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Yorodumi- PDB-5w7b: Rabbit acyloxyacyl hydrolase (AOAH), proteolytically processed, S... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5w7b | |||||||||
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Title | Rabbit acyloxyacyl hydrolase (AOAH), proteolytically processed, S262A mutant, with LPS | |||||||||
Components | (Acyloxyacyl hydrolase ...) x 2 | |||||||||
Keywords | HYDROLASE / lipopolysaccharide / LPS / GDSL esterase / saposin | |||||||||
Function / homology | Function and homology information lipopolysaccharide catabolic process / acyloxyacyl hydrolase / acyloxyacyl hydrolase activity / fatty acid metabolic process / cytoplasmic vesicle / calcium ion binding / extracellular region Similarity search - Function | |||||||||
Biological species | Oryctolagus cuniculus (rabbit) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | |||||||||
Authors | Gorelik, A. / Illes, K. / Nagar, B. | |||||||||
Funding support | Canada, 1items
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Citation | Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2018 Title: Crystal structure of the mammalian lipopolysaccharide detoxifier. Authors: Gorelik, A. / Illes, K. / Nagar, B. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5w7b.cif.gz | 429.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5w7b.ent.gz | 365.2 KB | Display | PDB format |
PDBx/mmJSON format | 5w7b.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/w7/5w7b ftp://data.pdbj.org/pub/pdb/validation_reports/w7/5w7b | HTTPS FTP |
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-Related structure data
Related structure data | 5w78C 5w7aC 5w7cC 5w7dC 5w7eC 5w7fC C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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Components on special symmetry positions |
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-Components
-Acyloxyacyl hydrolase ... , 2 types, 4 molecules ABCD
#1: Protein | Mass: 16384.969 Da / Num. of mol.: 2 / Fragment: residues 23-153 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Oryctolagus cuniculus (rabbit) / Gene: AOAH / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: O18823, acyloxyacyl hydrolase #2: Protein | Mass: 47621.781 Da / Num. of mol.: 2 / Fragment: residues 154-575 / Mutation: S262A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Oryctolagus cuniculus (rabbit) / Gene: AOAH / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: O18823, acyloxyacyl hydrolase |
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-Sugars , 4 types, 8 molecules
#3: Polysaccharide | Source method: isolated from a genetically manipulated source #4: Polysaccharide | Source method: isolated from a genetically manipulated source #5: Polysaccharide | Source method: isolated from a genetically manipulated source #6: Polysaccharide | Source method: isolated from a genetically manipulated source |
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-Non-polymers , 10 types, 500 molecules
#7: Chemical | ChemComp-PEG / #8: Chemical | ChemComp-PGE / #9: Chemical | ChemComp-FTT / #10: Chemical | ChemComp-MYR / #11: Chemical | ChemComp-CA / #12: Chemical | #13: Chemical | #14: Chemical | ChemComp-1PE / #15: Chemical | ChemComp-PO4 / #16: Water | ChemComp-HOH / | |
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-Details
Compound details | The authors state that the protein was treated with trypsin, and the exact cut site is unknown but ...The authors state that the protein was treated with trypsin, and the exact cut site is unknown but should be somewhere between K129 and R153. |
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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: 2.66 Å3/Da / Density % sol: 53.74 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: post-trypsin; 1 mM Triton X-100, 0.333 mM E. coli LPS Ra; 100 mM sodium MES pH 6; 34 % PEG 200; 5 % PEG 3000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 0.9801 Å |
Detector | Type: RAYONIX MX-300 / Detector: CCD / Date: Sep 17, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9801 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→50 Å / Num. obs: 106913 / % possible obs: 100 % / Redundancy: 14.6 % / Net I/σ(I): 19.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.9→44.765 Å / SU ML: 0.18 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 26.52
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→44.765 Å
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Refine LS restraints |
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LS refinement shell |
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