[English] 日本語
![](img/lk-miru.gif)
- PDB-5izo: Bacillus NanoRNase A (H103A) + 2 divalent cations + PO4 at the ac... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 5izo | ||||||
---|---|---|---|---|---|---|---|
Title | Bacillus NanoRNase A (H103A) + 2 divalent cations + PO4 at the active site | ||||||
![]() | Bifunctional oligoribonuclease and PAP phosphatase NrnA | ||||||
![]() | HYDROLASE / nanoRNA / RNA degradation / exonuclease / RNase / B. subtilis / abortive transcripts / pAp phosphatase | ||||||
Function / homology | ![]() 3'(2'),5'-bisphosphate nucleotidase / 3'(2'),5'-bisphosphate nucleotidase activity / exonuclease activity / nucleic acid binding / Hydrolases; Acting on ester bonds Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Schmier, B.J. / Malhotra, A. / Nelersa, C.M. | ||||||
Funding support | ![]()
| ||||||
![]() | ![]() Title: Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA. Authors: Schmier, B.J. / Nelersa, C.M. / Malhotra, A. #1: Journal: Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. Year: 2011 Title: Purification and crystallization of Bacillus subtilis NrnA, a novel enzyme involved in nanoRNA degradation. Authors: Nelersa, C.M. / Schmier, B.J. / Malhotra, A. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 259.5 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 206.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 5ippC ![]() 5iufC ![]() 5j21SC C: citing same article ( S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
3 | ![]()
| ||||||||
4 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 37416.793 Da / Num. of mol.: 4 / Mutation: H103A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: 168 / Gene: nrnA, ytqI, BSU29250 / Plasmid: plasmid / Details (production host): pET28B-TEV / Production host: ![]() ![]() References: UniProt: O34600, Hydrolases; Acting on ester bonds, 3'(2'),5'-bisphosphate nucleotidase #2: Chemical | ChemComp-MN / #3: Chemical | ChemComp-PO4 / #4: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.51 Å3/Da / Density % sol: 51.04 % |
---|---|
Crystal grow | Temperature: 298.15 K / Method: vapor diffusion, hanging drop Details: PEG MME 2000, sodium acetate, ammonium acetate, glycerol PH range: 4.5-5.5 / Temp details: room temperature |
-Data collection
Diffraction | Mean temperature: 100 K / Ambient temp details: liquid nitrogen |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Apr 22, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97918 Å / Relative weight: 1 |
Reflection | Resolution: 1.95→47.34 Å / Num. obs: 106608 / % possible obs: 94.1 % / Redundancy: 3.4 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 17.44 |
Reflection shell | Resolution: 1.95→2.02 Å / Mean I/σ(I) obs: 2.18 / % possible all: 80 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: 5J21 Resolution: 1.95→47.34 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.931 / SU B: 5.259 / SU ML: 0.146 / Cross valid method: THROUGHOUT / ESU R: 0.186 / ESU R Free: 0.178 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 41.65 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.95→47.34 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|