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- PDB-5icw: Crystal structure of human NatF (hNaa60) homodimer bound to Coenzyme A -
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Open data
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Basic information
Entry | Database: PDB / ID: 5icw | |||||||||||||||||||||
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Title | Crystal structure of human NatF (hNaa60) homodimer bound to Coenzyme A | |||||||||||||||||||||
![]() | N-alpha-acetyltransferase 60 | |||||||||||||||||||||
![]() | TRANSFERASE / Acetylation / GNAT / NAT | |||||||||||||||||||||
Function / homology | ![]() N-terminal methionine Nalpha-acetyltransferase NatF / N-terminal peptidyl-methionine acetylation / N-terminal protein amino acid acetylation / peptide alpha-N-acetyltransferase activity / histone H4 acetyltransferase activity / histone acetyltransferase activity / histone acetyltransferase / chromosome segregation / nucleosome assembly / cell population proliferation ...N-terminal methionine Nalpha-acetyltransferase NatF / N-terminal peptidyl-methionine acetylation / N-terminal protein amino acid acetylation / peptide alpha-N-acetyltransferase activity / histone H4 acetyltransferase activity / histone acetyltransferase activity / histone acetyltransferase / chromosome segregation / nucleosome assembly / cell population proliferation / Golgi membrane / protein homodimerization activity Similarity search - Function | |||||||||||||||||||||
Biological species | ![]() | |||||||||||||||||||||
Method | ![]() ![]() ![]() | |||||||||||||||||||||
![]() | Stove, S.I. / Magin, R.S. / Marmorstein, R. / Arnesen, T. | |||||||||||||||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Crystal Structure of the Golgi-Associated Human N alpha-Acetyltransferase 60 Reveals the Molecular Determinants for Substrate-Specific Acetylation. Authors: Stve, S.I. / Magin, R.S. / Foyn, H. / Haug, B.E. / Marmorstein, R. / Arnesen, 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 | ![]() | 168.3 KB | Display | ![]() |
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PDB format | ![]() | 133.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5icvC ![]() 4lx9S 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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3 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 20767.590 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q9H7X0, histone acetyltransferase, EC: 2.3.1.88 #2: Chemical | ChemComp-COA / #3: Chemical | ChemComp-CL / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.24 Å3/Da / Density % sol: 45 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, hanging drop Details: 3% Tascimate, 0.1 M Bistris pH 6.5 and 16% PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Mar 2, 2014 |
Radiation | Monochromator: Rigaku Osmic VariMax HF / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.951→46.458 Å / Num. obs: 52859 / % possible obs: 94.63 % / Redundancy: 13 % / Rmerge(I) obs: 0.098 / Net I/σ(I): 12.82 |
Reflection shell | Resolution: 1.951→1.989 Å |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4LX9 Resolution: 1.951→46.249 Å / SU ML: 0.25 / Cross valid method: FREE R-VALUE / σ(F): 1.37 / Phase error: 31.57 / 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: 1.951→46.249 Å
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Refine LS restraints |
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LS refinement shell |
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