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- PDB-2e29: Solution structure of the GUCT domain from human ATP-dependent RN... -
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Basic information
Entry | Database: PDB / ID: 2.0E+29 | ||||||
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Title | Solution structure of the GUCT domain from human ATP-dependent RNA helicase DDX50, DEAD box protein 50 | ||||||
![]() | ATP-dependent RNA helicase DDX50 | ||||||
![]() | HYDROLASE / ATP binding / Helicase / Nuclear protein / Nucleotide-binding / RNA-binding / GUCT domain / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | ![]() RNA helicase activity / RNA helicase / nucleolus / RNA binding / ATP binding / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics, restrained molecular dynamics | ||||||
![]() | Ohnishi, S. / Paakkonen, K. / Guntert, P. / Sato, M. / Koshiba, S. / Harada, T. / Watanabe, S. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
![]() | ![]() Title: Solution structure of the GUCT domain from human RNA helicase II/Gubeta reveals the RRM fold, but implausible RNA interactions Authors: Ohnishi, S. / Paakkonen, K. / Koshiba, S. / Tochio, N. / Sato, M. / Kobayashi, N. / Harada, T. / Watanabe, S. / Muto, Y. / Guntert, P. / Tanaka, A. / Kigawa, T. / Yokoyama, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 541.7 KB | Display | ![]() |
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PDB format | ![]() | 455.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 355.2 KB | Display | ![]() |
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Full document | ![]() | 452.8 KB | Display | |
Data in XML | ![]() | 25.1 KB | Display | |
Data in CIF | ![]() | 45.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 10149.377 Da / Num. of mol.: 1 / Fragment: GUCT domain, residues 8-92 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() References: UniProt: Q9BQ39, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 0.9mM protein U-15N,13C; 20mM d-Tris-HCl(pH7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O, 90% H2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 7.0 / Pressure: ambient / Temperature: 296 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics, restrained molecular dynamics Software ordinal: 1 Details: HNN and CACO RDC data, obtained from the Pf1 phage system, were used in the torsion angle dynamics calculation. | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |