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Yorodumi- PDB-1oys: Crystal Structure of the Phosphorolytic Exoribonuclease RNase PH ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1oys | ||||||
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Title | Crystal Structure of the Phosphorolytic Exoribonuclease RNase PH from Bacillus subtilis | ||||||
Components | Ribonuclease PH | ||||||
Keywords | TRANSFERASE / tRNA processing | ||||||
Function / homology | Function and homology information tRNA nucleotidyltransferase / tRNA nucleotidyltransferase activity / rRNA 3'-end processing / cytoplasmic exosome (RNase complex) / U4 snRNA 3'-end processing / poly(A)-dependent snoRNA 3'-end processing / : / rRNA catabolic process / tRNA processing / 3'-5'-RNA exonuclease activity / tRNA binding Similarity search - Function | ||||||
Biological species | Bacillus subtilis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Harlow, L.S. / Kadziola, A. / Jensen, K.F. / Larsen, S. | ||||||
Citation | Journal: Protein Sci. / Year: 2004 Title: Crystal structure of the phosphorolytic exoribonuclease RNase PH from Bacillus subtilis and implications for its quaternary structure and tRNA binding. Authors: Harlow, L.S. / Kadziola, A. / Jensen, K.F. / Larsen, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1oys.cif.gz | 49.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1oys.ent.gz | 36.7 KB | Display | PDB format |
PDBx/mmJSON format | 1oys.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oy/1oys ftp://data.pdbj.org/pub/pdb/validation_reports/oy/1oys | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 26626.244 Da / Num. of mol.: 1 / Mutation: R68Q,R73Q,R76Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus subtilis (bacteria) / Gene: RPH / Production host: Escherichia coli (E. coli) / References: UniProt: P28619, tRNA nucleotidyltransferase |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 4.47 Å3/Da / Density % sol: 72.29 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 6.2 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.4→20 Å / Num. obs: 16768 |
Reflection | *PLUS Lowest resolution: 20 Å / % possible obs: 98.8 % / Redundancy: 4.4 % / Rmerge(I) obs: 0.047 |
Reflection shell | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 2.44 Å / % possible obs: 100 % / Redundancy: 5.5 % / Num. unique obs: 817 / Rmerge(I) obs: 0.206 / Mean I/σ(I) obs: 7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.4→20 Å / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2.4→20 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 20 Å / % reflection Rfree: 5 % / Rfactor Rfree: 0.284 / Rfactor Rwork: 0.258 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS |