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Yorodumi- PDB-6grr: Crystal structure of Escherichia coli amine oxidase mutant I342F/E573Q -
+Open data
-Basic information
Entry | Database: PDB / ID: 6grr | ||||||
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Title | Crystal structure of Escherichia coli amine oxidase mutant I342F/E573Q | ||||||
Components | (Amine oxidase) x 2 | ||||||
Keywords | OXIDOREDUCTASE | ||||||
Function / homology | Function and homology information Oxidoreductases; Acting on the CH-NH2 group of donors; With oxygen as acceptor / aliphatic amine oxidase activity / phenylethylamine catabolic process / primary amine oxidase activity / : / : / : / primary-amine oxidase / L-phenylalanine catabolic process / amine metabolic process ...Oxidoreductases; Acting on the CH-NH2 group of donors; With oxygen as acceptor / aliphatic amine oxidase activity / phenylethylamine catabolic process / primary amine oxidase activity / : / : / : / primary-amine oxidase / L-phenylalanine catabolic process / amine metabolic process / quinone binding / periplasmic space / copper ion binding / calcium ion binding Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 1.7 Å | ||||||
Authors | Gaule, T.G. / Smith, M.A. / Tych, K.M. / Pirrat, P. / Trinh, C.H. / Pearson, A.R. / Knowles, P.F. / McPherson, M.J. | ||||||
Funding support | United Kingdom, 1items
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Citation | Journal: Biochemistry / Year: 2018 Title: Oxygen Activation Switch in the Copper Amine Oxidase of Escherichia coli. Authors: Gaule, T.G. / Smith, M.A. / Tych, K.M. / Pirrat, P. / Trinh, C.H. / Pearson, A.R. / Knowles, P.F. / McPherson, M.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6grr.cif.gz | 327.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6grr.ent.gz | 256.8 KB | Display | PDB format |
PDBx/mmJSON format | 6grr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gr/6grr ftp://data.pdbj.org/pub/pdb/validation_reports/gr/6grr | HTTPS FTP |
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-Related structure data
Related structure data | 6ezzC 1dyuS 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 , 2 types, 2 molecules AB
#1: Protein | Mass: 80405.719 Da / Num. of mol.: 1 / Mutation: I342F, E573Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: RK56_010715 / Plasmid: pKK233-2 / Production host: Escherichia coli (E. coli) / Variant (production host): XL-1 References: UniProt: A0A2K0PX72, UniProt: P46883*PLUS, Oxidoreductases; Acting on the CH-NH2 group of donors; With oxygen as acceptor |
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#2: Protein | Mass: 80673.055 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: RK56_010715 / Plasmid: pKK233-2 / Production host: Escherichia coli (E. coli) / Variant (production host): XL-1 blue References: UniProt: A0A2K0PX72, UniProt: P46883*PLUS, Oxidoreductases; Acting on the CH-NH2 group of donors; With oxygen as acceptor |
-Non-polymers , 4 types, 1220 molecules
#3: Chemical | #4: Chemical | #5: Chemical | ChemComp-GOL / #6: Water | ChemComp-HOH / | |
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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: 2.79 Å3/Da / Density % sol: 55.92 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / Details: 100 mM HEPES, 1.2 M sodium citrate / PH range: 6.9 - 7.2 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I02 / Wavelength: 0.979 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: May 10, 2012 |
Radiation | Monochromator: double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→105.05 Å / Num. obs: 196242 / % possible obs: 99.2 % / Redundancy: 5.1 % / CC1/2: 1 / Rmerge(I) obs: 0.036 / Rpim(I) all: 0.018 / Rrim(I) all: 0.04 / Net I/σ(I): 21.4 |
Reflection shell | Resolution: 1.7→1.73 Å / Redundancy: 5.1 % / Rmerge(I) obs: 0.785 / Mean I/σ(I) obs: 2.4 / Num. unique obs: 9515 / CC1/2: 0.873 / Rpim(I) all: 0.379 / Rrim(I) all: 0.875 / % possible all: 97.06 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS Starting model: 1DYU Resolution: 1.7→105.05 Å / Cor.coef. Fo:Fc: 0.976 / Cor.coef. Fo:Fc free: 0.969 / SU B: 2.588 / SU ML: 0.078 / Cross valid method: THROUGHOUT / ESU R: 0.087 / ESU R Free: 0.086 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 33.255 Å2
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Refinement step | Cycle: 1 / Resolution: 1.7→105.05 Å
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Refine LS restraints |
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