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Yorodumi- PDB-2xvj: Crystal structure of the mutant bacterial flavin containing monoo... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2xvj | ||||||
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Title | Crystal structure of the mutant bacterial flavin containing monooxygenase in complex with indole | ||||||
Components | FLAVIN-CONTAINING MONOOXYGENASE | ||||||
Keywords | OXIDOREDUCTASE | ||||||
Function / homology | Function and homology information trimethylamine monooxygenase / N,N-dimethylaniline monooxygenase activity / NADP binding / flavin adenine dinucleotide binding / identical protein binding Similarity search - Function | ||||||
Biological species | METHYLOPHAGA AMINISULFIDIVORANS (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.48 Å | ||||||
Authors | Cho, H.J. / Kang, B.S. | ||||||
Citation | Journal: J.Struct.Biol. / Year: 2011 Title: Structural and Functional Analysis of Bacterial Flavin-Containing Monooxygenase Reveals its Ping-Pong-Type Reaction Mechanism. Authors: Cho, H.J. / Cho, H.Y. / Kim, K.J. / Kim, M.H. / Kim, S.W. / Kang, B.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2xvj.cif.gz | 542.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2xvj.ent.gz | 452.2 KB | Display | PDB format |
PDBx/mmJSON format | 2xvj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2xvj_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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Full document | 2xvj_full_validation.pdf.gz | 1.2 MB | Display | |
Data in XML | 2xvj_validation.xml.gz | 50 KB | Display | |
Data in CIF | 2xvj_validation.cif.gz | 67 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xv/2xvj ftp://data.pdbj.org/pub/pdb/validation_reports/xv/2xvj | HTTPS FTP |
-Related 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
-Protein , 1 types, 3 molecules ABC
#1: Protein | Mass: 54048.414 Da / Num. of mol.: 3 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) METHYLOPHAGA AMINISULFIDIVORANS (bacteria) Strain: SK1 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) References: UniProt: Q83XK4, flavin-containing monooxygenase |
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-Non-polymers , 6 types, 154 molecules
#2: Chemical | #3: Chemical | #4: Chemical | #5: Chemical | #6: Chemical | ChemComp-MES / | #7: Water | ChemComp-HOH / | |
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-Details
Compound details | ENGINEERED RESIDUE IN CHAIN A, TYR 207 TO SER ENGINEERED RESIDUE IN CHAIN B, TYR 207 TO SER ...ENGINEERED |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.88 % / Description: NONE |
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Crystal grow | Details: 15% PEG 3350 0.1 M MES PH 6.0 0.2 M AMMONIUM NITRATE |
-Data collection
Diffraction | Mean temperature: 294 K |
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Diffraction source | Source: SYNCHROTRON / Site: PAL/PLS / Beamline: 6B / Wavelength: 1.1 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Jan 13, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→50 Å / Num. obs: 50468 / % possible obs: 98.1 % / Observed criterion σ(I): 2 / Redundancy: 3.4 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 17.9 |
Reflection shell | Resolution: 2.5→2.54 Å / Redundancy: 3 % / Rmerge(I) obs: 0.33 / Mean I/σ(I) obs: 2.64 / % possible all: 95 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: NONE Resolution: 2.48→50.01 Å / Cor.coef. Fo:Fc: 0.936 / Cor.coef. Fo:Fc free: 0.91 / SU B: 14.256 / SU ML: 0.156 / Cross valid method: THROUGHOUT / ESU R: 0.174 / ESU R Free: 0.061 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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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 mean: 41.834 Å2
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Refinement step | Cycle: LAST / Resolution: 2.48→50.01 Å
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Refine LS restraints |
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