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- PDB-2es4: Crystal structure of the Burkholderia glumae lipase-specific fold... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2es4 | ||||||
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Title | Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase | ||||||
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![]() | HYDROLASE / protein-protein complex / steric chaperone / triacylglycerol hydrolase / all alpha helix protein / a/b hydrolase fold / extensive interaction area | ||||||
Function / homology | ![]() triacylglycerol lipase / triacylglycerol lipase activity / lipid catabolic process / unfolded protein binding / protein folding / membrane => GO:0016020 / extracellular region / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Pauwels, K. / Wyns, L. / Tommassen, J. / Savvides, S.N. / Van Gelder, P. | ||||||
![]() | ![]() Title: Structure of a membrane-based steric chaperone in complex with its lipase substrate. Authors: Pauwels, K. / Lustig, A. / Wyns, L. / Tommassen, J. / Savvides, S.N. / Van Gelder, P. #1: ![]() Title: Crystallization and crystal manipulation of a steric chaperone in complex with its lipase substrate Authors: Pauwels, K. / Loris, R. / Vandenbussche, G. / Ruysschaert, J.-M. / Wyns, L. / Van Gelder, P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 247.5 KB | Display | ![]() |
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PDB format | ![]() | 194.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 471.4 KB | Display | ![]() |
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Full document | ![]() | 490.4 KB | Display | |
Data in XML | ![]() | 50.9 KB | Display | |
Data in CIF | ![]() | 74.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1cvlS 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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2 | ![]()
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3 | ![]()
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Unit cell |
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Details | There are 2 biological units in the asymmetric unit (chains A & D and chains B & E) |
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Components
#1: Protein | Mass: 33117.703 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: Q05489, UniProt: P0DUB8*PLUS, triacylglycerol lipase #2: Protein | Mass: 35236.238 Da / Num. of mol.: 2 / Fragment: periplasmic C-terminal domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Chemical | #4: Chemical | ChemComp-IOD / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.9 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 20 % PEG3350, 0.2 M KI, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→40 Å / Num. all: 119154 / Num. obs: 120503 / % possible obs: 99 % / Redundancy: 7 % / Rmerge(I) obs: 0.072 / Χ2: 1.077 / Net I/σ(I): 15.4 |
Reflection shell | Resolution: 1.85→1.92 Å / % possible obs: 91.3 % / Rmerge(I) obs: 0.521 / Mean I/σ(I) obs: 3.85 / Num. measured obs: 10920 / Χ2: 1.034 / % possible all: 91.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1CVL Resolution: 1.85→40 Å
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Displacement parameters | Biso mean: 34.93 Å2 | ||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.85→40 Å
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