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- PDB-1av4: CRYSTAL STRUCTURES OF THE COPPER-CONTAINING AMINE OXIDASE FROM AR... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1av4 | ||||||
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Title | CRYSTAL STRUCTURES OF THE COPPER-CONTAINING AMINE OXIDASE FROM ARTHROBACTER GLOBIFORMIS IN THE HOLO-AND APO-FORMS: IMPLICATIONS FOR THE BIOGENESIS OF TOPA QUINONE | ||||||
![]() | AMINE OXIDASE | ||||||
![]() | OXIDOREDUCTASE / COPPER CONTAINING / AMINE OXIDASE / ARTHROBACTER GLOBIFORMIS | ||||||
Function / homology | ![]() primary-amine oxidase / aliphatic amine oxidase activity / primary methylamine oxidase activity / amine metabolic process / quinone binding / copper ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Wilce, M.C.J. / Guss, J.M. / Freeman, H.C. | ||||||
![]() | ![]() Title: Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone. Authors: Wilce, M.C. / Dooley, D.M. / Freeman, H.C. / Guss, J.M. / Matsunami, H. / McIntire, W.S. / Ruggiero, C.E. / Tanizawa, K. / Yamaguchi, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 136.3 KB | Display | ![]() |
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PDB format | ![]() | 108 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 433.6 KB | Display | ![]() |
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Full document | ![]() | 442.1 KB | Display | |
Data in XML | ![]() | 26.4 KB | Display | |
Data in CIF | ![]() | 38 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1avkC ![]() 1avlC ![]() 1oacS S: Starting model for refinement 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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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 70752.742 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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#2: Chemical | ChemComp-CU / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.1 Å3/Da / Density % sol: 58 % | ||||||||||||||||||
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Crystal grow | pH: 8.1 / Details: pH 8.1 | ||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Detector: FILM / Date: Dec 1, 1995 / Details: BENT QUARTZ CRYSTAL |
Radiation | Monochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→8 Å / Num. obs: 33778 / % possible obs: 90.1 % / Observed criterion σ(I): -3 / Redundancy: 3.13 % / Biso Wilson estimate: 23 Å2 / Rmerge(I) obs: 0.085 |
Reflection shell | Resolution: 2.2→2.3 Å / Rmerge(I) obs: 0.31 / % possible all: 90 |
Reflection | *PLUS Num. measured all: 105840 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1OAC Resolution: 2.2→8 Å / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Cross valid method: THROUGHOUT / σ(F): 0 Details: STANDARD X-PLOR LIBRARIES USED FOR REFINEMENT EXCEPT FOR TPQ-NEW.PAR/.TOP FOR RESIDUE TPQ 382
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Displacement parameters | Biso mean: 20 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.3 Å / Total num. of bins used: 10
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.2 / Rfactor Rwork: 0.2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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