl-tRNA synthetase multienzyme complex / positive regulation of macrophage activation / ligase activity / tRNA binding / magnesium ion binding / protein homodimerization activity / extracellular space / ATP binding / membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Commans, S. / Dardel, F. | ||||||
![]() | ![]() Title: Solution structure of the anticodon-binding domain of Escherichia coli lysyl-tRNA synthetase and studies of its interaction with tRNA(Lys). Authors: Commans, S. / Plateau, P. / Blanquet, S. / Dardel, F. #1: ![]() Title: Homology of Lyss and Lysu, the Two Escherichia Coli Genes Encoding Distinct Lysyl-tRNA Synthetase Species Authors: Leveque, F. / Plateau, P. / Dessen, P. / Blanquet, S. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 47.3 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 32.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 245.7 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 245.5 KB | Display | |
Data in XML | ![]() | 6.3 KB | Display | |
Data in CIF | ![]() | 7.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 13544.372 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
---|
-
Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
---|
-
Processing
Software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR software | Name: ![]() | ||||||||||||
NMR ensemble | Conformers submitted total number: 1 |