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- PDB-5tcv: ACC oxidase complex with substrate 1-aminocyclopropane-1-carboxyl... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5tcv | ||||||
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Title | ACC oxidase complex with substrate 1-aminocyclopropane-1-carboxylic acid | ||||||
![]() | 1-aminocyclopropane-1-carboxylate oxidase 1 | ||||||
![]() | OXIDOREDUCTASE / substrate complex / OXYGENASE | ||||||
Function / homology | ![]() aminocyclopropanecarboxylate oxidase / 1-aminocyclopropane-1-carboxylate oxidase activity / coumarin biosynthetic process / response to molecule of fungal origin / ethylene biosynthetic process / 2-oxoglutarate-dependent dioxygenase activity / L-ascorbic acid binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gunawardana, D.M. / Yosaatmadja, Y. / Leung, I.K. / Squire, C.J. | ||||||
![]() | ![]() Title: ACC oxidase complex with substrate 1-aminocyclopropane-1-carboxylic acid Authors: Gunawardana, D.M. / Arabshahi, J. / Yosaatmadja, Y. / Reynisson, J. / Squire, C.J. / Leung, I.K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 75.5 KB | Display | ![]() |
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PDB format | ![]() | 54.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 439.2 KB | Display | ![]() |
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Full document | ![]() | 439.3 KB | Display | |
Data in XML | ![]() | 12.3 KB | Display | |
Data in CIF | ![]() | 15.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5tcwC ![]() 1wa6S C: citing same article ( S: Starting model for refinement |
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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: 36233.719 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q08506, aminocyclopropanecarboxylate oxidase |
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#2: Chemical | ChemComp-NI / |
#3: Chemical | ChemComp-1AC / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.85 Å3/Da / Density % sol: 56.83 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 10.5 Details: sodium dihydrogenphosphate, lithium sulfate, pottasium hydrogen phosphate, CAPS pH 10.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 210r / Detector: CCD / Date: Sep 7, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→39.96 Å / Num. obs: 13101 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 43.9 % / CC1/2: 1 / Net I/σ(I): 30 |
Reflection shell | Resolution: 2.6→2.72 Å / Redundancy: 44.5 % / Mean I/σ(I) obs: 1.7 / CC1/2: 0.718 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1WA6 Resolution: 2.6→39.96 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.915 / SU B: 16.651 / SU ML: 0.32 / Cross valid method: THROUGHOUT / ESU R: 0.566 / ESU R Free: 0.338 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 76.437 Å2
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Refinement step | Cycle: 1 / Resolution: 2.6→39.96 Å
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Refine LS restraints |
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