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- PDB-2f6i: Crystal structure of the ClpP protease catalytic domain from Plas... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2f6i | ||||||
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Title | Crystal structure of the ClpP protease catalytic domain from Plasmodium falciparum | ||||||
![]() | ATP-dependent CLP protease, putative | ||||||
![]() | HYDROLASE / Clp protease / structural genomics / Structural Genomics Consortium / SGC | ||||||
Function / homology | ![]() apicoplast / endopeptidase Clp complex / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / ATPase binding / hydrolase activity / serine-type endopeptidase activity / proteolysis Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Mulichak, A. / Loppnau, P. / Bray, J. / Amani, M. / Vedadi, M. / Wasney, G. / Finerty, P. / Sundstrom, M. / Weigelt, J. / Edwards, A. ...Mulichak, A. / Loppnau, P. / Bray, J. / Amani, M. / Vedadi, M. / Wasney, G. / Finerty, P. / Sundstrom, M. / Weigelt, J. / Edwards, A. / Arrowsmith, C. / Hui, R. / Plotnikova, O. / Structural Genomics Consortium (SGC) | ||||||
![]() | ![]() Title: The Clp chaperones and proteases of the human malaria parasite Plasmodium falciparum. Authors: El Bakkouri, M. / Pow, A. / Mulichak, A. / Cheung, K.L. / Artz, J.D. / Amani, M. / Fell, S. / de Koning-Ward, T.F. / Goodman, C.D. / McFadden, G.I. / Ortega, J. / Hui, R. / Houry, W.A. #1: ![]() Title: Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms. Authors: Vedadi, M. / Lew, J. / Artz, J. / Amani, M. / Zhao, Y. / Dong, A. / Wasney, G.A. / Gao, M. / Hills, T. / Brokx, S. / Qiu, W. / Sharma, S. / Diassiti, A. / Alam, Z. / Melone, M. / Mulichak, A. ...Authors: Vedadi, M. / Lew, J. / Artz, J. / Amani, M. / Zhao, Y. / Dong, A. / Wasney, G.A. / Gao, M. / Hills, T. / Brokx, S. / Qiu, W. / Sharma, S. / Diassiti, A. / Alam, Z. / Melone, M. / Mulichak, A. / Wernimont, A. / Bray, J. / Loppnau, P. / Plotnikova, O. / Newberry, K. / Sundararajan, E. / Houston, S. / Walker, J. / Tempel, W. / Bochkarev, A. / Kozieradzki, I. / Edwards, A. / Arrowsmith, C. / Roos, D. / Kain, K. / 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 | ![]() | 258.1 KB | Display | ![]() |
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PDB format | ![]() | 207.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 500 KB | Display | ![]() |
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Full document | ![]() | 532.8 KB | Display | |
Data in XML | ![]() | 48.8 KB | Display | |
Data in CIF | ![]() | 67 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1tyfS 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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1 | ![]()
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Unit cell |
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Details | The biological assembly is a tetradecamer generated from the heptamer in the asymmetric unit by the operation: -X, Y, -Z+1/2 |
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Components
#1: Protein | Mass: 24870.557 Da / Num. of mol.: 7 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: pET-28a vector customized for thrombin cleavage and LIC Production host: ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.11 Å3/Da / Density % sol: 60.43 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: PEG MME 550, Ammonium sulfate, cacodylate buffer., pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Sep 17, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 2.45→50 Å / Num. all: 78895 / Num. obs: 78895 / % possible obs: 99.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7.5 % / Rsym value: 0.078 |
Reflection shell | Resolution: 2.45→2.54 Å / Redundancy: 4.5 % / Num. unique all: 7777 / Rsym value: 0.316 / % possible all: 98.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 1TYF Resolution: 2.45→30 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber Details: The following loops are unobserved and omitted from the model: Chain A 297-304, Chain B 290-304, Chain C 298-303, Chain D 297-303, Chain E 297-304, Chain F 292-303. Side chain atoms of ...Details: The following loops are unobserved and omitted from the model: Chain A 297-304, Chain B 290-304, Chain C 298-303, Chain D 297-303, Chain E 297-304, Chain F 292-303. Side chain atoms of residues listed in Remark 470 are unobserved in electron density maps and are omitted from model.
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Refine analyze | Luzzati coordinate error obs: 0.34 Å / Luzzati d res low obs: 5 Å / Luzzati sigma a obs: 0.39 Å | ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.45→30 Å
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Refine LS restraints |
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