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Yorodumi- PDB-8s1z: Crystal structure of glycosylated human primary amine oxidase AOC3 -
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Open data
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Basic information
| Entry | Database: PDB / ID: 8s1z | ||||||
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| Title | Crystal structure of glycosylated human primary amine oxidase AOC3 | ||||||
Components | Membrane primary amine oxidase | ||||||
Keywords | OXIDOREDUCTASE / copper amine oxidase / TPQ / adhesion protein / human vascular adhesion protein-1 / membrane primary amine oxidase | ||||||
| Function / homology | Function and homology informationprimary-amine oxidase / primary methylamine oxidase activity / amine metabolic process / Phase I - Functionalization of compounds / microvillus / quinone binding / early endosome / cell adhesion / inflammatory response / protein heterodimerization activity ...primary-amine oxidase / primary methylamine oxidase activity / amine metabolic process / Phase I - Functionalization of compounds / microvillus / quinone binding / early endosome / cell adhesion / inflammatory response / protein heterodimerization activity / copper ion binding / calcium ion binding / cell surface / endoplasmic reticulum / Golgi apparatus / identical protein binding / membrane / plasma membrane / cytoplasm Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.8 Å | ||||||
Authors | Guedez, G. / Alix, M. / Salminen, T.A. | ||||||
| Funding support | Finland, 1items
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Citation | Journal: To Be PublishedTitle: Structural flexibility of domains in human AOC3 Authors: Guedez, G. / Alix, M. / Salminen, T.A. | ||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8s1z.cif.gz | 724.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8s1z.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 8s1z.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8s1z_validation.pdf.gz | 5.2 MB | Display | wwPDB validaton report |
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| Full document | 8s1z_full_validation.pdf.gz | 5.2 MB | Display | |
| Data in XML | 8s1z_validation.xml.gz | 110.6 KB | Display | |
| Data in CIF | 8s1z_validation.cif.gz | 142.7 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/s1/8s1z ftp://data.pdbj.org/pub/pdb/validation_reports/s1/8s1z | HTTPS FTP |
-Related structure data
| Similar structure data | Similarity search - Function & homology F&H Search |
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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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| Unit cell |
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Components
-Protein , 1 types, 4 molecules ABCD
| #1: Protein | Mass: 81896.852 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: AOC3, VAP1 / Production host: ![]() |
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-Sugars , 13 types, 24 molecules 
| #2: Polysaccharide | alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source | ||||||||||||||||||||||
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| #3: Polysaccharide | alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source #4: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #5: Polysaccharide | Type: oligosaccharide / Mass: 894.823 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source #6: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #7: Polysaccharide | alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Type: oligosaccharide / Mass: 748.682 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source #8: Polysaccharide | Source method: isolated from a genetically manipulated source #9: Polysaccharide | alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Type: oligosaccharide / Mass: 1072.964 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source #10: Polysaccharide | Source method: isolated from a genetically manipulated source #11: Polysaccharide | alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1- ...alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #12: Polysaccharide | alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #13: Polysaccharide | alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D- ...alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Type: oligosaccharide / Mass: 1072.964 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source #16: Sugar | ChemComp-NAG / |
-Non-polymers , 2 types, 12 molecules 


| #14: Chemical | ChemComp-CA / #15: Chemical | ChemComp-CU / |
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-Details
| Has ligand of interest | N |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 2.75 Å3/Da / Density % sol: 55.33 % |
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| Crystal grow | Temperature: 294 K / Method: vapor diffusion, sitting drop Details: 0.2 M Sodium Chloride, 0.1 M Sodium Acetate pH 5.0, 20% PEG 6000 |
-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: 0.918401 Å |
| Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Apr 18, 2019 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.918401 Å / Relative weight: 1 |
| Reflection | Resolution: 3.8→29.88 Å / Num. obs: 54606 / % possible obs: 87.44 % / Redundancy: 4 % / Biso Wilson estimate: 116.3 Å2 / CC1/2: 0.879 / Net I/σ(I): 1.68 |
| Reflection shell | Resolution: 3.8→3.9 Å / Num. unique obs: 3455 / CC1/2: 0.12 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.8→29.88 Å / SU ML: 0.8305 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 40.0551 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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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: 128.14 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3.8→29.88 Å
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| Refine LS restraints |
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| LS refinement shell |
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About Yorodumi



Homo sapiens (human)
X-RAY DIFFRACTION
Finland, 1items
Citation
PDBj




