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- PDB-1lih: THREE-DIMENSIONAL STRUCTURES OF THE LIGAND-BINDING DOMAIN OF THE ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1lih | ||||||
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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. / Scott, W. / Yeh, J.I. / Prive, G.G. / Milburn, M. | ||||||
![]() | ![]() 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 |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 45.5 KB | Display | ![]() |
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PDB format | ![]() | 31.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 384.8 KB | Display | ![]() |
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Full document | ![]() | 404.7 KB | Display | |
Data in XML | ![]() | 7.8 KB | Display | |
Data in CIF | ![]() | 10.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Atom site foot note | 1: THR 87 - ASP 88 OMEGA = 236.79 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION | ||||||||
Details | THE FOLLOWING CRYSTALLOGRAPHIC TWO-FOLD OPERATION CAN BE APPLIED TO THE COORDINATES IN THIS ENTRY TO OBTAIN A DIMER. SYMTR1 1 0.000000 0.000000 -1.000000 1.00000 SYMTR2 1 0.000000 -1.000000 0.000000 1.00000 SYMTR3 1 0.166700 0.000000 -1.000000 2.00000 |
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Components
#1: Protein | Mass: 18371.432 Da / Num. of mol.: 1 / Mutation: INS(MET 25), N36C Source method: isolated from a genetically manipulated source Details: CYS 36 CROSSLINKED PERIPLASMIC DOMAIN / Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-PHN / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.91 Å3/Da / Density % sol: 68.58 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 21 ℃ / pH: 7.4 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
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Processing
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Refinement | Rfactor Rwork: 0.188 / Rfactor obs: 0.188 / Highest resolution: 2.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.2 Å
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Refine LS restraints |
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