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- PDB-7llq: Substrate-dependent divergence of leukotriene A4 hydrolase aminop... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7llq | ||||||
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Title | Substrate-dependent divergence of leukotriene A4 hydrolase aminopeptidase activity | ||||||
![]() | Leukotriene A-4 hydrolase | ||||||
![]() | HYDROLASE / Leukotriene A4 hydrolase / 4MDM / Aminipeptidase / Activator | ||||||
Function / homology | ![]() leukotriene-A4 hydrolase / leukotriene-A4 hydrolase activity / tripeptide aminopeptidase / tripeptide aminopeptidase activity / Biosynthesis of protectins / Biosynthesis of aspirin-triggered D-series resolvins / Biosynthesis of E-series 18(R)-resolvins / Biosynthesis of D-series resolvins / Biosynthesis of E-series 18(S)-resolvins / Synthesis of Leukotrienes (LT) and Eoxins (EX) ...leukotriene-A4 hydrolase / leukotriene-A4 hydrolase activity / tripeptide aminopeptidase / tripeptide aminopeptidase activity / Biosynthesis of protectins / Biosynthesis of aspirin-triggered D-series resolvins / Biosynthesis of E-series 18(R)-resolvins / Biosynthesis of D-series resolvins / Biosynthesis of E-series 18(S)-resolvins / Synthesis of Leukotrienes (LT) and Eoxins (EX) / protein metabolic process / epoxide hydrolase activity / leukotriene biosynthetic process / type I pneumocyte differentiation / peptide catabolic process / response to zinc ion / metalloaminopeptidase activity / aminopeptidase activity / lipid metabolic process / response to peptide hormone / tertiary granule lumen / peptidase activity / ficolin-1-rich granule lumen / Neutrophil degranulation / proteolysis / RNA binding / extracellular exosome / zinc ion binding / extracellular region / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Lee, K.H. / Lee, S.H. / Shim, Y.M. / Paige, M. / Noble, S.M. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Substrate-dependent modulation of the leukotriene A 4 hydrolase aminopeptidase activity and effect in a murine model of acute lung inflammation. Authors: Lee, K.H. / Ali, N.F. / Lee, S.H. / Zhang, Z. / Burdick, M. / Beaulac, Z.J. / Petruncio, G. / Li, L. / Xiang, J. / Chung, E.M. / Foreman, K.W. / Noble, S.M. / Shim, Y.M. / Paige, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 377.6 KB | Display | ![]() |
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PDB format | ![]() | 303.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 7kzeC ![]() 4ms6S S: Starting model for refinement C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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3 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 69363.969 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P09960, leukotriene-A4 hydrolase, tripeptide aminopeptidase #2: Chemical | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 46.56 % |
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Crystal grow | Temperature: 295.15 K / Method: vapor diffusion, sitting drop Details: 60-90 mM magnesium formate dihydrate, 20-25 % PEG3350 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() |
Detector | Type: Bruker Platinum 135 / Detector: CCD / Date: Dec 12, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.85→45.19 Å / Num. obs: 81035 / % possible obs: 96.8 % / Redundancy: 8.93 % / Biso Wilson estimate: 24.74 Å2 / Rmerge(I) obs: 0.2 / Net I/σ(I): 5.86 |
Reflection shell | Resolution: 2.85→2.91 Å / Rmerge(I) obs: 0.2716 / Num. unique obs: 40598 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4MS6 Resolution: 2.85→45.19 Å / SU ML: 0.3209 / Cross valid method: THROUGHOUT / σ(F): 1.96 / Phase error: 22.5914 / Stereochemistry target values: GeoStd + Monomer Library
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 20.6 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.85→45.19 Å
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Refine LS restraints |
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LS refinement shell |
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