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- PDB-3q78: Cryptococcus neoformans protein farnesyltransferase in complex wi... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3q78 | ||||||
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Title | Cryptococcus neoformans protein farnesyltransferase in complex with FSPP and DDPTASACNIQ peptide | ||||||
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![]() | TRANSFERASE / Protein prenyltransferase | ||||||
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 | ![]() | 343.6 KB | Display | ![]() |
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PDB format | ![]() | 277.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 733.4 KB | Display | ![]() |
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Full document | ![]() | 746.7 KB | Display | |
Data in XML | ![]() | 34.2 KB | Display | |
Data in CIF | ![]() | 49 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3q73C ![]() 3q75C ![]() 3q79C ![]() 3q7aC ![]() 3q7fC ![]() 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.) ![]() ![]() ![]() |
-Protein/peptide , 1 types, 1 molecules D
#3: Protein/peptide | Mass: 1134.175 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: synthetic peptide substrate |
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-Non-polymers , 4 types, 348 molecules ![](data/chem/img/ZN.gif)
![](data/chem/img/3CX.gif)
![](data/chem/img/FPS.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/3CX.gif)
![](data/chem/img/FPS.gif)
![](data/chem/img/HOH.gif)
#4: Chemical | ChemComp-ZN / | ||||
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#5: Chemical | #6: Chemical | ChemComp-FPS / | #7: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.38 Å3/Da / Density % sol: 63.57 % |
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 9.5 Details: 15% PEG4K, 100mM CAPSO pH 9.5, 100 mm NaCl, 150 mM Lithium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Apr 18, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.971 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→50 Å / Num. obs: 65570 / % possible obs: 100 % / Observed criterion σ(I): -3 |
Reflection shell | Resolution: 2.2→2.27 Å / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 42.298 Å2 / ksol: 0.33 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.2→45.227 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: 28.9303 Å / Origin y: -32.2552 Å / Origin z: -3.0583 Å
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Refinement TLS group | Selection details: all |