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- PDB-1wxc: Crystal Structure of the copper-free Streptomyces castaneoglobisp... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1wxc | ||||||
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Title | Crystal Structure of the copper-free Streptomyces castaneoglobisporus tyrosinase complexed with a caddie protein | ||||||
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![]() | OXIDOREDUCTASE/METAL TRANSPORT / tyrosinase / binary complex / type-3 copper / OXIDOREDUCTASE-METAL TRANSPORT COMPLEX | ||||||
Function / homology | ![]() tyrosinase activity / melanin biosynthetic process / pigmentation / copper ion binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Matoba, Y. / Kumagai, T. / Yamamoto, A. / Yoshitsu, H. / Sugiyama, M. | ||||||
![]() | ![]() Title: Crystallographic Evidence That the Dinuclear Copper Center of Tyrosinase Is Flexible during Catalysis Authors: Matoba, Y. / Kumagai, T. / Yamamoto, A. / Yoshitsu, H. / 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 | ![]() | 92.5 KB | Display | ![]() |
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PDB format | ![]() | 69.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 447.4 KB | Display | ![]() |
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Full document | ![]() | 452.3 KB | Display | |
Data in XML | ![]() | 19.3 KB | Display | |
Data in CIF | ![]() | 29 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1wx2C ![]() 1wx4C ![]() 1wx5C ![]() 2ahkC ![]() 2ahlC ![]() 2zmxC 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: 32089.564 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: tyrc / Plasmid: pET-mel2 / Production host: ![]() ![]() | ||
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#2: Protein | Mass: 14203.812 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: orf378 / Plasmid: pET-mel2 / Production host: ![]() ![]() | ||
#3: Chemical | ChemComp-NO3 / #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.89 Å3/Da / Density % sol: 34.9 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: peg3350, sodium nitrate, hepes, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Feb 16, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.6199 Å / Relative weight: 1 |
Reflection | Resolution: 1.2→100 Å / Num. all: 104674 / Num. obs: 102888 / % possible obs: 97.8 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 1 / Redundancy: 8.1 % / Rmerge(I) obs: 0.085 / Rsym value: 0.08 / Net I/σ(I): 16.4 |
Reflection shell | Resolution: 1.2→1.26 Å / Redundancy: 5.1 % / Rmerge(I) obs: 0.366 / Mean I/σ(I) obs: 4.6 / Num. unique all: 15330 / Rsym value: 0.329 / % possible all: 99 |
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Processing
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Refinement | Method to determine structure: ![]()
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Refine analyze | Num. disordered residues: 15 / Occupancy sum hydrogen: 0 / Occupancy sum non hydrogen: 3150 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.2→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.2→1.28 Å
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