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- PDB-3fsc: Crystal structure of QdtC, the dTDP-3-amino-3,6-dideoxy-D-glucose... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3fsc | ||||||
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Title | Crystal structure of QdtC, the dTDP-3-amino-3,6-dideoxy-D-glucose N-acetyl transferase from Thermoanaerobacterium thermosaccharolyticum in complex with CoA and dTDP-3-amino-fucose | ||||||
![]() | QdtC | ||||||
![]() | TRANSFERASE / N-acetyltransferase / deoxysugar / natural product | ||||||
Function / homology | ![]() Ubiquitin Ligase Nedd4; Chain: W; - #30 / Ubiquitin Ligase Nedd4; Chain: W; / : / Hexapeptide repeat of succinyl-transferase / Hexapeptide repeat proteins / UDP N-Acetylglucosamine Acyltransferase; domain 1 / Hexapeptide repeat / Other non-globular / Bacterial transferase hexapeptide (six repeats) / Trimeric LpxA-like superfamily ...Ubiquitin Ligase Nedd4; Chain: W; - #30 / Ubiquitin Ligase Nedd4; Chain: W; / : / Hexapeptide repeat of succinyl-transferase / Hexapeptide repeat proteins / UDP N-Acetylglucosamine Acyltransferase; domain 1 / Hexapeptide repeat / Other non-globular / Bacterial transferase hexapeptide (six repeats) / Trimeric LpxA-like superfamily / 3 Solenoid / Special / Mainly Beta Similarity search - Domain/homology | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Holden, H.M. / Thoden, J.B. | ||||||
![]() | ![]() Title: Structural and Functional Studies of QdtC: an N-Acetyltransferase Required for the Biosynthesis of dTDP-3-Acetamido-3,6-Dideoxy-alpha-D-Glucose. Authors: Thoden, J. / Cook, P. / Schaffer, C. / Messner, P. / Holden, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 131 KB | Display | ![]() |
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PDB format | ![]() | 99.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 3fs8SC ![]() 3fsbC 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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2 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 30816.162 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: E2707-71 / Gene: qdtC / Plasmid: pET31 / Production host: ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 47.92 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 24% PEG 5000, 0.1M HEPES, 0.01M AcetylCoA, 0.04M dTDP-3-aminofucose, 2% ethyleneglycol, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: Bruker Platinum 135 / Detector: CCD / Date: Aug 3, 2008 / Details: montel |
Radiation | Monochromator: Ni-filter / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→30 Å / Num. all: 50462 / Num. obs: 50462 / % possible obs: 95.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Rsym value: 0.072 |
Reflection shell | Resolution: 1.8→1.9 Å / Redundancy: 1.5 % / Mean I/σ(I) obs: 2.7 / Num. unique all: 6644 / Rsym value: 0.273 / % possible all: 82.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 3fs8 Resolution: 1.8→30 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.8→30 Å
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