+Open data
-Basic information
Entry | Database: PDB / ID: 3hju | ||||||
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Title | Crystal structure of human monoglyceride lipase | ||||||
Components | Monoglyceride lipase | ||||||
Keywords | HYDROLASE / alpha/beta hydrolase / Serine esterase | ||||||
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 / acylglycerol lipase activity / arachidonic acid metabolic process / regulation of sensory perception of pain ...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 / acylglycerol lipase activity / arachidonic acid metabolic process / regulation of sensory perception of pain / lysophospholipase activity / Triglyceride catabolism / regulation of signal transduction / 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: 2.2 Å | ||||||
Authors | Labar, G. / Bauvois, C. / Borel, F. / Ferrer, J.-L. / Wouters, J. / Lambert, D.M. | ||||||
Citation | Journal: Chembiochem / Year: 2010 Title: Crystal Structure of the Human Monoacylglycerol Lipase, a Key Actor in Endocannabinoid Signaling Authors: Labar, G. / Bauvois, C. / Borel, F. / Ferrer, J.-L. / Wouters, J. / Lambert, D.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3hju.cif.gz | 127.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3hju.ent.gz | 99.4 KB | Display | PDB format |
PDBx/mmJSON format | 3hju.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hj/3hju ftp://data.pdbj.org/pub/pdb/validation_reports/hj/3hju | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 37698.066 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MGLL / Plasmid: pASK43 / Production host: Escherichia coli (E. coli) / Strain (production host): ROSETTA / 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: 2.48 Å3/Da / Density % sol: 50.48 % |
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Crystal grow | Temperature: 277 K / Method: under oil Details: 35% v/v MPD, 70mM Sodium Cacodylate, pH 4-6, under oil, temperature 277K PH range: 4-6 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.97618 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Mar 12, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97618 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→43.02 Å / Num. obs: 37674 / % possible obs: 97.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.5 % / Rsym value: 0.119 / Num. measured all: 162505 |
Reflection shell | Resolution: 2.2→2.3 Å / % possible obs: 86 % / Redundancy: 4.5 % / Mean I/σ(I) obs: 3.86 / Num. measured obs: 4066 / Rsym value: 0.4 / % possible all: 86.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: a partial/incomplete model of PDB entries obtained by other methods Resolution: 2.2→43.02 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.928 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.228 / ESU R Free: 0.187 / 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: 31.203 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→43.02 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.257 Å / Total num. of bins used: 20
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