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- PDB-3tqe: Structure of the malonyl CoA-acyl carrier protein transacylase (f... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3tqe | ||||||
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Title | Structure of the malonyl CoA-acyl carrier protein transacylase (fabD) from Coxiella burnetii | ||||||
![]() | Malonyl-CoA-[acyl-carrier-protein] transacylase | ||||||
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Function / homology | ![]() [acyl-carrier-protein] S-malonyltransferase / [acyl-carrier-protein] S-malonyltransferase activity / fatty acid biosynthetic process / ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Franklin, M.C. / Cheung, J. / Rudolph, M. / Cassidy, M. / Gary, E. / Burshteyn, F. / Love, J. | ||||||
![]() | ![]() Title: Structural genomics for drug design against the pathogen Coxiella burnetii. Authors: Franklin, M.C. / Cheung, J. / Rudolph, M.J. / Burshteyn, F. / Cassidy, M. / Gary, E. / Hillerich, B. / Yao, Z.K. / Carlier, P.R. / Totrov, M. / Love, J.D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 148 KB | Display | ![]() |
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PDB format | ![]() | 123.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 3tq8C ![]() 3tq9C ![]() 3tqaC ![]() 3tqbC ![]() 3tqcC ![]() 3tqdC ![]() 3tqfC ![]() 3tqgC ![]() 3tqhC ![]() 3tqiC ![]() 3tqjC ![]() 3tqlC ![]() 3tqmC ![]() 3tqnC ![]() 3tqoC ![]() 3tqpC ![]() 3tqqC ![]() 3tqrC ![]() 3tqsC ![]() 3tqtC ![]() 3tquC ![]() 3tqwC ![]() 3tqxC ![]() 3tqyC ![]() 3tqzC ![]() 3tr0C ![]() 3tr1C ![]() 3tr2C ![]() 3tr3C ![]() 3tr4C ![]() 3tr5C ![]() 3tr6C ![]() 3tr7C ![]() 3tr8C ![]() 3tr9C ![]() 3trbC ![]() 3trcC ![]() 3trdC ![]() 3treC ![]() 3trfC ![]() 3trgC ![]() 3trhC ![]() 3triC ![]() 3tthC ![]() 3ty2C ![]() 3uwcC ![]() 4f3qC ![]() 4f3rC ![]() 4nbqC ![]() 4ng4C 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: 34747.719 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() References: UniProt: Q83E39, [acyl-carrier-protein] S-malonyltransferase | ||||
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#2: Chemical | ![]() #3: Chemical | ChemComp-EDO / | ![]() #4: Water | ChemComp-HOH / | ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.33 Å3/Da / Density % sol: 63.07 % |
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Crystal grow![]() | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 10.5 Details: 0.2 M Li sulfate, 0.1 M glycine, 1.2 M NaH2PO4, 0.8 M K2HPO4, pH 10.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Feb 24, 2011 |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.5→100 Å / Num. all: 72753 / Num. obs: 72582 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 8 % / Rsym value: 0.076 / Net I/σ(I): 44.5 |
Reflection shell | Resolution: 1.5→1.53 Å / Redundancy: 4.7 % / Mean I/σ(I) obs: 3.1 / Num. unique all: 3642 / Rsym value: 0.385 / % possible all: 96.8 |
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Processing
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Refinement | Method to determine structure![]() ![]()
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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: 15.958 Å2
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Refinement step | Cycle: LAST / Resolution: 1.5→85.66 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.5→1.54 Å / Total num. of bins used: 20
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