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Yorodumi- PDB-3fuj: Leukotriene A4 hydrolase in complex with 5-[2-(1H-pyrrol-1-yl)eth... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3fuj | ||||||
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Title | Leukotriene A4 hydrolase in complex with 5-[2-(1H-pyrrol-1-yl)ethoxy]-1H-indole | ||||||
Components | Leukotriene A-4 hydrolase | ||||||
Keywords | HYDROLASE / Leukotriene A4 Hydrolase / LTA4H / Fragment crystallography / Fragments of Life / FOL / Alternative splicing / Cytoplasm / Leukotriene biosynthesis / Metal-binding / Metalloprotease / Multifunctional enzyme / Polymorphism / Protease / Zinc | ||||||
Function / homology | Function and homology information 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 / zinc ion binding / extracellular exosome / extracellular region / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Davies, D.R. | ||||||
Citation | Journal: J.Med.Chem. / Year: 2009 Title: Discovery of leukotriene A4 hydrolase inhibitors using metabolomics biased fragment crystallography. Authors: Davies, D.R. / Mamat, B. / Magnusson, O.T. / Christensen, J. / Haraldsson, M.H. / Mishra, R. / Pease, B. / Hansen, E. / Singh, J. / Zembower, D. / Kim, H. / Kiselyov, A.S. / Burgin, A.B. / ...Authors: Davies, D.R. / Mamat, B. / Magnusson, O.T. / Christensen, J. / Haraldsson, M.H. / Mishra, R. / Pease, B. / Hansen, E. / Singh, J. / Zembower, D. / Kim, H. / Kiselyov, A.S. / Burgin, A.B. / Gurney, M.E. / Stewart, L.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3fuj.cif.gz | 144.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3fuj.ent.gz | 109.9 KB | Display | PDB format |
PDBx/mmJSON format | 3fuj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3fuj_validation.pdf.gz | 465.3 KB | Display | wwPDB validaton report |
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Full document | 3fuj_full_validation.pdf.gz | 468.7 KB | Display | |
Data in XML | 3fuj_validation.xml.gz | 26.3 KB | Display | |
Data in CIF | 3fuj_validation.cif.gz | 39.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fu/3fuj ftp://data.pdbj.org/pub/pdb/validation_reports/fu/3fuj | HTTPS FTP |
-Related structure data
Related structure data | 3ftsC 3ftuC 3ftvC 3ftwC 3ftxC 3ftyC 3fu0C 3fu3C 3fu5C 3fu6C 3fudC 3fueC 3fufC 3fuhC 3fuiC 3fukC 3fumC 3funC 3fh7S S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 69363.969 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: LTA4H, LTA4 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21-AI/pRARE / References: UniProt: P09960, leukotriene-A4 hydrolase |
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-Non-polymers , 6 types, 416 molecules
#2: Chemical | ChemComp-ZN / | ||
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#3: Chemical | ChemComp-YB / | ||
#4: Chemical | ChemComp-00G / | ||
#5: Chemical | ChemComp-ACT / | ||
#6: Chemical | #7: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 50.07 % |
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Crystal grow | Method: vapor diffusion, sitting drop / pH: 6.5 Details: 13% PEG 8000, 100 mM Imidazole pH 6.5, 100 mM Na Acetate, 5 mM YbCl3, crystal soaked overnight with 15 mM 5-[2-(1H-pyrrol-1-yl)ethoxy]-1H-indole, VAPOR DIFFUSION, SITTING DROP |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 0.97 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Dec 7, 2007 |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→50 Å / Num. obs: 53229 / % possible obs: 97.4 % / Redundancy: 7 % / Rmerge(I) obs: 0.084 / Net I/σ(I): 8.9 |
Reflection shell | Resolution: 1.9→1.97 Å / Redundancy: 4.9 % / Rmerge(I) obs: 0.344 / % possible all: 81.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 3FH7 Resolution: 1.9→50 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.941 / SU B: 2.552 / SU ML: 0.078 / Cross valid method: THROUGHOUT / ESU R: 0.138 / ESU R Free: 0.126 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 18.85 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→1.95 Å / Total num. of bins used: 20
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