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Yorodumi- PDB-3lnb: Crystal Structure Analysis of Arylamine N-acetyltransferase C fro... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3lnb | ||||||
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Title | Crystal Structure Analysis of Arylamine N-acetyltransferase C from Bacillus anthracis | ||||||
Components | N-acetyltransferase family protein | ||||||
Keywords | TRANSFERASE / arylamine N-acetyltransferase / nat / acetyltransferase / Acyltransferase | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Bacillus anthracis (anthrax bacterium) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.01 Å | ||||||
Authors | Li de la Sierra-Gallay, I. / Pluvinage, B. / Rodrigues-Lima, F. | ||||||
Citation | Journal: Febs Lett. / Year: 2011 Title: The Bacillus anthracis arylamine N-acetyltransferase ((BACAN)NAT1) that inactivates sulfamethoxazole, reveals unusual structural features compared with the other NAT isoenzymes. Authors: Pluvinage, B. / Li de la Sierra-Gallay, I. / Kubiak, X. / Xu, X. / Dairou, J. / Dupret, J.M. / Rodrigues-Lima, F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3lnb.cif.gz | 71.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3lnb.ent.gz | 50.3 KB | Display | PDB format |
PDBx/mmJSON format | 3lnb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3lnb_validation.pdf.gz | 752.7 KB | Display | wwPDB validaton report |
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Full document | 3lnb_full_validation.pdf.gz | 755.3 KB | Display | |
Data in XML | 3lnb_validation.xml.gz | 13.1 KB | Display | |
Data in CIF | 3lnb_validation.cif.gz | 18.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ln/3lnb ftp://data.pdbj.org/pub/pdb/validation_reports/ln/3lnb | HTTPS FTP |
-Related structure data
Related structure data | 1e2tS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 35302.488 Da / Num. of mol.: 1 / Mutation: Y38F Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus anthracis (anthrax bacterium) / Strain: Strain Sterne (RTC50) / Plasmid: pET28a / Production host: Escherichia coli (E. coli) References: UniProt: Q81R98, UniProt: A0A6L7HKL6*PLUS, arylamine N-acetyltransferase | ||
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#2: Chemical | ChemComp-COA / | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.779778 Å3/Da / Density % sol: 30.890238 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion Details: 1.8-1.9M Ammonium sulfate, 0.17M-0.2M potassium nitrate, VAPOR DIFFUSION, temperature 294K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.92 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 21, 2008 / Details: mirrors |
Radiation | Monochromator: Silicon 1 1 1 channel / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Resolution: 2→50 Å / Num. all: 18116 / Num. obs: 17034 / % possible obs: 94 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 5.68 % / Biso Wilson estimate: 24.85 Å2 / Rmerge(I) obs: 0.062 / Rsym value: 0.063 / Net I/σ(I): 20.45 |
Reflection shell | Resolution: 2→2.2 Å / Redundancy: 4.24 % / Rmerge(I) obs: 0.202 / Mean I/σ(I) obs: 7.91 / Num. unique all: 4366 / Rsym value: 0.177 / % possible all: 75.7 |
-Phasing
Phasing | Method: molecular replacement | ||||||||||||||||||
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Phasing MR | Cor.coef. Fo:Fc: 0.69 / Packing: 0.682
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1E2T Resolution: 2.01→45.76 Å / Rfactor Rfree error: 0.008 / Occupancy max: 1 / Occupancy min: 1 / Data cutoff high absF: 2205494 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber / Details: BULK SOLVENT MODEL USED
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 39.02 Å2 / ksol: 0.4 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 44.33 Å2 / Biso mean: 19.19 Å2 / Biso min: 8.73 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.01→45.76 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.01→2.13 Å / Rfactor Rfree error: 0.022 / Total num. of bins used: 6
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Xplor file |
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