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- PDB-4xnh: Crystal structure of yeast N-terminal acetyltransferase NatE (IP6... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4xnh | |||||||||
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Title | Crystal structure of yeast N-terminal acetyltransferase NatE (IP6) in complex with a bisubstrate | |||||||||
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![]() | TRANSFERASE / N-terminal acetyltransferase / bisubstrate / inositol hexaxisphosphate | |||||||||
Function / homology | ![]() cellular pigmentation / positive regulation of oxytocin production / Peptide hormone biosynthesis / Defective ACTH causes obesity and POMCD / type 1 melanocortin receptor binding / N-terminal protein amino acid propionylation / type 3 melanocortin receptor binding / type 4 melanocortin receptor binding / regulation of corticosterone secretion / response to melanocyte-stimulating hormone ...cellular pigmentation / positive regulation of oxytocin production / Peptide hormone biosynthesis / Defective ACTH causes obesity and POMCD / type 1 melanocortin receptor binding / N-terminal protein amino acid propionylation / type 3 melanocortin receptor binding / type 4 melanocortin receptor binding / regulation of corticosterone secretion / response to melanocyte-stimulating hormone / Opioid Signalling / N-terminal methionine Nalpha-acetyltransferase NatE / N-terminal amino-acid Nalpha-acetyltransferase NatA / peptide-glutamate-alpha-N-acetyltransferase activity / NatA complex / Androgen biosynthesis / peptide-serine-alpha-N-acetyltransferase activity / regulation of appetite / N-terminal protein amino acid acetylation / peptide alpha-N-acetyltransferase activity / Glucocorticoid biosynthesis / regulation of glycogen metabolic process / neuropeptide hormone activity / mitotic sister chromatid cohesion / positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway / negative regulation of tumor necrosis factor production / neuropeptide signaling pathway / Endogenous sterols / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / Peptide ligand-binding receptors / secretory granule / generation of precursor metabolites and energy / G protein-coupled receptor binding / calcium-mediated signaling / G-protein activation / hormone activity / regulation of blood pressure / cell-cell signaling / ribosome binding / glucose homeostasis / G alpha (i) signalling events / G alpha (s) signalling events / Interleukin-4 and Interleukin-13 signaling / secretory granule lumen / signaling receptor binding / signal transduction / positive regulation of transcription by RNA polymerase II / mitochondrion / extracellular space / extracellular region / identical protein binding / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Dong, J. / Wang, S. / York, J.D. | |||||||||
![]() | ![]() Title: Crystal structure of yeast N-terminal acetyltransferase NatE (IP6) in complex with a bisubstrate Authors: Dong, J. / Wang, S. / York, J.D. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 464.7 KB | Display | ![]() |
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PDB format | ![]() | 377.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.6 MB | Display | ![]() |
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Full document | ![]() | 1.6 MB | Display | |
Data in XML | ![]() | 47.4 KB | Display | |
Data in CIF | ![]() | 69.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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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
-N-terminal acetyltransferase A complex subunit ... , 2 types, 2 molecules AC
#1: Protein | Mass: 99050.133 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
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#3: Protein | Mass: 19753.727 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() References: UniProt: Q08689, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups |
-Protein / Protein/peptide , 2 types, 2 molecules BF
#2: Protein | Mass: 27635.168 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
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#4: Protein/peptide | Mass: 1058.169 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() |
-Non-polymers , 4 types, 675 molecules ![](data/chem/img/IHP.gif)
![](data/chem/img/ACO.gif)
![](data/chem/img/CMC.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/ACO.gif)
![](data/chem/img/CMC.gif)
![](data/chem/img/HOH.gif)
#5: Chemical | ChemComp-IHP / |
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#6: Chemical | ChemComp-ACO / |
#7: Chemical | ChemComp-CMC / |
#8: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.45 Å3/Da / Density % sol: 49.71 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / Details: 14% PEG 400, 0.1 M MES, pH 6.0 / PH range: 6 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jun 30, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.978 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→50 Å / Num. obs: 82940 / % possible obs: 99.7 % / Redundancy: 7.3 % / Net I/σ(I): 13 |
Reflection shell | Resolution: 2.1→2.18 Å |
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Processing
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Refinement | Resolution: 2.1→40.595 Å / SU ML: 0.23 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 24.3 / Stereochemistry target values: ML
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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: 2.1→40.595 Å
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Refine LS restraints |
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LS refinement shell |
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