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Yorodumi- PDB-1lpa: INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE COMPLEX BY MIXED... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1lpa | ||||||
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Title | INTERFACIAL ACTIVATION OF THE LIPASE-PROCOLIPASE COMPLEX BY MIXED MICELLES REVEALED BY X-RAY CRYSTALLOGRAPHY | ||||||
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 / triacylglycerol 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 / triacylglycerol lipase activity / response to food / lipid catabolic process / Retinoid metabolism and transport / enzyme activator activity / digestion / 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: 3.04 Å | ||||||
Authors | Van Tilbeurgh, H. / Egloff, M.-P. / Cambillau, C. | ||||||
Citation | 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. #1: Journal: To be Published Title: The 2.46 Angstroms 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. #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 | 1lpa.cif.gz | 111.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lpa.ent.gz | 88.5 KB | Display | PDB format |
PDBx/mmJSON format | 1lpa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1lpa_validation.pdf.gz | 493.4 KB | Display | wwPDB validaton report |
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Full document | 1lpa_full_validation.pdf.gz | 518.2 KB | Display | |
Data in XML | 1lpa_validation.xml.gz | 16.1 KB | Display | |
Data in CIF | 1lpa_validation.cif.gz | 23 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lp/1lpa ftp://data.pdbj.org/pub/pdb/validation_reports/lp/1lpa | HTTPS FTP |
-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: TRP B 30 - SER B 30A OMEGA = 141.29 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: SER B 30A - PRO B 31 OMEGA = 285.07 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 4: CIS PROLINE - PRO B 211 / 5: CIS PROLINE - PRO B 298 |
-Components
#1: Protein | Mass: 10345.731 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 |
#3: Sugar | ChemComp-BNG / |
#4: Chemical | ChemComp-CA / |
#5: Chemical | ChemComp-PLC / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.44 Å3/Da / Density % sol: 64.2 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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: 3 Å / Lowest resolution: 8 Å / Num. obs: 15496 / % possible obs: 90 % / Num. measured all: 97990 / Rmerge(I) obs: 0.2 |
-Processing
Software |
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Refinement | Resolution: 3.04→8 Å / Rfactor Rwork: 0.186 / Rfactor obs: 0.186 / σ(F): 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.04→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.186 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 3.6 |