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Open data
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Basic information
Entry | Database: PDB / ID: 6mrg | ||||||
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Title | FAAH bound to non covalent inhibitor | ||||||
![]() | Fatty-acid amide hydrolase 1 | ||||||
![]() | HYDROLASE/INHIBITOR / Complex / HYDROLASE-INHIBITOR complex | ||||||
Function / homology | ![]() Arachidonic acid metabolism / fatty acid amide hydrolase / fatty acid amide hydrolase activity / monoacylglycerol catabolic process / monoacylglycerol lipase activity / amidase activity / fatty acid catabolic process / Hydrolases; Acting on ester bonds; Carboxylic-ester hydrolases / hydrolase activity, acting on ester bonds / organelle membrane ...Arachidonic acid metabolism / fatty acid amide hydrolase / fatty acid amide hydrolase activity / monoacylglycerol catabolic process / monoacylglycerol lipase activity / amidase activity / fatty acid catabolic process / Hydrolases; Acting on ester bonds; Carboxylic-ester hydrolases / hydrolase activity, acting on ester bonds / organelle membrane / positive regulation of vasoconstriction / fatty acid metabolic process / phospholipid binding / Golgi membrane / lipid binding / endoplasmic reticulum membrane / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Saha, A. / Shih, A. / Mirzadegan, T. / Seierstad, M. | ||||||
![]() | ![]() Title: Predicting the Binding of Fatty Acid Amide Hydrolase Inhibitors by Free Energy Perturbation. Authors: Saha, A. / Shih, A.Y. / Mirzadegan, T. / Seierstad, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 829.9 KB | Display | ![]() |
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PDB format | ![]() | 694.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.3 MB | Display | ![]() |
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Full document | ![]() | 1.3 MB | Display | |
Data in XML | ![]() | 76.1 KB | Display | |
Data in CIF | ![]() | 101.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 63779.285 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-JXV / ( #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.22 Å3/Da / Density % sol: 61.82 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.4 / Details: PEG8000, PHOSPHATE, PH 7.4 |
-Data collection
Diffraction | Mean temperature: 273 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 R 1M / Detector: PIXEL / Date: Oct 22, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0094 Å / Relative weight: 1 |
Reflection | Resolution: 2.76→49.392 Å / Num. obs: 78055 / % possible obs: 92.2 % / Redundancy: 4.7 % / Biso Wilson estimate: 64.7 Å2 / Rmerge(I) obs: 0.086 / Net I/σ(I): 12.35 |
Reflection shell | Resolution: 2.76→2.91 Å / Redundancy: 4.4 % / Rmerge(I) obs: 0.623 / Mean I/σ(I) obs: 2.58 / Num. unique obs: 10777 / % possible all: 88.7 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.77→49.392 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | S33: -0 Å ° / Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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