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- PDB-1wat: THE THREE-DIMENSIONAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF A... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1wat | ||||||
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Title | THE THREE-DIMENSIONAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF A WILD-TYPE BACTERIAL CHEMOTAXIS RECEPTOR | ||||||
![]() | ASPARTATE RECEPTOR | ||||||
![]() | CHEMOTAXIS | ||||||
Function / homology | ![]() transmembrane signaling receptor activity / chemotaxis / signal transduction / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Kim, S.-H. | ||||||
![]() | ![]() 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. #1: ![]() 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.I. / Jancarik, 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 | ![]() | 58.1 KB | Display | ![]() |
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PDB format | ![]() | 41.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 391.3 KB | Display | ![]() |
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Full document | ![]() | 430.7 KB | Display | |
Data in XML | ![]() | 12.2 KB | Display | |
Data in CIF | ![]() | 16.5 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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Unit cell |
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Atom site foot note | 1: THR A 111 - PRO A 112 OMEGA = 111.59 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: LEU A 113 - PRO A 114 OMEGA = 211.53 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: THR B 179 - PHE B 180 OMEGA = 84.24 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 4: THE LOOP REGIONS, RESIDUES A 76 - A 84 AND B 76 - B 84, ARE DISORDERED. | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.8583, 0.439267, 0.2652), Vector: Details | THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL GENERATE APPROXIMATE COORDINATES FOR CHAIN *A* WHEN APPLIED TO CHAIN *B*. THIS CORRESPONDS TO A ROTATION OF 178.2 DEGREES, WHICH IS AN APPROXIMATE (MOLECULAR) TWO-FOLD. | |
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Components
#1: Protein | Mass: 16366.229 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #2: Chemical | ChemComp-ASP / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.34 Å3/Da / Density % sol: 71.68 % | ||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, sitting drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 3 Å / Num. obs: 7114 / % possible obs: 62 % / Num. measured all: 15061 / Rmerge(I) obs: 0.071 |
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Processing
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Refinement | Highest resolution: 3 Å / σ(F): 1.5 Details: THE LOOP REGIONS, RESIDUES A 76 - A 84 AND B 76 - B 84, ARE DISORDERED.
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Refinement step | Cycle: LAST / Highest resolution: 3 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.192 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 32.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 3.696 |