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Yorodumi- PDB-3sma: A new N-acetyltransferase fold in the structure and mechanism of ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3sma | ||||||
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Title | A new N-acetyltransferase fold in the structure and mechanism of the phosphonate biosynthetic enzyme FrbF | ||||||
Components | FrbF | ||||||
Keywords | TRANSFERASE / N-acetyl transferase / acetyl CoA binding | ||||||
Function / homology | aminoglycoside 3-N-acetyltransferase / aminoglycoside 3-N-acetyltransferase activity / Aminoglycoside N(3)-acetyltransferase / Aminoglycoside 3-N-acetyltransferase / Aminoglycoside 3-N-acetyltransferase-like / response to antibiotic / ACETYL COENZYME *A / Aminoglycoside N(3)-acetyltransferase Function and homology information | ||||||
Biological species | Streptomyces rubellomurinus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Bae, B. / Nair, S.K. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2011 Title: New N-Acetyltransferase Fold in the Structure and Mechanism of the Phosphonate Biosynthetic Enzyme FrbF. Authors: Bae, B. / Cobb, R.E. / Desieno, M.A. / Zhao, H. / Nair, S.K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3sma.cif.gz | 223.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3sma.ent.gz | 180.6 KB | Display | PDB format |
PDBx/mmJSON format | 3sma.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3sma_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 3sma_full_validation.pdf.gz | 1.2 MB | Display | |
Data in XML | 3sma_validation.xml.gz | 46.8 KB | Display | |
Data in CIF | 3sma_validation.cif.gz | 64 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sm/3sma ftp://data.pdbj.org/pub/pdb/validation_reports/sm/3sma | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 31586.535 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptomyces rubellomurinus (bacteria) / Gene: frbF / Production host: Escherichia coli (E. coli) / References: UniProt: Q0ZQ43 #2: Chemical | ChemComp-ACO / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.19 Å3/Da / Density % sol: 43.95 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.7 Details: 0.2M magnesium chloride, 0.1 Tris, 20%-25% peg 4000, 20% glycerol, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 21-ID-D |
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Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jun 12, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2→45.34 Å / Num. all: 93253 / Num. obs: 74767 / Biso Wilson estimate: 26.44 Å2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→45.34 Å / Cor.coef. Fo:Fc: 0.8846 / Cor.coef. Fo:Fc free: 0.8466 / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 35.93 Å2
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Refine analyze | Luzzati coordinate error obs: 0.254 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→45.34 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.05 Å / Total num. of bins used: 20
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