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- PDB-4a54: Structural basis of the Dcp1:Dcp2 mRNA decapping complex activati... -
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Basic information
Entry | Database: PDB / ID: 4a54 | ||||||
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Title | Structural basis of the Dcp1:Dcp2 mRNA decapping complex activation by Edc3 and Scd6 | ||||||
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![]() | RNA BINDING PROTEIN/HYDROLASE / RNA BINDING PROTEIN-HYDROLASE COMPLEX | ||||||
Function / homology | ![]() : / RNA decapping complex / mRNA methylguanosine-cap decapping / 5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity / deadenylation-independent decapping of nuclear-transcribed mRNA / mRNA 5'-diphosphatase activity / 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity / Hydrolases / mRNA cap binding / deadenylation-dependent decapping of nuclear-transcribed mRNA ...: / RNA decapping complex / mRNA methylguanosine-cap decapping / 5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity / deadenylation-independent decapping of nuclear-transcribed mRNA / mRNA 5'-diphosphatase activity / 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity / Hydrolases / mRNA cap binding / deadenylation-dependent decapping of nuclear-transcribed mRNA / P-body assembly / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / molecular condensate scaffold activity / P-body / mRNA processing / cytoplasmic stress granule / manganese ion binding / single-stranded RNA binding / mRNA binding / magnesium ion binding / ATP binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / XPLOR | ||||||
![]() | Fromm, S.A. / Truffault, V. / Kamenz, J. / Braun, J.E. / Hoffmann, N.A. / Izaurralde, E. / Sprangers, R. | ||||||
![]() | ![]() Title: The Structural Basis of Edc3- and Scd6-Mediated Activation of the Dcp1:Dcp2 Mrna Decapping Complex. Authors: Fromm, S.A. / Truffault, V. / Kamenz, J. / Braun, J.E. / Hoffmann, N.A. / Izaurralde, E. / Sprangers, 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 | ![]() | 961.2 KB | Display | ![]() |
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PDB format | ![]() | 812.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 475.8 KB | Display | ![]() |
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Full document | ![]() | 731.8 KB | Display | |
Data in XML | ![]() | 64 KB | Display | |
Data in CIF | ![]() | 87.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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: 10601.993 Da / Num. of mol.: 1 / Fragment: LSM, RESIDUES 1-94 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
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#2: Protein | Mass: 5342.786 Da / Num. of mol.: 1 / Fragment: HLM1, RESIDUES 242-291 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: NOESY |
NMR details | Text: NONE |
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Sample preparation
Details | Contents: 90% WATER/10% D2O |
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Sample conditions | Ionic strength: 125 mM / pH: 7.3 / Pressure: 1.0 atm / Temperature: 303.0 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: XPLOR / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 50 / Conformers submitted total number: 22 |