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- PDB-3wth: Crystal Structure of Lymnaea stagnalis Acetylcholine-Binding Prot... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3wth | ||||||
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Title | Crystal Structure of Lymnaea stagnalis Acetylcholine-Binding Protein Q55R Mutant Complexed with Imidacloprid | ||||||
![]() | Acetylcholine-binding protein | ||||||
![]() | SIGNALING PROTEIN / neonicotinoids / nicotinic acetylcholine receptor / imidacloprid / acetylcholine binding | ||||||
Function / homology | ![]() acetylcholine receptor activity / acetylcholine-gated monoatomic cation-selective channel activity / synaptic cleft / response to nicotine / neuron projection / synapse / membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Okajima, T. / Ihara, M. / Yamashita, A. / Oda, T. / Matsuda, K. | ||||||
![]() | ![]() Title: Studies on an acetylcholine binding protein identify a basic residue in loop G on the beta 1 strand as a new structural determinant of neonicotinoid actions Authors: Ihara, M. / Okajima, T. / Yamashita, A. / Oda, T. / Asano, T. / Matsui, M. / Sattelle, D.B. / Matsuda, K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 220.8 KB | Display | ![]() |
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PDB format | ![]() | 185.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.7 MB | Display | ![]() |
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Full document | ![]() | 1.8 MB | Display | |
Data in XML | ![]() | 47.4 KB | Display | |
Data in CIF | ![]() | 64.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3wtiC ![]() 3wtjC ![]() 3wtkC ![]() 3wtlC ![]() 3wtmC ![]() 3wtnC ![]() 3wtoC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 24250.875 Da / Num. of mol.: 5 / Fragment: UNP residues 21-229 / Mutation: Q55R Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-IM4 / ( #3: Water | ChemComp-HOH / | Sequence details | AUTHORS STATE THAT BEFORE CRYSTALLIZATION, THE N-GLUCOSIDE GROUPS WERE REMOVED BY PEPTIDE-N- ...AUTHORS STATE THAT BEFORE CRYSTALLIZ | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.32 Å3/Da / Density % sol: 47.04 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion / pH: 5.7 Details: 0.2M Na citrate pH 5.7, 15-22% PEG3350, 0.5mM imidacloprid, VAPOR DIFFUSION, temperature 293K |
-Data collection
Diffraction | Mean temperature: 90 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: Bruker DIP-6040 / Detector: CCD / Date: Oct 8, 2007 |
Radiation | Monochromator: Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 2.52→18.1 Å / Num. all: 36029 / Num. obs: 36007 / % possible obs: 99.7 % / Observed criterion σ(I): 3 / Redundancy: 5.1 % / Biso Wilson estimate: 35.1 Å2 / Rsym value: 0.087 / Net I/σ(I): 12.6 |
Reflection shell | Resolution: 2.52→2.66 Å / Redundancy: 5.1 % / Rmerge(I) obs: 0.4 / Mean I/σ(I) obs: 4.7 / Num. unique all: 5273 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 48.9551 Å2 / ksol: 0.4 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 38.9 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.54→18.05 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.54→2.7 Å / Rfactor Rfree error: 0.022 / Total num. of bins used: 6
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Xplor file |
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