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Open data
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Basic information
Entry | Database: PDB / ID: 1rgh | ||||||
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Title | HYDROLASE, GUANYLORIBONUCLEASE | ||||||
![]() | RIBONUCLEASE | ||||||
![]() | HYDROLASE (GUANYLORIBONUCLEASE) | ||||||
Function / homology | ![]() ribonuclease T1 activity / ribonuclease T1 / RNA endonuclease activity / lyase activity / RNA binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Sevcik, J. / Dauter, Z. / Lamzin, V.S. / Wilson, K.S. | ||||||
![]() | ![]() Title: Ribonuclease from Streptomyces aureofaciens at atomic resolution. Authors: Sevcik, J. / Dauter, Z. / Lamzin, V.S. / Wilson, K.S. #1: ![]() Title: Complex of Ribonuclease from Streptomyces Aureofaciens with 2'-Gmp at 1.7A Resolution Authors: Sevcik, J. / Hill, C.P. / Dauter, Z. / Wilson, K.S. #2: ![]() Title: Complex of Ribonuclease Sa with a Cyclic Nucleotide and a Proposed Model for the Reaction Intermediate Authors: Sevcik, J. / Zegers, I. / Wyns, L. / Dauter, Z. / Wilson, K.S. #3: ![]() Title: Determination and Restrained Least-Squares Refinement of the Structures of Ribonuclease Sa and its Complex with 3'-Guanylic Acid at 1.8 A Resolution Authors: Sevcik, J. / Dodson, E.J. / Dodson, G.G. #4: ![]() Title: Comparison of Active Sites of Some Microbial Ribonucleases: Structural Basis for Guanylic Specificity Authors: Sevcik, J. / Sanishvili, R.G. / Pavlovsky, A.G. / Polyakov, K.M. #5: ![]() Title: Amino Acid Sequence Determination of Guanyl-Specific Ribonuclease Sa from Streptomyces Aureofaciens Authors: Shlyapnikov, S.V. / Both, V. / Kulikov, V.A. / Dementiev, A.A. / Sevcik, J. / Zelinka, J. #6: ![]() Title: Exocellular Ribonuclease from Streptomyces Aureofaciens. I. Isolation and Purification Authors: Bacova, M. / Zelinkova, E. / Zelinka, J. #7: ![]() Title: Exocellular Ribonuclease from Streptomyces Aureofaciens. II. Properties and Specificity Authors: Zelinkova, E. / Bacova, M. / Zelinka, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 120 KB | Display | ![]() |
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PDB format | ![]() | 96.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.97224, 0.22967, 0.04478), Vector: |
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Components
#1: Protein | Mass: 10582.492 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Chemical | #3: Water | ChemComp-HOH / | Compound details | SECONDARY STRUCTURE BOUNDARIES HAVE BEEN DETERMINED USING SS PROGRAM (V.S.LAMZIN, EMBL HAMBURG) AS ...SECONDARY STRUCTURE BOUNDARIES | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 47.6 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.7 / Method: vapor diffusion | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 1, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Redundancy: 4.1 % / Rmerge(I) obs: 0.039 |
Reflection | *PLUS Highest resolution: 1.2 Å / Num. obs: 60670 / % possible obs: 95.3 % / Num. measured all: 246637 / Biso Wilson estimate: 10.8 Å2 |
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Processing
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Refinement | Resolution: 1.2→10 Å / Num. parameters: 7268 / Num. restraintsaints: 6152 / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER Details: ANISOU VALUES HAVE BEEN SUPPLIED FOR GLU B 54. THEY HAVE GENERATED FOR THE REMAINING ATOMS FROM THE B VALUES.
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Solvent computation | Solvent model: BASED ON BABINET'S PRINCIPLE | |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 5 / Occupancy sum non hydrogen: 1794 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.2→10 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL-93 / Classification: refinement | |||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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