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- PDB-3zsn: Structure of the mixed-function P450 MycG F286A mutant in complex... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3zsn | ||||||
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Title | Structure of the mixed-function P450 MycG F286A mutant in complex with mycinamicin IV | ||||||
![]() | P-450-LIKE PROTEIN | ||||||
![]() | OXIDOREDUCTASE / MYCINAMICIN BIOSYNTHESIS | ||||||
Function / homology | ![]() Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen / cholest-4-en-3-one 26-monooxygenase activity / antibiotic biosynthetic process / steroid hydroxylase activity / cholesterol catabolic process / monooxygenase activity / iron ion binding / heme binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Li, S. / Kells, P.M. / Rutaganira, F.U. / Anzai, Y. / Kato, F. / Sherman, D.H. / Podust, L.M. | ||||||
![]() | ![]() Title: Substrate Recognition by the Multifunctional Cytochrome P450 Mycg in Mycinamicin Hydroxylation and Epoxidation Reactions. Authors: Li, S. / Tietz, D.R. / Rutaganira, F.U. / Kells, P.M. / Anzai, Y. / Kato, F. / Pochapsky, T.C. / Sherman, D.H. / Podust, L.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 276.6 KB | Display | ![]() |
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PDB format | ![]() | 222.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2 MB | Display | ![]() |
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Full document | ![]() | 2.1 MB | Display | |
Data in XML | ![]() | 58.8 KB | Display | |
Data in CIF | ![]() | 84.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2y46C ![]() 2y5nC ![]() 2y5zC ![]() 2y98C ![]() 2ycaC ![]() 2ygxC ![]() 4aw3C ![]() 2y4h 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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3 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
-Protein , 1 types, 3 molecules ABC
#1: Protein | Mass: 46480.668 Da / Num. of mol.: 3 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Non-polymers , 5 types, 1038 molecules ![](data/chem/img/HEM.gif)
![](data/chem/img/MIV.gif)
![](data/chem/img/BEN.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/MIV.gif)
![](data/chem/img/BEN.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | #3: Chemical | #4: Chemical | ChemComp-BEN / #5: Chemical | ChemComp-GOL / #6: Water | ChemComp-HOH / | |
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-Details
Compound details | ENGINEERED RESIDUE IN CHAIN A, PHE 286 TO ALA ENGINEERED RESIDUE IN CHAIN B, PHE 286 TO ALA ...ENGINEERED |
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Nonpolymer details | PROTOPORPHYRIN IX (HEM): HEME THIOLATE BOND TO CYS 346 BENZAMIDINE (BEN): ADDITIVE MYCINAMICIN IV ...PROTOPORPH |
Sequence details | THE 6XHIS TAG AND THROMBIN CLEAVAGE SITE ARE ENGINEERED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48.9 % / Description: NONE |
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Crystal grow | pH: 5 Details: 2.5% PEG 1500; 0.1 M SODIUM MALONATE, PH 5.0; 2% BENZAMIDINE. |
-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: May 28, 2011 / Details: MIRRORS |
Radiation | Monochromator: SI (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.11587 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→146.95 Å / Num. obs: 91500 / % possible obs: 89.2 % / Observed criterion σ(I): 1.5 / Redundancy: 5.4 % / Biso Wilson estimate: 24.4 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 10.9 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.56 / Mean I/σ(I) obs: 1.7 / % possible all: 64.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2Y4H ![]() 2y4h Resolution: 1.9→220.42 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.923 / SU B: 3.753 / SU ML: 0.109 / Cross valid method: THROUGHOUT / ESU R: 0.185 / ESU R Free: 0.174 / 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: 24.422 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→220.42 Å
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Refine LS restraints |
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