[English] 日本語
![](img/lk-miru.gif)
- PDB-5nuu: Torpedo californica acetylcholinesterase in complex with a chloro... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 5nuu | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Torpedo californica acetylcholinesterase in complex with a chlorotacrine-tryptophan hybrid inhibitor | |||||||||
![]() | Acetylcholinesterase | |||||||||
![]() | HYDROLASE / Alzheimer's disease / Tacrine / Acetylcholinesterase / Acetylcholiensterase inhibitor | |||||||||
Function / homology | ![]() acetylcholine catabolic process in synaptic cleft / acetylcholinesterase / acetylcholinesterase activity / choline metabolic process / side of membrane / synaptic cleft / synapse / extracellular space / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Caliandro, R. / Pesaresi, A. / Lamba, D. | |||||||||
![]() | ![]() Title: Novel tacrine-tryptophan hybrids: Multi-target directed ligands as potential treatment for Alzheimer's disease. Authors: Chalupova, K. / Korabecny, J. / Bartolini, M. / Monti, B. / Lamba, D. / Caliandro, R. / Pesaresi, A. / Brazzolotto, X. / Gastellier, A.J. / Nachon, F. / Pejchal, J. / Jarosova, M. / ...Authors: Chalupova, K. / Korabecny, J. / Bartolini, M. / Monti, B. / Lamba, D. / Caliandro, R. / Pesaresi, A. / Brazzolotto, X. / Gastellier, A.J. / Nachon, F. / Pejchal, J. / Jarosova, M. / Hepnarova, V. / Jun, D. / Hrabinova, M. / Dolezal, R. / Zdarova Karasova, J. / Mzik, M. / Kristofikova, Z. / Misik, J. / Muckova, L. / Jost, P. / Soukup, O. / Benkova, M. / Setnicka, V. / Habartova, L. / Chvojkova, M. / Kleteckova, L. / Vales, K. / Mezeiova, E. / Uliassi, E. / Valis, M. / Nepovimova, E. / Bolognesi, M.L. / Kuca, K. | |||||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 128.5 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 98.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 1.5 MB | Display | |
Data in XML | ![]() | 24 KB | Display | |
Data in CIF | ![]() | 34.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6i0bC ![]() 6i0cC ![]() 5e4tS S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 61325.090 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: P04058, acetylcholinesterase | ||||
---|---|---|---|---|---|
#2: Polysaccharide | alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source | ||||
#3: Polysaccharide | Source method: isolated from a genetically manipulated source #4: Chemical | ChemComp-9A5 / ( | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 4.05 Å3/Da / Density % sol: 69.65 % |
---|---|
Crystal grow | Temperature: 277.15 K / Method: vapor diffusion, hanging drop / Details: MES 100 mM, pH 6.2 PEG200 30% |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Jan 23, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→48.49 Å / Num. obs: 35012 / % possible obs: 100 % / Redundancy: 10 % / Rmerge(I) obs: 0.224 / Net I/σ(I): 7.6 |
Reflection shell | Resolution: 2.5→2.6 Å / Redundancy: 9.8 % / Rmerge(I) obs: 2.572 / % possible all: 100 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: 5E4T Resolution: 2.5→48.49 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.929 / SU B: 8.617 / SU ML: 0.18 / Cross valid method: THROUGHOUT / ESU R: 0.266 / ESU R Free: 0.232 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 51.32 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→48.49 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|