+Open data
-Basic information
Entry | Database: PDB / ID: 2x80 | ||||||
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Title | P450 BM3 F87A in complex with DMSO | ||||||
Components | BIFUNCTIONAL P-450/NADPH-P450 REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE / ELECTRON TRANSPORT / DMSO-INHIBITION / METAL-BINDING | ||||||
Function / homology | Function and homology information NADPH-hemoprotein reductase / NADPH-hemoprotein reductase activity / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen / unspecific monooxygenase / aromatase activity / metabolic process / FMN binding / iron ion binding / heme binding / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | BACILLUS MEGATERIUM (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Kuper, J. / Wong, T.S. / Roccatano, D. / Wilmanns, M. / Schwaneberg, U. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.F / Year: 2012 Title: The Role of Active-Site Phe87 in Modulating the Organic Co-Solvent Tolerance of Cytochrome P450 Bm3 Monooxygenase. Authors: Kuper, J. / Tee, K.L. / Wilmanns, M. / Roccatano, D. / Schwaneberg, U. / Wong, T.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2x80.cif.gz | 202.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2x80.ent.gz | 162.4 KB | Display | PDB format |
PDBx/mmJSON format | 2x80.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/x8/2x80 ftp://data.pdbj.org/pub/pdb/validation_reports/x8/2x80 | HTTPS FTP |
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-Related structure data
Related structure data | 2x7yC 2j4sS C: citing same article (ref.) 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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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.5309, 0.8469, -0.03183), Vector: |
-Components
#1: Protein | Mass: 52093.367 Da / Num. of mol.: 2 / Fragment: HEME DOMAIN, RESIDUES 2-456 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) BACILLUS MEGATERIUM (bacteria) / Plasmid: PETM11 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: P14779, unspecific monooxygenase #2: Chemical | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | Compound details | ENGINEERED | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.19 Å3/Da / Density % sol: 61.41 % / Description: NONE |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X12 / Wavelength: 0.98 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Apr 10, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→47.62 Å / Num. obs: 58691 / % possible obs: 99.7 % / Observed criterion σ(I): -3 / Redundancy: 6.49 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 12.42 |
Reflection shell | Resolution: 2.3→2.32 Å / Redundancy: 6.42 % / Rmerge(I) obs: 0.49 / Mean I/σ(I) obs: 3.17 / % possible all: 99.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2J4S Resolution: 2.3→41.1 Å / Cor.coef. Fo:Fc: 0.938 / Cor.coef. Fo:Fc free: 0.907 / SU B: 6.742 / SU ML: 0.166 / Cross valid method: THROUGHOUT / ESU R: 0.27 / ESU R Free: 0.22 / 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 / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL PLUS MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 43.977 Å2
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Refinement step | Cycle: LAST / Resolution: 2.3→41.1 Å
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Refine LS restraints |
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