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Yorodumi- PDB-4uuq: Crystal structure of human mono-glyceride lipase in complex with ... -
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-Basic information
Entry | Database: PDB / ID: 4uuq | ||||||
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Title | Crystal structure of human mono-glyceride lipase in complex with SAR127303 | ||||||
Components | MONOGLYCERIDE LIPASE | ||||||
Keywords | HYDROLASE | ||||||
Function / homology | Function and homology information Arachidonate production from DAG / acylglycerol catabolic process / Acyl chain remodeling of DAG and TAG / acylglycerol lipase / monoacylglycerol catabolic process / triglyceride catabolic process / regulation of endocannabinoid signaling pathway / monoacylglycerol lipase activity / regulation of sensory perception of pain / lysophospholipase activity ...Arachidonate production from DAG / acylglycerol catabolic process / Acyl chain remodeling of DAG and TAG / acylglycerol lipase / monoacylglycerol catabolic process / triglyceride catabolic process / regulation of endocannabinoid signaling pathway / monoacylglycerol lipase activity / regulation of sensory perception of pain / lysophospholipase activity / Triglyceride catabolism / regulation of signal transduction / arachidonate metabolic process / lipid metabolic process / fatty acid biosynthetic process / regulation of inflammatory response / inflammatory response / endoplasmic reticulum membrane / protein homodimerization activity / membrane / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.36 Å | ||||||
Authors | Griebel, G. / Pichat, P. / Beeske, S. / Leroy, T. / Redon, N. / Francon, D. / Bert, L. / Even, L. / Lopez-Grancha, M. / Tolstykh, T. ...Griebel, G. / Pichat, P. / Beeske, S. / Leroy, T. / Redon, N. / Francon, D. / Bert, L. / Even, L. / Lopez-Grancha, M. / Tolstykh, T. / Sun, F. / Yu, Q. / Brittain, S. / Arlt, H. / He, T. / Zhang, B. / Wiederschain, D. / Bertrand, T. / Houtman, J. / Rak, A. / Vallee, F. / Michot, N. / Auge, F. / Menet, V. / Bergis, O.E. / George, P. / Avenet, P. / Mikol, V. / Didier, M. / Escoubet, J. | ||||||
Citation | Journal: Sci.Rep. / Year: 2015 Title: Selective Blockade of the Hydrolysis of the Endocannabinoid 2-Arachidonoylglycerol Impairs Learning and Memory Performance While Producing Antinociceptive Activity in Rodents. Authors: Griebel, G. / Pichat, P. / Beeske, S. / Leroy, T. / Redon, N. / Jacquet, A. / Francon, D. / Bert, L. / Even, L. / Lopez-Grancha, M. / Tolstykh, T. / Sun, F. / Yu, Q. / Brittain, S. / Arlt, H. ...Authors: Griebel, G. / Pichat, P. / Beeske, S. / Leroy, T. / Redon, N. / Jacquet, A. / Francon, D. / Bert, L. / Even, L. / Lopez-Grancha, M. / Tolstykh, T. / Sun, F. / Yu, Q. / Brittain, S. / Arlt, H. / He, T. / Zhang, B. / Wiederschain, D. / Bertrand, T. / Houtmann, J. / Rak, A. / Vallee, F. / Michot, N. / Auge, F. / Menet, V. / Bergis, O.E. / George, P. / Avenet, P. / Mikol, V. / Didier, M. / Escoubet, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4uuq.cif.gz | 127 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4uuq.ent.gz | 98.9 KB | Display | PDB format |
PDBx/mmJSON format | 4uuq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4uuq_validation.pdf.gz | 956.9 KB | Display | wwPDB validaton report |
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Full document | 4uuq_full_validation.pdf.gz | 977 KB | Display | |
Data in XML | 4uuq_validation.xml.gz | 26.8 KB | Display | |
Data in CIF | 4uuq_validation.cif.gz | 37.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uu/4uuq ftp://data.pdbj.org/pub/pdb/validation_reports/uu/4uuq | HTTPS FTP |
-Related structure data
Related structure data | 3jw8S 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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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 35292.512 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PET28 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q99685, acylglycerol lipase #2: Chemical | #3: 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: 3.02 Å3/Da / Density % sol: 59 % / Description: NONE |
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Crystal grow | Temperature: 277 K / pH: 6 / Details: MES BUFFER 50MM PH6.0, MPD 40%(V/V) AT 4C |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.9814 |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Oct 20, 2008 / Details: TOROIDAL MIRROR |
Radiation | Monochromator: DIAMOND (111), GE(220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9814 Å / Relative weight: 1 |
Reflection | Resolution: 2.36→73.32 Å / Num. obs: 20609 / % possible obs: 95.2 % / Observed criterion σ(I): 3 / Redundancy: 4.6 % / Biso Wilson estimate: 52.356 Å2 / Rmerge(I) obs: 0.01 / Net I/σ(I): 17.7 |
Reflection shell | Resolution: 2.36→2.5 Å / Redundancy: 4.7 % / Rmerge(I) obs: 0.45 / Mean I/σ(I) obs: 2.6 / % possible all: 97.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 3JW8 Resolution: 2.36→73.32 Å / Cross valid method: THROUGHOUT / σ(F): 0 Details: COVALENT BONDING BETWEEN CLEAVED LIGAND AND SERINE 132
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Displacement parameters | Biso mean: 46.06 Å2
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Refinement step | Cycle: LAST / Resolution: 2.36→73.32 Å
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LS refinement shell | Resolution: 2.36→2.5 Å / Total num. of bins used: 9
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