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- PDB-2rnt: THREE-DIMENSIONAL STRUCTURE OF RIBONUCLEASE T1 COMPLEXED WITH GUA... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2rnt | ||||||
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Title | THREE-DIMENSIONAL STRUCTURE OF RIBONUCLEASE T1 COMPLEXED WITH GUANYLYL-2(PRIME),5(PRIME)-GUANOSINE AT 1.8 ANGSTROMS RESOLUTION | ||||||
![]() | RIBONUCLEASE T1 | ||||||
![]() | HYDROLASE(ENDORIBONUCLEASE) | ||||||
Function / homology | ![]() hyphal tip / ribonuclease T1 activity / ribonuclease T1 / cell septum / endonuclease activity / lyase activity / RNA binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Saenger, W. / Koepke, J. / Maslowska, M. / Heinemann, U. | ||||||
![]() | ![]() Title: Three-dimensional structure of ribonuclease T1 complexed with guanylyl-2',5'-guanosine at 1.8 A resolution. Authors: Koepke, J. / Maslowska, M. / Heinemann, U. / Saenger, W. #1: ![]() Title: Crystal Structure of Guanosine-Free Ribonuclease T1, Complexed with Vanadate(V), Suggests Conformational Change Upon Substrate Binding Authors: Kostrewa, D. / Choe, H.-W. / Heinemann, U. / Saenger, W. #2: ![]() Title: Three-Dimensional Structure of the Ribonuclease T1(Asterisk)2(Prime)-Gmp Complex at 1.9-Angstroms Resolution Authors: Arni, R. / Heinemann, U. / Tokuoka, R. / Saenger, W. #3: ![]() Title: Struktur Und Funktion Des Enzyms Ribonuclease T1 (German) Authors: Arni, R. / Heinemann, U. / Saenger, W. #4: ![]() Title: Restrained Least-Squares Refinement of the Crystal Structure of the Ribonuclease T1(Asterisk)2(Prime)Guanylic Acid Complex at 1.9 Angstroms Resolution Authors: Arni, R. / Heinemann, U. / Maslowska, M. / Tokuoka, R. / Saenger, W. #5: ![]() Title: Mechanism of Guanosine Recognition and RNA Hydrolysis by Ribonuclease T1 Authors: Heinemann, U. / Saenger, W. #6: ![]() Title: The Structural and Sequence Homology of a Family of Microbial Ribonucleases Authors: Hill, C. / Dodson, G. / Heinemann, U. / Saenger, W. / Mitsui, Y. / Nakamura, K. / Borisov, S. / Tischenko, G. / Polyakov, K. / Pavlovsky, S. #7: ![]() Title: Ribonuclease T1. Mechanism of Specific Guanine Recognition and RNA Hydrolysis Authors: Heinemann, U. / Saenger, W. #8: ![]() Title: Crystallographic Study of Mechanism of Ribonuclease T1-Catalysed Specific RNA Hydrolysis Authors: Heinemann, U. / Saenger, W. #9: ![]() Title: Specific Protein-Nucleic Acid Recognition in Ribonuclease T1-2(Prime)-Guanylic Acid Complex. An X-Ray Study Authors: Heinemann, U. / Saenger, W. #10: ![]() Title: Crystallization of a Complex between Ribonuclease T1 and 2(Prime)-Guanylic Acid Authors: Heinemann, U. / Wernitz, M. / Paehler, A. / Saenger, W. / Menke, G. / Rueterjans, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 33.1 KB | Display | ![]() |
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PDB format | ![]() | 25.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 944.4 KB | Display | ![]() |
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Full document | ![]() | 953.5 KB | Display | |
Data in XML | ![]() | 9.5 KB | Display | |
Data in CIF | ![]() | 12.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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Atom site foot note | 1: RESIDUES 39 AND 55 ARE CIS PROLINES. |
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Components
#1: Protein | Mass: 11094.694 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-CA / |
#3: Chemical | ChemComp-GPG / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 44.07 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 5 / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 9999 Å / Num. obs: 7069 / Observed criterion σ(F): 1 / Num. measured all: 10563 / Rmerge F obs: 0.0317 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.8→6 Å / σ(F): 3 /
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Refinement step | Cycle: LAST / Resolution: 1.8→6 Å
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Refine LS restraints |
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