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- PDB-3iw1: Crystal structure of Mycobacterium tuberculosis cytochrome P450 C... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3iw1 | ||||||
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Title | Crystal structure of Mycobacterium tuberculosis cytochrome P450 CYP125 in complex with androstenedione | ||||||
![]() | Cytochrome P450 CYP125 | ||||||
![]() | OXIDOREDUCTASE / androstenedione / cholesterol / monoxygenase / tuberculosis / cytochrome P450 / Heme / Iron / Metal-binding / Monooxygenase | ||||||
Function / homology | ![]() cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming] / biological process involved in interaction with host / cholest-4-en-3-one 26-monooxygenase activity / steroid hydroxylase activity / cholesterol catabolic process / iron ion binding / heme binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | McLean, K.J. / Levy, C. / Munro, A.W. / Leys, D. | ||||||
![]() | ![]() Title: The Structure of Mycobacterium tuberculosis CYP125: molecular basis for cholesterol binding in a P450 needed for host infection. Authors: McLean, K.J. / Lafite, P. / Levy, C. / Cheesman, M.R. / Mast, N. / Pikuleva, I.A. / Leys, D. / Munro, A.W. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 176.9 KB | Display | ![]() |
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PDB format | ![]() | 137.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 3ivySC ![]() 3iw0C ![]() 3iw2C S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 48491.492 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Protein was produced in E.coli HMS174(DE3) (typically 15-20 L, grown in 2YT media) by IPTG (0.15 mM) induction in presence of the heme precursor delta aminolevulinic acid (delALA, 0.1 mM) at ...Details: Protein was produced in E.coli HMS174(DE3) (typically 15-20 L, grown in 2YT media) by IPTG (0.15 mM) induction in presence of the heme precursor delta aminolevulinic acid (delALA, 0.1 mM) at OD600 = 0.6, with temperature then reduced from 37 deg C to 23 deg C and culture continued for 24 hrs. Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P63709, UniProt: P9WPP1*PLUS, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen |
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#2: Chemical | ChemComp-ASD / |
#3: Chemical | ChemComp-HEM / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.37 Å3/Da / Density % sol: 48.03 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: Crystallization was refined to two different conditions, both consisting of MgCl2 with 0.1 M HEPES (either pH 7.0 or 7.5) and 20% PEG 6000 or 25% PEG 3350, respectively., VAPOR DIFFUSION, ...Details: Crystallization was refined to two different conditions, both consisting of MgCl2 with 0.1 M HEPES (either pH 7.0 or 7.5) and 20% PEG 6000 or 25% PEG 3350, respectively., VAPOR DIFFUSION, SITTING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: Bruker Platinum 135 / Detector: CCD / Date: Jul 1, 2008 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→50 Å / Num. all: 30031 / Num. obs: 30031 / % possible obs: 99.02 % / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.089 / Net I/σ(I): 11.4 |
Reflection shell | Resolution: 2→2.1 Å / Rmerge(I) obs: 0.323 / Mean I/σ(I) obs: 3.5 / % possible all: 87.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 3IVY Resolution: 2→49.75 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.925 / SU B: 6.288 / SU ML: 0.096 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 1.687 / ESU R Free: 0.151 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 15.031 Å2
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Refinement step | Cycle: LAST / Resolution: 2→49.75 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.048 Å / Total num. of bins used: 20
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