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Open data
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Basic information
Entry | Database: PDB / ID: 1rp1 | ||||||
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Title | DOG PANCREATIC LIPASE RELATED PROTEIN 1 | ||||||
![]() | PANCREATIC LIPASE RELATED PROTEIN 1 | ||||||
![]() | HYDROLASE / LIPID DEGRADATION / PANCREATIC LIPASE | ||||||
Function / homology | ![]() Digestion of dietary lipid / carboxylic ester hydrolase activity / lipid catabolic process / calcium ion binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Roussel, A. / Cambillau, C. | ||||||
![]() | ![]() Title: Reactivation of the totally inactive pancreatic lipase RP1 by structure-predicted point mutations. Authors: Roussel, A. / de Caro, J. / Bezzine, S. / Gastinel, L. / de Caro, A. / Carriere, F. / Leydier, S. / Verger, R. / Cambillau, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 103.3 KB | Display | ![]() |
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PDB format | ![]() | 79.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 439.7 KB | Display | ![]() |
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Full document | ![]() | 446.4 KB | Display | |
Data in XML | ![]() | 21.7 KB | Display | |
Data in CIF | ![]() | 32.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1thgS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 49676.816 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Sugar | ChemComp-NAG / |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 53 % | ||||||||||||||||||||
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Crystal grow | pH: 4.2 Details: PROTEIN WAS CRYSTALLIZED FROM 20% PEG 8000 WITH 25MM POTASSIUM PHOSPHATE BUFFER AT PH 4.2. | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusionDetails: drop was diluted with an equal volume of the reservoir solution | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 1, 1997 / Details: MIRRORS |
Radiation | Monochromator: SPHERICAL GRATING MONOCHROMATOR / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→9 Å / Num. obs: 30017 / % possible obs: 97.8 % / Observed criterion σ(I): 1.5 / Redundancy: 3.4 % / Biso Wilson estimate: 33.17 Å2 / Rmerge(I) obs: 0.067 / Rsym value: 0.067 / Net I/σ(I): 11.2 |
Reflection shell | Resolution: 2.1→2.14 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.368 / Mean I/σ(I) obs: 3 / Rsym value: 0.368 / % possible all: 94.6 |
Reflection shell | *PLUS % possible obs: 94.6 % |
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Processing
Software |
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1THG Resolution: 2.1→9 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 1300 / Data cutoff low absF: 70 / σ(F): 2
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Displacement parameters | Biso mean: 31.01 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→9 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.1→2.17 Å / Rfactor Rfree error: 0.032 / Total num. of bins used: 10
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.183 |