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Yorodumi- PDB-8awh: Leukotriene A4 hydrolase in complex with 4-(4-Benzylphenyl)-selen... -
+Open data
-Basic information
Entry | Database: PDB / ID: 8awh | |||||||||
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Title | Leukotriene A4 hydrolase in complex with 4-(4-Benzylphenyl)-selenazol-2-amine | |||||||||
Components | Leukotriene A-4 hydrolase | |||||||||
Keywords | IMMUNE SYSTEM / Leukotriene B4 / complex / inhibitor / inflammation | |||||||||
Function / homology | Function and homology information leukotriene-A4 hydrolase / leukotriene-A4 hydrolase activity / tripeptide aminopeptidase activity / tripeptide aminopeptidase / 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 / protein metabolic process ...leukotriene-A4 hydrolase / leukotriene-A4 hydrolase activity / tripeptide aminopeptidase activity / tripeptide aminopeptidase / 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 / protein metabolic process / Synthesis of Leukotrienes (LT) and Eoxins (EX) / 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 | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.42 Å | |||||||||
Authors | Teder, T. / Haeggstrom, J.Z. | |||||||||
Funding support | Sweden, Estonia, 2items
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Citation | Journal: Int J Mol Sci / Year: 2023 Title: Modulation of the 5-Lipoxygenase Pathway by Chalcogen-Containing Inhibitors of Leukotriene A 4 Hydrolase. Authors: Teder, T. / Konig, S. / Singh, R. / Samuelsson, B. / Werz, O. / Garscha, U. / Haeggstrom, J.Z. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8awh.cif.gz | 158.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8awh.ent.gz | 118.8 KB | Display | PDB format |
PDBx/mmJSON format | 8awh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8awh_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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Full document | 8awh_full_validation.pdf.gz | 1.4 MB | Display | |
Data in XML | 8awh_validation.xml.gz | 28.8 KB | Display | |
Data in CIF | 8awh_validation.cif.gz | 45.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/aw/8awh ftp://data.pdbj.org/pub/pdb/validation_reports/aw/8awh | HTTPS FTP |
-Related structure data
Related structure data | 8avaC 4l2lS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-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: 70192.852 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) References: UniProt: P09960, leukotriene-A4 hydrolase, tripeptide aminopeptidase |
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-Non-polymers , 7 types, 592 molecules
#2: Chemical | ChemComp-ZN / | ||||||||||
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#3: Chemical | #4: Chemical | ChemComp-ACT / #5: Chemical | #6: Chemical | ChemComp-OD6 / | #7: Chemical | #8: Water | ChemComp-HOH / | |
-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.38 Å3/Da / Density % sol: 48.25 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.8 Details: 12% PEG 8000, 100 mM sodium acetate, 5 mM ytterbium chloride, 100 mM imidazole pH 6.8 PH range: 6.5-7.0 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: MAX IV / Beamline: BioMAX / Wavelength: 0.9763 Å |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Oct 2, 2021 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9763 Å / Relative weight: 1 |
Reflection | Resolution: 1.415→43.13 Å / Num. obs: 76734 / % possible obs: 95.6 % / Redundancy: 13.3 % / CC1/2: 0.996 / Rmerge(I) obs: 0.199 / Rpim(I) all: 0.056 / Rrim(I) all: 0.207 / Net I/σ(I): 11.3 |
Reflection shell | Resolution: 1.415→1.606 Å / Rmerge(I) obs: 1.917 / Mean I/σ(I) obs: 1.838 / Num. unique obs: 3837 / CC1/2: 0.996 / Rpim(I) all: 0.59 / Rrim(I) all: 2.007 |
-Phasing
Phasing | Method: molecular replacement | |||||||||
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Phasing MR |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4L2L Resolution: 1.42→43.13 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.956 / WRfactor Rfree: 0.172 / WRfactor Rwork: 0.1428 / FOM work R set: 0.8584 / SU B: 1.564 / SU ML: 0.055 / SU R Cruickshank DPI: 0.0897 / SU Rfree: 0.0891 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.09 / ESU R Free: 0.089 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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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 max: 67.43 Å2 / Biso mean: 17.891 Å2 / Biso min: 9.18 Å2
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Refinement step | Cycle: final / Resolution: 1.42→43.13 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.42→1.452 Å / Rfactor Rfree error: 0
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