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- PDB-6c9m: The Human NatA (Naa10/Naa15) amino-terminal acetyltransferase complex -
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Open data
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Basic information
Entry | Database: PDB / ID: 6c9m | ||||||
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Title | The Human NatA (Naa10/Naa15) amino-terminal acetyltransferase complex | ||||||
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![]() | TRANSFERASE / NatA / N-terminal acetylation / protein complex | ||||||
Function / homology | ![]() negative regulation of maintenance of mitotic sister chromatid cohesion, centromeric / N-terminal amino-acid Nalpha-acetyltransferase NatA / peptide-glutamate-alpha-N-acetyltransferase activity / NatA complex / peptide-serine-alpha-N-acetyltransferase activity / N-terminal protein amino acid acetylation / peptide alpha-N-acetyltransferase activity / N-acetyltransferase activity / internal protein amino acid acetylation / protein acetylation ...negative regulation of maintenance of mitotic sister chromatid cohesion, centromeric / N-terminal amino-acid Nalpha-acetyltransferase NatA / peptide-glutamate-alpha-N-acetyltransferase activity / NatA complex / peptide-serine-alpha-N-acetyltransferase activity / N-terminal protein amino acid acetylation / peptide alpha-N-acetyltransferase activity / N-acetyltransferase activity / internal protein amino acid acetylation / protein acetylation / chromosome organization / ribosome binding / angiogenesis / transcription regulator complex / cell differentiation / nuclear body / protein stabilization / intracellular membrane-bounded organelle / nucleolus / negative regulation of apoptotic process / positive regulation of DNA-templated transcription / RNA binding / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gottlieb, L. / Marmorstein, R. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of Human NatA and Its Regulation by the Huntingtin Interacting Protein HYPK. Authors: Gottlieb, L. / Marmorstein, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 771 KB | Display | ![]() |
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PDB format | ![]() | 642 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.4 MB | Display | ![]() |
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Full document | ![]() | 1.5 MB | Display | |
Data in XML | ![]() | 65.9 KB | Display | |
Data in CIF | ![]() | 88.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6c95C ![]() 4kvoS 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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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 101427.562 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 26522.602 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P41227, N-terminal amino-acid Nalpha-acetyltransferase NatA #3: Chemical | #4: Chemical | ChemComp-1PE / | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.85 Å3/Da / Density % sol: 56.89 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / Details: 16% PEG3350, 10% Tascimate, pH 7.5, 2% acetone |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Jul 28, 2017 |
Radiation | Monochromator: cryo-cooled double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→48.95 Å / Num. obs: 72780 / % possible obs: 99.8 % / Redundancy: 11.1 % / Rmerge(I) obs: 0.01 / Net I/σ(I): 20.8 |
Reflection shell | Resolution: 2.8→2.9 Å / Redundancy: 11.3 % / Rmerge(I) obs: 0.229 / Mean I/σ(I) obs: 1.44 / % possible all: 98.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 4KVO Resolution: 2.8→48.95 Å / SU ML: 0.4 / Cross valid method: THROUGHOUT / σ(F): 1.6 / Phase error: 26.12
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→48.95 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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