[English] 日本語
![](img/lk-miru.gif)
- PDB-2lig: THREE-DIMENSIONAL STRUCTURES OF THE LIGAND-BINDING DOMAIN OF THE ... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2lig | ||||||
---|---|---|---|---|---|---|---|
Title | THREE-DIMENSIONAL STRUCTURES OF THE LIGAND-BINDING DOMAIN OF THE BACTERIAL ASPARTATE RECEPTOR WITH AND WITHOUT A LIGAND | ||||||
![]() | ASPARTATE RECEPTOR | ||||||
![]() | CHEMOTAXIS | ||||||
Function / homology | ![]() transmembrane signaling receptor activity / chemotaxis / signal transduction / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Kim, S.-H. / Yeh, J.I. / Prive, G.G. / Milburn, M. / Scott, W. / Koshland Junior, D.E. | ||||||
![]() | ![]() Title: Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand. Authors: Milburn, M.V. / Prive, G.G. / Milligan, D.L. / Scott, W.G. / Yeh, J. / Jancarik, J. / Koshland Jr., D.E. / Kim, S.H. #1: ![]() Title: The Three-Dimensional Structure of the Ligand-Binding Domain of a Wild-Type Bacterial Chemotaxis Receptor. Structural Comparison to the Cross-Linked Mutant Forms and Conformational Changes Upon Ligand Binding Authors: Yeh, J.I. / Biemann, H.-P. / Pandit, J. / Koshland, D.E. / Kim, S.-H. #2: ![]() Title: Refined Structures of the Ligand-Binding Domain of the Aspartate Receptor from Salmonella Typhimurium Authors: Scott, W.G. / Milligan, D.L. / Milburn, M.V. / Prive, G.G. / Yeh, J. / Koshland Junior, D.E. / Kim, S.-H. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 69.8 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 55.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 415.4 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 434.6 KB | Display | |
Data in XML | ![]() | 10.7 KB | Display | |
Data in CIF | ![]() | 15.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Atom site foot note | 1: PHE B 180 - ASP B 181 OMEGA = 100.60 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
-
Components
#1: Protein | Mass: 18371.432 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Chemical | ChemComp-ASP / | #4: Chemical | ChemComp-PHN / | #5: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.32 Å3/Da / Density % sol: 46.94 % | ||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS Temperature: 21 ℃ / pH: 7.4 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Rfactor Rwork: 0.176 / Rfactor obs: 0.176 / Highest resolution: 2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|