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- PDB-4nv8: Crystal Structure of Mesorhizobium Loti Arylamine N-acetyltransfe... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4nv8 | ||||||
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Title | Crystal Structure of Mesorhizobium Loti Arylamine N-acetyltransferase F42W Mutant | ||||||
![]() | Arylamine N-acetyltransferase | ||||||
![]() | TRANSFERASE / NAT / Arylamine N-acetyltransferase / acetyltransferase | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Xu, X.M. / Haouz, A. / Weber, P. / Li de la sierra-gallay, I. / Kubiak, X. / Dupret, J.-M. / Rodrigues-lima, F. | ||||||
![]() | ![]() Title: Insight into cofactor recognition in arylamine N-acetyltransferase enzymes: structure of Mesorhizobium loti arylamine N-acetyltransferase in complex with coenzyme A. Authors: Xu, X. / Li de la Sierra-Gallay, I. / Kubiak, X. / Duval, R. / Chaffotte, A.F. / Dupret, J.M. / Haouz, A. / Rodrigues-Lima, F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 121.8 KB | Display | ![]() |
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PDB format | ![]() | 93.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 443.3 KB | Display | ![]() |
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Full document | ![]() | 448.6 KB | Display | |
Data in XML | ![]() | 22.2 KB | Display | |
Data in CIF | ![]() | 32 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4nv7C ![]() 2bszS 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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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: _ / Ens-ID: 1 / Beg auth comp-ID: PRO / Beg label comp-ID: PRO / End auth comp-ID: GLU / End label comp-ID: GLU / Refine code: _ / Auth seq-ID: 5 - 275 / Label seq-ID: 39 - 309
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Components
#1: Protein | Mass: 34361.777 Da / Num. of mol.: 2 / Mutation: F42W Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.57 Å3/Da / Density % sol: 52.09 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 30% PEG 5000, 0.2M ammonium sulfate, 0.1M MES buffer, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: May 25, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.07169 Å / Relative weight: 1 |
Reflection | Resolution: 1.84→32.01 Å / Num. obs: 61856 / % possible obs: 99.7 % / Observed criterion σ(F): -3 / Rmerge(I) obs: 0.064 / Rsym value: 0.071 / Net I/σ(I): 14.1 |
Reflection shell | Resolution: 1.84→1.89 Å / Redundancy: 4.4 % / Rmerge(I) obs: 0.601 / Mean I/σ(I) obs: 2.2 / Rsym value: 0.682 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2BSZ Resolution: 1.84→32.01 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.942 / SU B: 2.886 / SU ML: 0.087 / Cross valid method: THROUGHOUT / ESU R: 0.126 / ESU R Free: 0.118 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.7 Å / Shrinkage radii: 0.7 Å / VDW probe radii: 1 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 33.561 Å2
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Refinement step | Cycle: LAST / Resolution: 1.84→32.01 Å
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Refine LS restraints |
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