+Open data
-Basic information
Entry | Database: PDB / ID: 4do3 | ||||||
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Title | Structure of FAAH with a non-steroidal anti-inflammatory drug | ||||||
Components | Fatty-acid amide hydrolase 1 | ||||||
Keywords | HYDROLASE/HYDROLASE INHIBITOR / AMIDASE / HYDROLASE / ANANDAMIDE / NSAID / DRUG / COX / INHIBITOR / INFLAMMATION / PAIN / HYDROLASE-HYDROLASE INHIBITOR complex | ||||||
Function / homology | Function and homology information Arachidonic acid metabolism / fatty acid amide hydrolase / fatty acid amide hydrolase activity / monoacylglycerol catabolic process / acylglycerol 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 / acylglycerol 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 | Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.25 Å | ||||||
Authors | Garau, G. | ||||||
Citation | Journal: J.Am.Chem.Soc. / Year: 2013 Title: A Binding Site for Nonsteroidal Anti-inflammatory Drugs in Fatty Acid Amide Hydrolase. Authors: Bertolacci, L. / Romeo, E. / Veronesi, M. / Magotti, P. / Albani, C. / Dionisi, M. / Lambruschini, C. / Scarpelli, R. / Cavalli, A. / De Vivo, M. / Piomelli, D. / Garau, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4do3.cif.gz | 230.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4do3.ent.gz | 182.6 KB | Display | PDB format |
PDBx/mmJSON format | 4do3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/do/4do3 ftp://data.pdbj.org/pub/pdb/validation_reports/do/4do3 | HTTPS FTP |
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-Related structure data
Related structure data | 3lj7S S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
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-Components
#1: Protein | Mass: 62872.398 Da / Num. of mol.: 2 / Fragment: UNP residues 32-575 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Faah, Faah1 / Production host: Escherichia coli (E. coli) / References: UniProt: P97612, fatty acid amide hydrolase #2: Chemical | ChemComp-CL / | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.17 Å3/Da / Density % sol: 60.9 % |
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 30% PEG400, 100 MM TRIS-HCL, PH 7.5, 100 MM MGCL2, 100 MM NACL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 287K, temperature 290K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 1.008 / Wavelength: 1.008 Å |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Apr 23, 2011 |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.008 Å / Relative weight: 1 |
Reflection | Resolution: 2.25→44.5 Å / Num. all: 76448 / Num. obs: 76403 / % possible obs: 99.9 % / Observed criterion σ(F): 3 / Observed criterion σ(I): 3 / Redundancy: 11.6 % / Biso Wilson estimate: 32.5 Å2 / Rmerge(I) obs: 0.111 / Net I/σ(I): 15.9 |
Reflection shell | Resolution: 2.25→2.37 Å / Redundancy: 10.8 % / Rmerge(I) obs: 0.578 / Mean I/σ(I) obs: 4.1 / % possible all: 98.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 3LJ7 Resolution: 2.25→44.5 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.938 / SU B: 4.133 / SU ML: 0.103 / Cross valid method: THROUGHOUT / σ(F): 3 / ESU R: 0.187 / ESU R Free: 0.16 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 28.831 Å2
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Refinement step | Cycle: LAST / Resolution: 2.25→44.5 Å
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Refine LS restraints |
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Refine LS restraints NCS | Dom-ID: 1 / Auth asym-ID: A / Ens-ID: 1 / Number: 4216 / Refine-ID: X-RAY DIFFRACTION
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LS refinement shell | Resolution: 2.25→2.308 Å / Total num. of bins used: 20
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