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- PDB-2o1o: Cryptosporidium parvum putative polyprenyl pyrophosphate synthase... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2o1o | ||||||
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Title | Cryptosporidium parvum putative polyprenyl pyrophosphate synthase (cgd4_2550) in complex with risedronate. | ||||||
![]() | Putative farnesyl pyrophosphate synthase | ||||||
![]() | STRUCTURAL GENOMICS / UNKNOWN FUNCTION / putative polyprenyl pyrophosphate synthase / Structural Genomics Consortium / SGC | ||||||
Function / homology | ![]() farnesyl diphosphate biosynthetic process / dimethylallyltranstransferase activity / geranyltranstransferase activity / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Chruszcz, M. / Artz, J.D. / Dong, A. / Dunford, J. / Lew, J. / Zhao, Y. / Kozieradski, I. / Kavanaugh, K.L. / Oppermann, U. / Sundstrom, M. ...Chruszcz, M. / Artz, J.D. / Dong, A. / Dunford, J. / Lew, J. / Zhao, Y. / Kozieradski, I. / Kavanaugh, K.L. / Oppermann, U. / Sundstrom, M. / Weigelt, J. / Edwards, A.M. / Arrowsmith, C.H. / Bochkarev, A. / Hui, R. / Minor, W. / Structural Genomics Consortium (SGC) | ||||||
![]() | ![]() Title: Targeting a uniquely nonspecific prenyl synthase with bisphosphonates to combat cryptosporidiosis Authors: Artz, J.D. / Dunford, J.E. / Arrowood, M.J. / Dong, A. / Chruszcz, M. / Kavanagh, K.L. / Minor, W. / Russell, R.G. / Ebetino, F.H. / Oppermann, U. / Hui, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 148.3 KB | Display | ![]() |
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PDB format | ![]() | 114.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 27.9 KB | Display | |
Data in CIF | ![]() | 37.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2q58C ![]() 2her C: citing same article ( S: Starting model for refinement |
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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
#1: Protein | Mass: 42973.051 Da / Num. of mol.: 2 / Fragment: residues 38-384 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-MG / #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.62 Å3/Da / Density % sol: 53.04 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 1.6 M ammonium sulfate, 10 mM MgCl2, and 100 mM HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: May 5, 2006 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 2.42→50 Å / Num. all: 64868 / Num. obs: 32655 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 5 % / Rmerge(I) obs: 0.066 / Rsym value: 0.046 / Net I/σ(I): 29.7 |
Reflection shell | Resolution: 2.42→2.53 Å / Redundancy: 5.2 % / Rmerge(I) obs: 0.464 / Mean I/σ(I) obs: 3.4 / Num. unique all: 4061 / Rsym value: 0.49 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 2HER ![]() 2her Resolution: 2.42→50 Å / Num. parameters: 21516 / Num. restraintsaints: 21967 / Cross valid method: FREE R / σ(F): 0 / σ(I): 0 / Stereochemistry target values: ENGH AND HUBER Details: SHELXL-97, RESOLVE, and COOT were used for refinement.
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Solvent computation | Solvent model: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-228 | |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 0 / Occupancy sum hydrogen: 0 / Occupancy sum non hydrogen: 5378 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.42→50 Å
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Refine LS restraints |
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