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- PDB-7o1j: Structure of Mycobacterium tuberculosis beta-oxidation trifunctio... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7o1j | ||||||||||||
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Title | Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme beta-C92A mutant | ||||||||||||
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![]() | OXIDOREDUCTASE / trifunctional enzyme / fatty acid beta oxidation / mycobacterium tuberculosis | ||||||||||||
Function / homology | ![]() long-chain-3-hydroxyacyl-CoA dehydrogenase activity / enoyl-CoA hydratase activity / acyltransferase activity, transferring groups other than amino-acyl groups / fatty acid beta-oxidation / NAD+ binding / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / peptidoglycan-based cell wall / plasma membrane / cytosol Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Dalwani, S. / Wierenga, R.K. / Venkatesan, R. | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Substrate specificity and conformational flexibility properties of the Mycobacterium tuberculosis beta-oxidation trifunctional enzyme. Authors: Dalwani, S. / Lampela, O. / Leprovost, P. / Schmitz, W. / Juffer, A.H. / Wierenga, R.K. / Venkatesan, R. #1: ![]() Title: Structure of Mycobacterial Beta-Oxidation Trifunctional Enzyme Reveals its Altered Assembly and Putative Substrate Channeling Pathway Authors: Venkatesan, R. / Wierenga, R.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 | ![]() | 514 KB | Display | ![]() |
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PDB format | ![]() | 351.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 280.3 KB | Display | ![]() |
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Full document | ![]() | 285 KB | Display | |
Data in XML | ![]() | 21.5 KB | Display | |
Data in CIF | ![]() | 34.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7o1gC ![]() 7o1iC ![]() 7o1kC ![]() 7o1lC ![]() 7o1mC ![]() 7o4qC ![]() 7o4rC ![]() 7o4sC ![]() 7o4tC ![]() 7o4uC ![]() 7o4vC ![]() 4b3hS 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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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 42444.289 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: fadA, Rv0859 / Production host: ![]() ![]() References: UniProt: O53871, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups | ||||||
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#2: Protein | Mass: 78005.805 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: fadB, Rv0860 / Production host: ![]() ![]() References: UniProt: O53872, 3-hydroxyacyl-CoA dehydrogenase | ||||||
#3: Chemical | #4: Chemical | ChemComp-SO4 / #5: Water | ChemComp-HOH / | Has ligand of interest | N | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.94 Å3/Da / Density % sol: 58.3 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion / pH: 7.5 / Details: 2 M Ammonium Sulfate, 0.1M Tea pH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Sep 27, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.966 Å / Relative weight: 1 |
Reflection | Resolution: 2.36→66.73 Å / Num. obs: 58404 / % possible obs: 99.7 % / Redundancy: 4.3 % / Biso Wilson estimate: 45.43 Å2 / CC1/2: 0.996 / Net I/σ(I): 8 |
Reflection shell | Resolution: 2.36→2.42 Å / Num. unique obs: 4525 / CC1/2: 0.588 / % possible all: 99.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4B3H Resolution: 2.36→66.73 Å / SU ML: 0.3161 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 28.9623 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 66.91 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.36→66.73 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: -31.8304317201 Å / Origin y: 26.0505947014 Å / Origin z: -8.54851237867 Å
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Refinement TLS group | Selection details: all |