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Yorodumi- PDB-1lpb: THE 2.46 ANGSTROMS RESOLUTION STRUCTURE OF THE PANCREATIC LIPASE ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1lpb | ||||||
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Title | THE 2.46 ANGSTROMS RESOLUTION STRUCTURE OF THE PANCREATIC LIPASE COLIPASE COMPLEX INHIBITED BY A C11 ALKYL PHOSPHONATE | ||||||
Components |
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Keywords | HYDROLASE(CARBOXYLIC ESTERASE) | ||||||
Function / homology | Function and homology information positive regulation of triglyceride lipase activity / all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity / Digestion of dietary lipid / Retinoid metabolism and transport / Digestion of dietary lipid / lipase binding / lipase activity / intestinal cholesterol absorption / triacylglycerol lipase / triglyceride lipase activity ...positive regulation of triglyceride lipase activity / all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity / Digestion of dietary lipid / Retinoid metabolism and transport / Digestion of dietary lipid / lipase binding / lipase activity / intestinal cholesterol absorption / triacylglycerol lipase / triglyceride lipase activity / response to food / enzyme activator activity / lipid catabolic process / Retinoid metabolism and transport / digestion / response to bacterium / lipid metabolic process / extracellular space / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | Sus scrofa (pig) Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.46 Å | ||||||
Authors | Egloff, M.-P. / Van Tilbeurgh, H. / Cambillau, C. | ||||||
Citation | Journal: Biochemistry / Year: 1995 Title: The 2.46 A resolution structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate. Authors: Egloff, M.P. / Marguet, F. / Buono, G. / Verger, R. / Cambillau, C. / van Tilbeurgh, H. #1: Journal: Nature / Year: 1993 Title: Interfacial Activation of the Lipase-Procolipase Complex by Mixed Micelles Revealed by X-Ray Crystallography Authors: Van Tilbeurgh, H. / Egloff, M.-P. / Martinez, C. / Rugani, N. / Verger, R. / Cambillau, C. #2: Journal: Nature / Year: 1992 Title: Structure of the Pancreatic Lipase-Procolipase Complex Authors: Van Tilbeurgh, H. / Sarda, L. / Verger, R. / Cambillau, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lpb.cif.gz | 151.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lpb.ent.gz | 123 KB | Display | PDB format |
PDBx/mmJSON format | 1lpb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lp/1lpb ftp://data.pdbj.org/pub/pdb/validation_reports/lp/1lpb | 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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Atom site foot note | 1: CIS PROLINE - PRO B 16 / 2: CIS PROLINE - PRO B 211 / 3: CIS PROLINE - PRO B 298 |
-Components
-Protein , 2 types, 2 molecules AB
#1: Protein | Mass: 10319.651 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sus scrofa (pig) / Organ: PANCREAS / References: UniProt: P02703 |
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#2: Protein | Mass: 49573.562 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Organ: PANCREAS / References: UniProt: P16233, triacylglycerol lipase |
-Sugars , 1 types, 5 molecules
#3: Sugar | ChemComp-BOG / |
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-Non-polymers , 3 types, 287 molecules
#4: Chemical | ChemComp-CA / |
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#5: Chemical | ChemComp-MUP / |
#6: Water | ChemComp-HOH / |
-Details
Nonpolymer details | USE OF PARTIAL OCCUPANCY FOR THE INHIBITOR (REFINED OCCUPANCY) AND FOR BETA-OCTYLGLUCO |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.48 Å3/Da / Density % sol: 64.65 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.46 Å / Lowest resolution: 20 Å / Num. obs: 29845 / % possible obs: 92 % / Redundancy: 9.4 % / Num. measured all: 271893 / Rmerge(I) obs: 0.106 |
Reflection shell | *PLUS Highest resolution: 2.46 Å / Lowest resolution: 2.53 Å / % possible obs: 77.8 % / Redundancy: 3.9 % / Mean I/σ(I) obs: 84.9 |
-Processing
Software |
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Refinement | Resolution: 2.46→6 Å / Rfactor Rfree: 0.285 / Rfactor Rwork: 0.183 / Rfactor obs: 0.183 / σ(F): 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.46→6 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection obs: 27738 / Rfactor obs: 0.183 / Rfactor Rfree: 0.285 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 1.96 |