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Open data
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Basic information
Entry | Database: PDB / ID: 5ee0 | ||||||
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Title | Crystal structure of OsYchF1 at pH 6.5 | ||||||
![]() | Obg-like ATPase 1 | ||||||
![]() | HYDROLASE / OSYCHF1 / GTP-BINDING PROTEIN / AMP-PNP / YCHF-TYPE / P-LOOP NTPASE / ATP-BINDING PROTEIN | ||||||
Function / homology | ![]() negative regulation of response to salt stress / negative regulation of defense response to bacterium / ribosomal large subunit binding / response to salt stress / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / GTPase activity / GTP binding / ATP hydrolysis activity / ATP binding / metal ion binding ...negative regulation of response to salt stress / negative regulation of defense response to bacterium / ribosomal large subunit binding / response to salt stress / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / GTPase activity / GTP binding / ATP hydrolysis activity / ATP binding / metal ion binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Li, X. / Chen, Z. | ||||||
![]() | ![]() Title: ATP binding by the P-loop NTPase OsYchF1 (an unconventional G protein) contributes to biotic but not abiotic stress responses Authors: Cheung, M.-Y. / Li, X. / Miao, R. / Fong, Y.-H. / Li, K.-P. / Yung, Y.-L. / Yu, M.-H. / Wong, K.-B. / Chen, Z. / Lam, H.-M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 159.4 KB | Display | ![]() |
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PDB format | ![]() | 124.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5ee1C ![]() 5ee3C ![]() 5ee9C ![]() 2ohfS 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: 44485.887 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: OS08G0199300, OSYCHF1 / Plasmid: PRSETA-HISSUMO / Production host: ![]() ![]() References: UniProt: Q6Z1J6, Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.72 Å3/Da / Density % sol: 54.84 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.5 / Details: PEG, 0.2M MGCL2, PH 6.5 |
-Data collection
Diffraction | Mean temperature: 130 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 270 / Detector: CCD / Date: May 11, 2013 |
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: 23625 / % possible obs: 97.3 % / Observed criterion σ(I): 3 / Redundancy: 4.8 % / Rmerge(I) obs: 0.077 / Rsym value: 0.052 / Net I/σ(I): 19 |
Reflection shell | Resolution: 2.21→2.25 Å / Rmerge(I) obs: 0.59 / % possible all: 99.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2OHF Resolution: 2.2→32.84 Å / Cor.coef. Fo:Fc: 0.907 / Cor.coef. Fo:Fc free: 0.9 / SU B: 11.723 / SU ML: 0.155 / Cross valid method: THROUGHOUT / σ(F): 3 / ESU R: 0.415 / ESU R Free: 0.261 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 38.21 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→32.84 Å
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Refine LS restraints |
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