+Open data
-Basic information
Entry | Database: PDB / ID: 7v51 | |||||||||
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Title | BVMO_negative mutant D432V | |||||||||
Components | Putative flavin-binding monooxygenase | |||||||||
Keywords | OXIDOREDUCTASE / BVMO_negative mutant | |||||||||
Function / homology | Flavin monooxygenase-like / Flavin-binding monooxygenase-like / N,N-dimethylaniline monooxygenase activity / FAD/NAD(P)-binding domain superfamily / NADP binding / flavin adenine dinucleotide binding / FLAVIN-ADENINE DINUCLEOTIDE / Putative flavin-binding monooxygenase Function and homology information | |||||||||
Biological species | Acinetobacter calcoaceticus (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.42 Å | |||||||||
Authors | Wu, Y. / Yu, H.-L. | |||||||||
Funding support | 1items
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Citation | Journal: CHINESE J CATAL / Year: 2023 Title: Precise regulation of the substrate selectivity of Baeyer-Villiger monooxygenase to minimize overoxidation of prazole sulfoxides. Authors: Wu, Y. / Chen, Q.Q. / Chen, Q. / Geng, Q. / Zhang, Q. / Zheng, Y.C. / Zhao, C. / Zhang, Y. / Zhou, J. / Wang, B. / Xu, J.H. / Yu, H.L. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7v51.cif.gz | 122.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7v51.ent.gz | 91.4 KB | Display | PDB format |
PDBx/mmJSON format | 7v51.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7v51_validation.pdf.gz | 702.2 KB | Display | wwPDB validaton report |
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Full document | 7v51_full_validation.pdf.gz | 711.2 KB | Display | |
Data in XML | 7v51_validation.xml.gz | 22 KB | Display | |
Data in CIF | 7v51_validation.cif.gz | 30.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v5/7v51 ftp://data.pdbj.org/pub/pdb/validation_reports/v5/7v51 | HTTPS FTP |
-Related structure data
Related structure data | 7v4xC 7v50C 6a37S S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 60076.906 Da / Num. of mol.: 1 Mutation: F246Y,K326C,N386S,I388K,M390I,L426F,F432V,T433A,L435S,S438I,E488K,S489C,W490R,F505L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Acinetobacter calcoaceticus (bacteria) / Gene: P23_1101 Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) References: UniProt: A0A0A8XFY0 |
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#2: Chemical | ChemComp-FAD / |
#3: Water | ChemComp-HOH / |
Has ligand of interest | N |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48.84 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, sitting drop / Details: HEPES, PEG4000, CaCl2 |
-Data collection
Diffraction | Mean temperature: 80 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.987 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 1, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.987 Å / Relative weight: 1 |
Reflection | Resolution: 2.42→50 Å / Num. obs: 21933 / % possible obs: 99.8 % / Redundancy: 4.1 % / Rmerge(I) obs: 0.066 / Net I/σ(I): 15.628 |
Reflection shell | Resolution: 2.42→2.46 Å / Rmerge(I) obs: 0.066 / Num. unique obs: 431919 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 6A37 Resolution: 2.42→39.09 Å / SU ML: 0.31 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 25.8 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.42→39.09 Å
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Refine LS restraints |
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LS refinement shell |
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