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Yorodumi- PDB-1weo: Solution structure of RING-finger in the catalytic subunit (IRX3)... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1weo | ||||||
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Title | Solution structure of RING-finger in the catalytic subunit (IRX3) of cellulose synthase | ||||||
Components | cellulose synthase, catalytic subunit (IRX3) | ||||||
Keywords | DNA BINDING PROTEIN / structure genomics / RING-finger / cellulose synthase / catalytic subunit(IRX3) / RIKEN Structural Genomics/Proteomics Initiative / RSGI / Structural Genomics | ||||||
Function / homology | Function and homology information cellulose synthase complex / rhamnogalacturonan I side chain metabolic process / plant-type cell wall biogenesis / plant-type secondary cell wall biogenesis / cellulose synthase activity / plant-type primary cell wall biogenesis / cellulose synthase (UDP-forming) / cellulose synthase (UDP-forming) activity / cellulose biosynthetic process / chloroplast ...cellulose synthase complex / rhamnogalacturonan I side chain metabolic process / plant-type cell wall biogenesis / plant-type secondary cell wall biogenesis / cellulose synthase activity / plant-type primary cell wall biogenesis / cellulose synthase (UDP-forming) / cellulose synthase (UDP-forming) activity / cellulose biosynthetic process / chloroplast / trans-Golgi network / membrane => GO:0016020 / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | Arabidopsis thaliana (thale cress) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | He, F. / Muto, Y. / Inoue, M. / Kigawa, T. / Shirouzu, M. / Terada, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of RING-finger in the catalytic subunit (IRX3) of cellulose synthase Authors: He, F. / Muto, Y. / Inoue, M. / Kigawa, T. / Shirouzu, M. / Terada, T. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1weo.cif.gz | 527.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1weo.ent.gz | 439.4 KB | Display | PDB format |
PDBx/mmJSON format | 1weo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1weo_validation.pdf.gz | 342.1 KB | Display | wwPDB validaton report |
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Full document | 1weo_full_validation.pdf.gz | 477.6 KB | Display | |
Data in XML | 1weo_validation.xml.gz | 32.9 KB | Display | |
Data in CIF | 1weo_validation.cif.gz | 51.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/we/1weo ftp://data.pdbj.org/pub/pdb/validation_reports/we/1weo | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 10109.072 Da / Num. of mol.: 1 / Fragment: RING-finger Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Description: Cell free protein synthesis / Gene: RAFL09-35-F05 / Plasmid: P030224-84 / References: UniProt: Q9SWW6 |
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#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.8mM U-15,13C; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 0.1mM ZnCl2; 1mM d-DTT; 0.02% NaN3; 90%H2O, 10%D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 7 / Pressure: ambient / Temperature: 293 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations, structures with the lowest energy, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |