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Open data
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Basic information
Entry | Database: PDB / ID: 4yrh | ||||||
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Title | p21 isoform of MEC-17 from Danio Rerio | ||||||
![]() | Alpha-tubulin N-acetyltransferase 1 | ||||||
![]() | TRANSFERASE / Acetyltransferase / acetylation / complex | ||||||
Function / homology | ![]() alpha-tubulin N-acetyltransferase / tubulin N-acetyltransferase activity / alpha-tubulin acetylation / lysine N-acetyltransferase activity, acting on acetyl phosphate as donor / neuron development / regulation of microtubule cytoskeleton organization / clathrin-coated pit / spindle / microtubule / axon ...alpha-tubulin N-acetyltransferase / tubulin N-acetyltransferase activity / alpha-tubulin acetylation / lysine N-acetyltransferase activity, acting on acetyl phosphate as donor / neuron development / regulation of microtubule cytoskeleton organization / clathrin-coated pit / spindle / microtubule / axon / focal adhesion / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Xue, T. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of DrMEC-17 residue 2-185 at 2.85 Angstroms resolution Authors: Xue, T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 154.8 KB | Display | ![]() |
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PDB format | ![]() | 130.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 18.6 KB | Display | |
Data in CIF | ![]() | 22.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 20885.523 Da / Num. of mol.: 2 / Fragment: UNP residues 2-185 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q6PH17, alpha-tubulin N-acetyltransferase #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.2 Å3/Da / Density % sol: 70.72 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.5 / Details: 25% PEG3350, 0.1M HEPES, 0.2M (NH4)2SO4 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Oct 14, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9791 Å / Relative weight: 1 |
Reflection | Resolution: 2.85→50 Å / Num. obs: 32007 / % possible obs: 98.9 % / Redundancy: 7 % / Net I/σ(I): 18.57 |
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Processing
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Refinement | Resolution: 2.861→49.272 Å / SU ML: 0.36 / Cross valid method: THROUGHOUT / σ(F): 0 / Phase error: 29.7 / Stereochemistry target values: MLHL
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.861→49.272 Å
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Refine LS restraints |
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LS refinement shell |
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