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Yorodumi- PDB-1rgc: THE COMPLEX BETWEEN RIBONUCLEASE T1 AND 3'-GUANYLIC ACID SUGGESTS... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1rgc | ||||||
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Title | THE COMPLEX BETWEEN RIBONUCLEASE T1 AND 3'-GUANYLIC ACID SUGGESTS GEOMETRY OF ENZYMATIC REACTION PATH. AN X-RAY STUDY | ||||||
Components | RIBONUCLEASE T1 | ||||||
Keywords | HYDROLASE(ENDORIBONUCLEASE) | ||||||
Function / homology | Function and homology information hyphal tip / ribonuclease T1 / ribonuclease T1 activity / cell septum / RNA endonuclease activity / lyase activity / RNA binding Similarity search - Function | ||||||
Biological species | Aspergillus oryzae (mold) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Heydenreich, A. / Koellner, G. / Choe, H.W. / Cordes, F. / Kisker, C. / Schindelin, H. / Adamiak, R. / Hahn, U. / Saenger, W. | ||||||
Citation | Journal: Eur.J.Biochem. / Year: 1993 Title: The complex between ribonuclease T1 and 3'GMP suggests geometry of enzymic reaction path. An X-ray study. Authors: Heydenreich, A. / Koellner, G. / Choe, H.W. / Cordes, F. / Kisker, C. / Schindelin, H. / Adamiak, R. / Hahn, U. / Saenger, W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1rgc.cif.gz | 55.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1rgc.ent.gz | 39.5 KB | Display | PDB format |
PDBx/mmJSON format | 1rgc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1rgc_validation.pdf.gz | 520.9 KB | Display | wwPDB validaton report |
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Full document | 1rgc_full_validation.pdf.gz | 526.2 KB | Display | |
Data in XML | 1rgc_validation.xml.gz | 6.9 KB | Display | |
Data in CIF | 1rgc_validation.cif.gz | 10.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rg/1rgc ftp://data.pdbj.org/pub/pdb/validation_reports/rg/1rgc | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO A 39 / 2: CIS PROLINE - PRO A 55 / 3: CIS PROLINE - PRO B 39 / 4: CIS PROLINE - PRO B 55 |
-Components
#1: Protein | Mass: 11094.694 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aspergillus oryzae (mold) / Production host: Escherichia coli (E. coli) / References: UniProt: P00651, EC: 3.1.27.3 #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | Has protein modification | Y | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.19 Å3/Da / Density % sol: 43.81 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 4 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2 Å / Lowest resolution: 2.2 Å / % possible obs: 76 % |
-Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Resolution: 2→10 Å / σ(F): 1 /
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Refinement step | Cycle: LAST / Resolution: 2→10 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 10 Å / Num. reflection obs: 11338 / σ(F): 1 / Rfactor obs: 0.153 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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