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- PDB-5z0m: Crystal structure of copper-bound H63F-mutated tyrosinase from St... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5z0m | ||||||
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Title | Crystal structure of copper-bound H63F-mutated tyrosinase from Streptomyces castaneoglobisporus in complex with the caddie protein obtained by soaking in the hydroxylamine-containing solution for 12 h at 298 K | ||||||
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![]() | OXIDOREDUCTASE/METAL BINDING PROTEIN / tyrosinase / catalytic mechanism / OXIDOREDUCTASE-METAL BINDING PROTEIN complex | ||||||
Function / homology | ![]() tyrosinase activity / melanin biosynthetic process / pigmentation / copper ion binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Matoba, Y. / Sugiyama, M. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Catalytic mechanism of tyrosinase implied from the quinone formation on the Tyr98 residue of the caddie protein Authors: Matoba, Y. / Sugiyama, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 167.4 KB | Display | ![]() |
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PDB format | ![]() | 136.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 455.9 KB | Display | ![]() |
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Full document | ![]() | 460.5 KB | Display | |
Data in XML | ![]() | 19.1 KB | Display | |
Data in CIF | ![]() | 28 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5z0dC ![]() 5z0eC ![]() 5z0fC ![]() 5z0gC ![]() 5z0hC ![]() 5z0iC ![]() 5z0jC ![]() 5z0kC ![]() 5z0lC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 32098.592 Da / Num. of mol.: 1 / Mutation: H63F Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: HUT6202 / Gene: tyrC / Plasmid: pET-mel2 / Production host: ![]() ![]() | ||||||
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#2: Protein | Mass: 14105.643 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: HUT6202 / Gene: orf378 / Plasmid: pET-mel2 / Production host: ![]() ![]() | ||||||
#3: Chemical | #4: Chemical | ChemComp-NO3 / #5: Water | ChemComp-HOH / | Sequence details | TYR98 IN PROTEIN MELC WAS PARTIALLY HYDROXYLAT | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.93 Å3/Da / Density % sol: 34.53 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 6.5 / Details: PEG 3350, SODIUM NITRATE, HEPES |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX-225 / Detector: CCD / Date: Jan 25, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→100 Å / Num. obs: 35544 / % possible obs: 90.7 % / Redundancy: 6 % / Rmerge(I) obs: 0.058 / Net I/σ(I): 28.8 |
Reflection shell | Resolution: 1.7→1.76 Å / Redundancy: 5.1 % / Rmerge(I) obs: 0.442 / Mean I/σ(I) obs: 2.7 / Num. unique obs: 3515 / % possible all: 91.8 |
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Processing
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Refinement | Method to determine structure: ![]() Details: ANISOTROPIC REFINEMENT REDUCED FREE R (NO CUTOFF) BY ?
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Refine analyze | Num. disordered residues: 14 / Occupancy sum hydrogen: 0 / Occupancy sum non hydrogen: 3120.4 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→30 Å
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Refine LS restraints |
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