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- PDB-1s60: Aminoglycoside N-Acetyltransferase AAC(6')-Iy in Complex with CoA... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1s60 | ||||||
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Title | Aminoglycoside N-Acetyltransferase AAC(6')-Iy in Complex with CoA and N-terminal His(6)-tag (crystal form 2) | ||||||
![]() | aminoglycoside 6'-N-acetyltransferase | ||||||
![]() | TRANSFERASE / GNAT / N-acetyltransferase / acetyltransferase / aminoglycoside / CoA | ||||||
Function / homology | ![]() aminoglycoside 6'-N-acetyltransferase / aminoglycoside 6'-N-acetyltransferase activity / acetyl-CoA metabolic process / response to antibiotic / protein homodimerization activity Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Vetting, M.W. / Magnet, S. / Nieves, E. / Roderick, S.L. / Blanchard, J.S. | ||||||
![]() | ![]() Title: A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones Authors: Vetting, M.W. / Magnet, S. / Nieves, E. / Roderick, S.L. / Blanchard, J.S. #1: ![]() Title: Kinetic and mutagenic characterization of the chromosomally encoded Salmonella enterica AAC(6')-Iy aminoglycoside N-acetyltransferase Authors: Magnet, S. / Lambert, T. / Courvalin, P. / Blanchard, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 44.8 KB | Display | ![]() |
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PDB format | ![]() | 31 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 756.2 KB | Display | ![]() |
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Full document | ![]() | 763.8 KB | Display | |
Data in XML | ![]() | 9.8 KB | Display | |
Data in CIF | ![]() | 11.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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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Details | The biological assembly is a dimer generated from the monomer in the assymetric unit by the operations 1 0 0 0 -1 0 0 0 -1 0 146.5 89.0 |
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Components
#1: Protein | Mass: 18556.926 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q9R381, aminoglycoside 6'-N-acetyltransferase |
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#2: Chemical | ChemComp-SO4 / |
#3: Chemical | ChemComp-COA / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.71 Å3/Da / Density % sol: 66.89 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion under oil / pH: 8.8 Details: Bicine, Ammonium Sulfate, pH 8.8, vapor diffusion under oil, temperature 293K |
-Data collection
Diffraction | Mean temperature: 77 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jun 26, 2002 / Details: MSC Blue Confocal |
Radiation | Monochromator: Optics MSC Blue Confocal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 3→20 Å / Num. all: 5773 / Num. obs: 5773 / % possible obs: 95.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4 % / Biso Wilson estimate: 71 Å2 / Rsym value: 0.046 / Net I/σ(I): 19.8 |
Reflection shell | Resolution: 3→3.11 Å / Rsym value: 0.136 / % possible all: 87 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: Partially refined model created by fitting a Se-MET derived Map from same crystal form collected at synchotron radiation source. Resolution: 3→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 3→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3→3.14 Å / Rfactor Rfree: 0.352 / Rfactor Rwork: 0.281 |