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- PDB-2whw: Selective oxidation of carbolide C-H bonds by engineered macrolid... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2whw | ||||||
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Title | Selective oxidation of carbolide C-H bonds by engineered macrolide P450 monooxygenase | ||||||
![]() | CYTOCHROME P450 MONOOXYGENASE | ||||||
![]() | OXIDOREDUCTASE / ANTIBIOTIC BIOSYNTHESIS / CYP107L1 / CYTOCHROME P450 / HEME / IRON / MACROLIDE MONOOXYGENASE / METAL-BINDING / MONOOXYGENASE / OXIDOREDUCTASE ANTIBIOTIC BIOSYNTHESIS / PIKC | ||||||
Function / homology | ![]() pikromycin synthase / macrolide biosynthetic process / cholest-4-en-3-one 26-monooxygenase activity / steroid hydroxylase activity / cholesterol catabolic process / monooxygenase activity / iron ion binding / heme binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Li, S. / Chaulagain, M.R. / Knauff, A.R. / Podust, L.M. / Montgomery, J. / Sherman, D.H. | ||||||
![]() | ![]() Title: Selective Oxidation of Carbolide C-H Bonds by an Engineered Macrolide P450 Mono-Oxygenase. Authors: Li, S. / Chaulagain, M.R. / Knauff, A.R. / Podust, L.M. / Montgomery, J. / Sherman, D.H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 188 KB | Display | ![]() |
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PDB format | ![]() | 148.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2wi9C ![]() 2c6hS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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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: (-0.99997, -0.00789, 0.00156), Vector: |
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Components
#1: Protein | Mass: 48181.641 Da / Num. of mol.: 2 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | Compound details | ENGINEERED | Sequence details | 20 N-TERMINAL RESIDUES INCLUDING 6XHIS TAG ARE ENGINEERED | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.75 Å3/Da / Density % sol: 55.2 % / Description: NONE |
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Crystal grow | pH: 6.5 Details: 12% PEG 8000, 0.1 M NA CACODILATE, PH 6.5; 200 MM LI2SO4 |
-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Apr 26, 2008 / Details: MIRRORS |
Radiation | Monochromator: SI (111) DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.11587 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→50 Å / Num. obs: 52386 / % possible obs: 99.8 % / Observed criterion σ(I): 0 / Redundancy: 4.2 % / Biso Wilson estimate: 27 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 20.9 |
Reflection shell | Resolution: 2.2→2.24 Å / Redundancy: 4.3 % / Rmerge(I) obs: 0.5 / Mean I/σ(I) obs: 3.6 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2C6H Resolution: 2.2→89.09 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.904 / SU B: 4.981 / SU ML: 0.129 / Cross valid method: THROUGHOUT / ESU R: 0.229 / ESU R Free: 0.217 / 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: 27.95 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→89.09 Å
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Refine LS restraints |
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