+Open data
-Basic information
Entry | Database: PDB / ID: 2jjh | ||||||
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Title | E243 mutant of M. tuberculosis Rv3290C | ||||||
Components | L-LYSINE EPSILON AMINOTRANSFERASE | ||||||
Keywords | TRANSFERASE / RV3290C / E243A MUTANT / M. TUBERCULOSIS / LYSINE EPSILON AMINOTRANSFERASE / AMINOTRANSFERASE / PYRIDOXAL PHOSPHATE | ||||||
Function / homology | Function and homology information L-lysine 6-transaminase / L-lysine 6-transaminase activity / 4-aminobutyrate transaminase activity / gamma-aminobutyric acid catabolic process / antibiotic biosynthetic process / pyridoxal phosphate binding Similarity search - Function | ||||||
Biological species | MYCOBACTERIUM TUBERCULOSIS (bacteria) | ||||||
Method | X-RAY DIFFRACTION / OTHER / Resolution: 2.7 Å | ||||||
Authors | Tripathi, S.M. / Ramachandran, R. | ||||||
Citation | Journal: Biochem.Biophys.Res.Commun. / Year: 2015 Title: Mutational Analysis of Mycobacterium Tuberculosis Lysine Epsilon-Aminotransferase and Inhibitor Co-Crystal Structures, Reveals Distinct Binding Modes. Authors: Tripathi, S.M. / Agarwal, A. / Ramachandran, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jjh.cif.gz | 91.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jjh.ent.gz | 74.3 KB | Display | PDB format |
PDBx/mmJSON format | 2jjh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jj/2jjh ftp://data.pdbj.org/pub/pdb/validation_reports/jj/2jjh | HTTPS FTP |
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-Related 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: 49010.934 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) MYCOBACTERIUM TUBERCULOSIS (bacteria) / Production host: ESCHERICHIA COLI (E. coli) References: UniProt: P63509, UniProt: P9WQ77*PLUS, L-lysine 6-transaminase |
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#2: Chemical | ChemComp-PLP / |
#3: Chemical | ChemComp-AKG / |
#4: Water | ChemComp-HOH / |
Compound details | ENGINEERED |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.11 Å3/Da / Density % sol: 60.12 % / Description: NONE |
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Wavelength: 1.5418 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→21.44 Å / Num. obs: 16720 / % possible obs: 99.6 % / Observed criterion σ(I): 2 / Redundancy: 3.5 % / Rmerge(I) obs: 0.14 / Net I/σ(I): 8.3 |
-Processing
Software | Name: REFMAC / Version: 5.2.0005 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: OTHER Starting model: NONE Resolution: 2.7→89.09 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.924 / SU B: 8.172 / SU ML: 0.163 / Cross valid method: THROUGHOUT / ESU R: 0.525 / ESU R Free: 0.249 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THIS ENTRY IS E243A MUTANT OF PDB 2CIN
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 20.266 Å2
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Refinement step | Cycle: LAST / Resolution: 2.7→89.09 Å
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Refine LS restraints |
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