+Open data
-Basic information
Entry | Database: PDB / ID: 3veg | ||||||
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Title | Rhodococcus jostii RHA1 DypB R244L variant in complex with heme | ||||||
Components | DypB | ||||||
Keywords | OXIDOREDUCTASE / peroxidase / lignan / Dyp | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Rhodococcus jostii (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.35 Å | ||||||
Authors | Grigg, J.C. / Singh, R. / Armstrong, Z. / Eltis, L.D. / Murphy, M.E.P. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2012 Title: Distal heme pocket residues of B-type dye-decolorizing peroxidase: arginine but not aspartate is essential for peroxidase activity. Authors: Singh, R. / Grigg, J.C. / Armstrong, Z. / Murphy, M.E. / Eltis, L.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3veg.cif.gz | 201.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3veg.ent.gz | 159.3 KB | Display | PDB format |
PDBx/mmJSON format | 3veg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ve/3veg ftp://data.pdbj.org/pub/pdb/validation_reports/ve/3veg | HTTPS FTP |
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-Related structure data
Related structure data | 3vecC 3vedC 3veeC 3vefC 3qnrS 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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Unit cell |
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-Components
#1: Protein | Mass: 37493.531 Da / Num. of mol.: 3 / Mutation: R244L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rhodococcus jostii (bacteria) / Strain: RHA1 / Gene: dypB, RHA1_ro02407 / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 References: UniProt: Q0SE24, Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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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: 3.62 Å3/Da / Density % sol: 66.02 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4.5 Details: 0.1 M sodium acetate trihydrate, 3 M sodium chloride, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: CLSI / Beamline: 08B1-1 / Wavelength: 0.97952 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: RAYONIX MX300HE / Detector: CCD / Date: Dec 15, 2010 Details: Collimating Mirror with two stripes (Si, Rh/Pt), Toroidal Focusing Mirror (Rh/Pt) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Monochromator: KOHZU double crystal monochromator (DCM), featuring indirectly water-cooled first crystal and flat, long second crystal Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.97952 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.35→115.375 Å / Num. obs: 67790 / % possible obs: 99.9 % / Redundancy: 6 % / Rmerge(I) obs: 0.096 / Χ2: 0.999 / Net I/σ(I): 10.8 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 3QNR Resolution: 2.35→53 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.934 / Occupancy max: 1 / Occupancy min: 0.4 / SU B: 5.503 / SU ML: 0.129 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.215 / ESU R Free: 0.185 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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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: 74.47 Å2 / Biso mean: 39.1026 Å2 / Biso min: 10.17 Å2
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Refinement step | Cycle: LAST / Resolution: 2.35→53 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.35→2.414 Å / Total num. of bins used: 20
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