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- PDB-4a6n: STRUCTURE OF THE TETRACYCLINE DEGRADING MONOOXYGENASE TETX IN COM... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4a6n | ||||||
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Title | STRUCTURE OF THE TETRACYCLINE DEGRADING MONOOXYGENASE TETX IN COMPLEX WITH TIGECYCLINE | ||||||
![]() | (TETX2 PROTEIN) x 2 | ||||||
![]() | OXIDOREDUCTASE / ANTIBIOTIC RESISTANCE | ||||||
Function / homology | ![]() tetracycline 11a-monooxygenase / monooxygenase activity / FAD binding / response to antibiotic / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Volkers, G. / Palm, G.J. / Weiss, M.S. / Hinrichs, W. | ||||||
![]() | ![]() Title: Putative Dioxygen-Binding Sites and Recognition of Tigecycline and Minocycline in the Tetracycline-Degrading Monooxygenase Tetx Authors: Volkers, G. / Damas, J.M. / Palm, G.J. / Panjikar, S. / Soares, C.M. / Hinrichs, W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 597.5 KB | Display | ![]() |
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PDB format | ![]() | 496.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.4 MB | Display | ![]() |
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Full document | ![]() | 2.4 MB | Display | |
Data in XML | ![]() | 60.1 KB | Display | |
Data in CIF | ![]() | 78.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4a99C ![]() 4guvC ![]() 2xdoS 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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2 | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS oper:
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Components
-Protein , 2 types, 4 molecules ABCD
#1: Protein | Mass: 44703.461 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() ![]() |
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#2: Protein | Mass: 44703.395 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() ![]() |
-Non-polymers , 4 types, 229 molecules ![](data/chem/img/FAD.gif)
![](data/chem/img/T1C.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/T1C.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-FAD / #4: Chemical | ChemComp-T1C / #5: Chemical | ChemComp-SO4 / #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.44 Å3/Da / Density % sol: 49.6 % / Description: NONE |
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Crystal grow | pH: 7 / Details: pH 7 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Apr 28, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91841 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→81.897 Å / Num. obs: 75167 / % possible obs: 96 % / Redundancy: 3.9 % / Rmerge(I) obs: 0.088 / Net I/σ(I): 9.1 |
Reflection shell | Resolution: 2.3→2.42 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.622 / Mean I/σ(I) obs: 2 / % possible all: 95.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2XDO Resolution: 2.3→81.9 Å / Cor.coef. Fo:Fc: 0.939 / Cor.coef. Fo:Fc free: 0.913 / SU B: 15.307 / SU ML: 0.202 / Cross valid method: THROUGHOUT / ESU R: 0.377 / ESU R Free: 0.255 / 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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 61.598 Å2
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Refinement step | Cycle: LAST / Resolution: 2.3→81.9 Å
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Refine LS restraints |
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