+Open data
-Basic information
Entry | Database: PDB / ID: 5ys1 | ||||||
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Title | Crystal structure of Multicopper Oxidase CueO G304K mutant | ||||||
Components | Blue copper oxidase CueO | ||||||
Keywords | METAL BINDING PROTEIN / Multicopper Oxidase / Cu-binding protein / CueO mutant | ||||||
Function / homology | Function and homology information cuproxidase / oxidoreductase activity, acting on metal ions, oxygen as acceptor / oxidoreductase activity, acting on metal ions / detoxification of copper ion / oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor / response to copper ion / ferroxidase activity / outer membrane-bounded periplasmic space / periplasmic space / copper ion binding Similarity search - Function | ||||||
Biological species | Escherichia coli K12 (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.49 Å | ||||||
Authors | Wang, H.Q. / Liu, X.Q. / Zhao, J.T. / Yue, Q.X. / Yan, Y.H. / Dong, Y.H. / Fan, Y.L. / Tian, J. / Wu, N.F. / Gong, Y. | ||||||
Citation | Journal: Sci Rep / Year: 2018 Title: Crystal structures of multicopper oxidase CueO G304K mutant: structural basis of the increased laccase activity Authors: Wang, H. / Liu, X. / Zhao, J. / Yue, Q. / Yan, Y. / Gao, Z. / Dong, Y. / Zhang, Z. / Fan, Y. / Tian, J. / Wu, N. / Gong, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5ys1.cif.gz | 201.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5ys1.ent.gz | 157.5 KB | Display | PDB format |
PDBx/mmJSON format | 5ys1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ys/5ys1 ftp://data.pdbj.org/pub/pdb/validation_reports/ys/5ys1 | HTTPS FTP |
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-Related structure data
Related structure data | 5ys5C 1n68S 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
#1: Protein | Mass: 56695.117 Da / Num. of mol.: 1 / Mutation: G304K Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli K12 (bacteria) / Strain: K12 / Gene: cueO / Production host: Escherichia coli K-12 (bacteria) / Strain (production host): K-12 / References: UniProt: P36649 | ||
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#2: Chemical | #3: 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: 1.82 Å3/Da / Density % sol: 32.43 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: 0.2M Sodium formate (pH 8.5), 20%(w/v) Polyethyleneglycerol 3,350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U1 / Wavelength: 0.98 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Mar 25, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 1.49→50 Å / Num. obs: 65684 / % possible obs: 98.6 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.04 / Net I/σ(I): 26.9 |
Reflection shell | Resolution: 1.49→1.52 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.459 / % possible all: 88.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1N68 Resolution: 1.49→50 Å / SU ML: 0.16 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 17.61
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.49→50 Å
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Refine LS restraints |
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LS refinement shell |
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