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- PDB-3q7f: Cryptococcus neoformans protein farnesyltransferase in complex wi... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3q7f | |||||||||
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Title | Cryptococcus neoformans protein farnesyltransferase in complex with FPP and ethylenediamine inhibitor 1 | |||||||||
![]() | (Farnesyltransferase ...) x 2 | |||||||||
![]() | TRANSFERASE/TRANSFERASE INHIBITOR / protein prenyltransferase / TRANSFERASE-TRANSFERASE INHIBITOR complex | |||||||||
Function / homology | ![]() protein prenyltransferase activity / protein farnesyltransferase / protein farnesyltransferase activity / protein farnesyltransferase complex / zinc ion binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Hast, M.A. / Beese, L.S. | |||||||||
![]() | ![]() Title: Structures of Cryptococcus neoformans Protein Farnesyltransferase Reveal Strategies for Developing Inhibitors That Target Fungal Pathogens. Authors: Hast, M.A. / Nichols, C.B. / Armstrong, S.M. / Kelly, S.M. / Hellinga, H.W. / Alspaugh, J.A. / Beese, L.S. | |||||||||
History |
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Remark 999 | There is no UniPort database reference sequence available at the time of the deposition. The ...There is no UniPort database reference sequence available at the time of the deposition. The sequences presented here are of farnesyltransferase alpha subunit(residues 15-349) and beta subunit from Cryptococcus neoformans var. grubii strain H99. The first 14 residues in the alpha subunit(chain A) represent expression tag. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 338 KB | Display | ![]() |
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PDB format | ![]() | 271.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.3 MB | Display | ![]() |
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Full document | ![]() | 2.3 MB | Display | |
Data in XML | ![]() | 36.5 KB | Display | |
Data in CIF | ![]() | 53.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3q73C ![]() 3q75C ![]() 3q78C ![]() 3q79C ![]() 3q7aC ![]() 3sfxC ![]() 3sfyC 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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Unit cell |
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Components
-Farnesyltransferase ... , 2 types, 2 molecules AB
#1: Protein | Mass: 40913.234 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 56806.879 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
-Sugars , 1 types, 3 molecules
#3: Polysaccharide |
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-Non-polymers , 6 types, 495 molecules ![](data/chem/img/ZN.gif)
![](data/chem/img/3CX.gif)
![](data/chem/img/FPP.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/ED2.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/3CX.gif)
![](data/chem/img/FPP.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/ED2.gif)
![](data/chem/img/HOH.gif)
#4: Chemical | ChemComp-ZN / | ||||||||
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#5: Chemical | #6: Chemical | ChemComp-FPP / | #7: Chemical | ChemComp-SO4 / | #8: Chemical | ChemComp-ED2 / | #9: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.45 Å3/Da / Density % sol: 64.32 % |
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 9.5 Details: 15% PEG 4K, 100mM CAPSO pH 9.5, 100mM NaCl, 150mM Lithium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jun 29, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→50 Å / Num. obs: 65610 / % possible obs: 99.1 % / Observed criterion σ(I): -3 |
Reflection shell | Resolution: 2.2→2.257 Å / % possible all: 94.5 |
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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: 38.037 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→44.94 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.257 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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