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Yorodumi- PDB-3ltw: The structure of mycobacterium marinum arylamine n-acetyltransfer... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3ltw | ||||||
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Title | The structure of mycobacterium marinum arylamine n-acetyltransferase in complex with hydralazine | ||||||
Components | Arylamine N-acetyltransferase Nat | ||||||
Keywords | TRANSFERASE / Mycobacterium marinum / aryalmine N-acetyl transferase / MMNAT / hydralazine / Mycobacterium tuberculosis | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Mycobacterium marinum (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.1 Å | ||||||
Authors | Abuhammad, A.M. / Lowe, E.D. / Fullam, E. / Noble, M. / Garman, E.F. / Sim, E. | ||||||
Citation | Journal: Protein Cell / Year: 2010 Title: Probing the architecture of the Mycobacterium marinum arylamine N-acetyltransferase active site Authors: Abuhammad, A.M. / Lowe, E.D. / Fullam, E. / Noble, M. / Garman, E.F. / Sim, E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3ltw.cif.gz | 119.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3ltw.ent.gz | 92.5 KB | Display | PDB format |
PDBx/mmJSON format | 3ltw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3ltw_validation.pdf.gz | 453.4 KB | Display | wwPDB validaton report |
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Full document | 3ltw_full_validation.pdf.gz | 453.8 KB | Display | |
Data in XML | 3ltw_validation.xml.gz | 13 KB | Display | |
Data in CIF | 3ltw_validation.cif.gz | 17.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lt/3ltw ftp://data.pdbj.org/pub/pdb/validation_reports/lt/3ltw | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 30668.752 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mycobacterium marinum (bacteria) / Strain: ATCC BAA-535 / M / Gene: nat, MMAR_5055 / Plasmid: pET28B / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) PLYSS / References: UniProt: B2HIZ6, arylamine N-acetyltransferase | ||||
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#2: Chemical | #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: 1.94 Å3/Da / Density % sol: 36.67 % / Mosaicity: 0.42 ° |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion / pH: 6.7 Details: 0.1M sodium chloride 0.1M MES pH 6.7, 1.65M ammonium sulphate, vapour diffusion, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.873 Å |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Apr 23, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.873 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→38.952 Å / Num. all: 15018 / Num. obs: 15018 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.2 % / Rmerge(I) obs: 0.125 / Rsym value: 0.125 |
Reflection shell | Resolution: 2.1→2.21 Å / Redundancy: 5.1 % / Rmerge(I) obs: 0.58 / Mean I/σ(I) obs: 2.9 / Num. unique all: 2110 / % possible all: 100 |
-Phasing
Phasing | Method: molecular replacement | |||||||||
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Phasing MR |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.1→38.95 Å / Cor.coef. Fo:Fc: 0.936 / Cor.coef. Fo:Fc free: 0.903 / WRfactor Rfree: 0.258 / WRfactor Rwork: 0.211 / Occupancy max: 1 / Occupancy min: 0.5 / FOM work R set: 0.844 / SU B: 12.594 / SU ML: 0.152 / SU R Cruickshank DPI: 0.292 / SU Rfree: 0.222 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.292 / ESU R Free: 0.222 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES: RESIDUAL ONLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 58.74 Å2 / Biso mean: 28.511 Å2 / Biso min: 13.38 Å2
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Refinement step | Cycle: LAST / Resolution: 2.1→38.95 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.1→2.154 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Origin x: -24.458 Å / Origin y: -3.567 Å / Origin z: -12.022 Å
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