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Yorodumi- PDB-1s59: Structure of nucleoside diphosphate kinase 2 with bound dGTP from... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1s59 | ||||||
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Title | Structure of nucleoside diphosphate kinase 2 with bound dGTP from Arabidopsis | ||||||
Components | Nucleoside diphosphate kinase IINucleoside-diphosphate kinase | ||||||
Keywords | TRANSFERASE / kinase | ||||||
Function / homology | Function and homology information red, far-red light phototransduction / auxin-activated signaling pathway / thylakoid / nucleoside-diphosphate kinase / chloroplast envelope / CTP biosynthetic process / UTP biosynthetic process / GTP biosynthetic process / nucleoside diphosphate kinase activity / plastid ...red, far-red light phototransduction / auxin-activated signaling pathway / thylakoid / nucleoside-diphosphate kinase / chloroplast envelope / CTP biosynthetic process / UTP biosynthetic process / GTP biosynthetic process / nucleoside diphosphate kinase activity / plastid / chloroplast stroma / response to UV / chloroplast / response to hydrogen peroxide / phosphorylation / ATP binding / metal ion binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Arabidopsis thaliana (thale cress) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å | ||||||
Authors | Im, Y.J. / Kim, J.-I. / Shen, Y. / Na, Y. / Han, Y.-J. / Kim, S.-H. / Song, P.-S. / Eom, S.H. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2004 Title: Structural analysis of Arabidopsis thaliana nucleoside diphosphate kinase-2 for phytochrome-mediated light signaling Authors: Im, Y.J. / Kim, J.-I. / Shen, Y. / Na, Y. / Han, Y.-J. / Kim, S.-H. / Song, P.-S. / Eom, S.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1s59.cif.gz | 186.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1s59.ent.gz | 149.8 KB | Display | PDB format |
PDBx/mmJSON format | 1s59.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/s5/1s59 ftp://data.pdbj.org/pub/pdb/validation_reports/s5/1s59 | HTTPS FTP |
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-Related structure data
Related structure data | 1s57SC 1u8wC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 17081.633 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: NDPK2 / Plasmid: pGEX-4T-1 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: O64903, nucleoside-diphosphate kinase #2: Chemical | ChemComp-DGI / | #3: Chemical | ChemComp-DGT / | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.14 Å3/Da / Density % sol: 42.14 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: Ammonium Sulfate, dGTP, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: PAL/PLS / Beamline: 6B / Wavelength: 1.127 Å |
Detector | Type: MAC Science DIP-2030B / Detector: IMAGE PLATE / Date: Oct 22, 2003 / Details: mirrors |
Radiation | Monochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.127 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→50 Å / Num. all: 27836 / Num. obs: 27023 / % possible obs: 95.9 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 3 / Redundancy: 5.5 % / Biso Wilson estimate: 36.4 Å2 / Rmerge(I) obs: 0.123 / Rsym value: 0.123 / Net I/σ(I): 15.4 |
Reflection shell | Resolution: 2.6→2.69 Å / Redundancy: 5.1 % / Rmerge(I) obs: 0.394 / Mean I/σ(I) obs: 3.8 / Num. unique all: 2529 / Rsym value: 0.394 / % possible all: 91.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1S57 Resolution: 2.6→34.6 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 1864833.98 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 2 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 14.5654 Å2 / ksol: 0.370344 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 19.6 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.6→34.6 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.6→2.76 Å / Rfactor Rfree error: 0.026 / Total num. of bins used: 6
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Xplor file |
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