+Open data
-Basic information
Entry | Database: PDB / ID: 1n68 | ||||||
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Title | Copper bound to the Multicopper Oxidase CueO | ||||||
Components | Blue copper oxidase cueO | ||||||
Keywords | OXIDOREDUCTASE / copper / multicopper oxidase | ||||||
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 (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.7 Å | ||||||
Authors | Roberts, S.A. / Wildner, G.F. / Grass, G. / Weichsel, A. / Ambrus, A. / Rensing, C. / Montfort, W.R. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2003 Title: A Labile Regulatory Copper Ion Lies Near the T1 Copper Site in the Multicopper Oxidase CueO. Authors: Roberts, S.A. / Wildner, G.F. / Grass, G. / Weichsel, A. / Ambrus, A. / Rensing, C. / Montfort, W.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1n68.cif.gz | 114.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1n68.ent.gz | 85.7 KB | Display | PDB format |
PDBx/mmJSON format | 1n68.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1n68_validation.pdf.gz | 440.1 KB | Display | wwPDB validaton report |
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Full document | 1n68_full_validation.pdf.gz | 443 KB | Display | |
Data in XML | 1n68_validation.xml.gz | 22.8 KB | Display | |
Data in CIF | 1n68_validation.cif.gz | 35 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n6/1n68 ftp://data.pdbj.org/pub/pdb/validation_reports/n6/1n68 | HTTPS FTP |
-Related structure data
Related structure data | 1pf3C 1kv7S 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: 53483.285 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: CUEO / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P36649 | ||||
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#2: Chemical | ChemComp-CU / #3: Chemical | ChemComp-C2C / | #4: 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: 2.23 Å3/Da / Density % sol: 44.92 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: 20% PEG, 200 MM AMMONIUM ACETATE, 100 MM SODIUM ACETATE,10 MM COPPER CHLORIDE , pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL9-2 / Wavelength: 1.378 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: May 16, 2002 / Details: double crystal monochromator |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.378 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→26.3 Å / Num. all: 51492 / Num. obs: 51492 / % possible obs: 99.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.6 % / Biso Wilson estimate: 26 Å2 / Rsym value: 0.075 / Net I/σ(I): 11.6 |
Reflection shell | Resolution: 1.7→1.76 Å / Redundancy: 4.6 % / Mean I/σ(I) obs: 3 / Num. unique all: 5142 / Rsym value: 0.256 / % possible all: 100 |
-Processing
Software |
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Refinement | Starting model: PDB ENTRY 1KV7 Resolution: 1.7→26.3 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber Details: Missing from the model are residues 1-29 at the N-terminus (1-28 are a presumably cleaved signal peptide), and residues 380-402 which are not visible in the electron density map and ...Details: Missing from the model are residues 1-29 at the N-terminus (1-28 are a presumably cleaved signal peptide), and residues 380-402 which are not visible in the electron density map and presumably disordered. Metal-ligand bond distances and angles were not restrained.
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Displacement parameters | Biso mean: 21.4 Å2 | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→26.3 Å
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Refine LS restraints |
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