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Open data
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Basic information
Entry | Database: PDB / ID: 6vcp | ||||||
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Title | Crystal structure of E.coli RppH in complex with UTP | ||||||
![]() | RNA pyrophosphohydrolase | ||||||
![]() | RNA BINDING PROTEIN / RNA degradation | ||||||
Function / homology | ![]() RNA NAD-cap (NMN-forming) hydrolase activity / RNA decapping / RNA destabilization / NAD-cap decapping / mRNA 5'-diphosphatase activity / deadenylation-dependent decapping of nuclear-transcribed mRNA / hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides / tRNA processing / mRNA catabolic process / Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides ...RNA NAD-cap (NMN-forming) hydrolase activity / RNA decapping / RNA destabilization / NAD-cap decapping / mRNA 5'-diphosphatase activity / deadenylation-dependent decapping of nuclear-transcribed mRNA / hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides / tRNA processing / mRNA catabolic process / Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides / P-body / magnesium ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Gao, A. / Vasilyev, N. / Kaushik, A. / Duan, W. / Serganov, A. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Principles of RNA and nucleotide discrimination by the RNA processing enzyme RppH. Authors: Gao, A. / Vasilyev, N. / Kaushik, A. / Duan, W. / Serganov, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 54.3 KB | Display | ![]() |
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PDB format | ![]() | 35.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 390.3 KB | Display | ![]() |
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Full document | ![]() | 390.5 KB | Display | |
Data in XML | ![]() | 1.5 KB | Display | |
Data in CIF | ![]() | 4.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6vckC ![]() 6vclC ![]() 6vcmC ![]() 6vcnC ![]() 6vcoC ![]() 6vcqC ![]() 6vcrC ![]() 4s2yS 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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1 |
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Unit cell |
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Components
#1: Protein | Mass: 18965.773 Da / Num. of mol.: 1 / Mutation: Q159A, E160A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P0A776, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides | ||||
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#2: Chemical | #3: Water | ChemComp-HOH / | Has ligand of interest | Y | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 47.96 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, hanging drop Details: 0.4 M (NH4)2SO4, 10% (v/v) PEG3350, 10% (v/v) glycerol |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Sep 19, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→19.37 Å / Num. obs: 19245 / % possible obs: 99.2 % / Redundancy: 3.9 % / Biso Wilson estimate: 19.41 Å2 / CC1/2: 0.99 / Net I/σ(I): 15.6 |
Reflection shell | Resolution: 1.7→1.76 Å / Num. unique obs: 1896 / CC1/2: 0.77 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4S2Y Resolution: 1.7→19.37 Å / SU ML: 0.1638 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 23.6711
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 25.47 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→19.37 Å
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Refine LS restraints |
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LS refinement shell |
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