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Open data
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Basic information
Entry | Database: PDB / ID: 1jme | ||||||
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Title | Crystal Structure of Phe393His Cytochrome P450 BM3 | ||||||
![]() | BIFUNCTIONAL P-450:NADPH-P450 REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / CYTOCHROME P450 / FATTY ACID HYDROXYLASE / MONOOXYGENASE | ||||||
Function / homology | ![]() 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 / response to hormone / FMN binding / flavin adenine dinucleotide binding / iron ion binding ...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 / response to hormone / FMN binding / flavin adenine dinucleotide binding / iron ion binding / heme binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Ost, T.W.B. / Munro, A.W. / Mowat, C.G. / Pesseguiero, A. / Fulco, A.J. / Cho, A.K. / Cheesman, M.A. / Walkinshaw, M.D. / Chapman, S.K. | ||||||
![]() | ![]() Title: Structural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3. Authors: Ost, T.W. / Munro, A.W. / Mowat, C.G. / Taylor, P.R. / Pesseguiero, A. / Fulco, A.J. / Cho, A.K. / Cheesman, M.A. / Walkinshaw, M.D. / Chapman, S.K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 215.5 KB | Display | ![]() |
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PDB format | ![]() | 169.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 547.1 KB | Display | ![]() |
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Full document | ![]() | 561.9 KB | Display | |
Data in XML | ![]() | 20 KB | Display | |
Data in CIF | ![]() | 36.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2hpdS 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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Unit cell |
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Components
#1: Protein | Mass: 52160.434 Da / Num. of mol.: 2 / Fragment: CYTOCHROME P450 / Mutation: F393H Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.64 Å3/Da / Density % sol: 53.49 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: PEG 8000, PIPES, magnesium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP at 277K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7.4 | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: May 20, 2000 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.3 Å / Relative weight: 1 |
Reflection | Resolution: 2→40 Å / Num. all: 73016 / Num. obs: 73016 / % possible obs: 96.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.58 % / Biso Wilson estimate: 25.5 Å2 / Rmerge(I) obs: 0.054 / Net I/σ(I): 19.4 |
Reflection shell | Resolution: 2→2.07 Å |
Reflection | *PLUS Num. measured all: 480222 |
Reflection shell | *PLUS Rmerge(I) obs: 0.138 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2HPD Resolution: 2→40 Å / Cross valid method: THROUGHOUT
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Refinement step | Cycle: LAST / Resolution: 2→40 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / % reflection Rfree: 5.2 % | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: p_angle_d / Dev ideal: 1.8 |