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- PDB-1s7n: Ribosomal L7/L12 alpha-N-protein acetyltransferase in complex wit... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1s7n | ||||||
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Title | Ribosomal L7/L12 alpha-N-protein acetyltransferase in complex with Coenzyme A (CoA free sulfhydryl) | ||||||
![]() | acetyl transferase | ||||||
![]() | TRANSFERASE / acetyltransferase / GNAT / alpha-N-protein acetyltransferase / Coenzyme A / L7/L12 | ||||||
Function / homology | ![]() peptide-alanine-alpha-N-acetyltransferase activity / peptide-serine-alpha-N-acetyltransferase activity / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Vetting, M.W. / de Carvalho, L.P. / Roderick, S.L. / Blanchard, J.S. | ||||||
![]() | ![]() Title: A novel dimeric structure of the RimL Nalpha-acetyltransferase from Salmonella typhimurium. Authors: Vetting, M.W. / de Carvalho, L.P. / Roderick, S.L. / Blanchard, J.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 164 KB | Display | ![]() |
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PDB format | ![]() | 131 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.4 MB | Display | ![]() |
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Full document | ![]() | 1.4 MB | Display | |
Data in XML | ![]() | 33.6 KB | Display | |
Data in CIF | ![]() | 46.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1s7fSC ![]() 1s7kC ![]() 1s7lC 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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Details | The biological assembly is a dimer. Monomers A/B and C/D make up the two physiological dimers in the asymmetric unit. |
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Components
#1: Protein | Mass: 20912.771 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q8ZPC0, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups #2: Chemical | ChemComp-COA / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.54 Å3/Da / Density % sol: 51.61 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion under oil / pH: 8 Details: pentaerythritiol propoxylate 426, triethanolamine, KCl, ammonium sulfate, acetylCoenzyme A, TCEP, pH 8.0, 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: May 23, 2003 / Details: MSC Blue Confocal |
Radiation | Monochromator: 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: 2.1→30 Å / Num. all: 45918 / Num. obs: 45918 / % possible obs: 93.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.4 % / Biso Wilson estimate: 31.7 Å2 / Rsym value: 0.046 / Net I/σ(I): 16.9 |
Reflection shell | Resolution: 2.1→2.18 Å / Redundancy: 2.1 % / Rsym value: 0.13 / % possible all: 86.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1S7F Resolution: 2.1→30 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: 2.1→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.1→2.18 Å / Rfactor Rfree: 0.265 / Rfactor Rwork: 0.239 |