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Yorodumi- PDB-1lra: CRYSTALLOGRAPHIC STUDY OF GLU 58 ALA RNASE T1(ASTERISK)2'-GUANOSI... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1lra | ||||||
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Title | CRYSTALLOGRAPHIC STUDY OF GLU 58 ALA RNASE T1(ASTERISK)2'-GUANOSINE MONOPHOSPHATE AT 1.9 ANGSTROMS RESOLUTION | ||||||
Components | RIBONUCLEASE T1 | ||||||
Keywords | HYDROLASE(ENDORIBONUCLEASE) | ||||||
Function / homology | Function and homology information hyphal tip / ribonuclease T1 activity / ribonuclease T1 / cell septum / endonuclease activity / lyase activity / RNA binding Similarity search - Function | ||||||
Biological species | Aspergillus oryzae (mold) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.9 Å | ||||||
Authors | Pletinckx, J. / Steyaert, J. / Choe, H.-W. / Heinemann, U. / Wyns, L. | ||||||
Citation | Journal: Biochemistry / Year: 1994 Title: Crystallographic study of Glu58Ala RNase T1 x 2'-guanosine monophosphate at 1.9-A resolution. Authors: Pletinckx, J. / Steyaert, J. / Zegers, I. / Choe, H.W. / Heinemann, U. / Wyns, L. #1: Journal: J.Mol.Biol. / Year: 1989 Title: Three-Dimensional Structure of Ribonuclease T1 Complexed with Guanylyl-2',5'-Guanosine at 1.8 Angstroms Resolution Authors: Koepke, J. / Maslowska, M. / Heinemann, U. / Saenger, W. #2: Journal: J.Biol.Chem. / Year: 1988 Title: Three-Dimensional Structure of the Ribonuclease T1(Asterisk)2'-Gmp Complex at 1.9-Angstroms Resolution Authors: Arni, R. / Heinemann, U. / Tokuoka, R. / Saenger, W. #3: Journal: Acta Crystallogr.,Sect.B / Year: 1987 Title: Restrained Least-Squares Refinement of the Crystal Structure of the Ribonuclease T1(Asterisk)2'-Guanylic Acid Complex at 1.9 Angstroms Resolution Authors: Arni, R. / Heinemann, U. / Maslowska, M. / Tokuoka, R. / Saenger, W. #4: Journal: Trends Biochem.Sci.(Pers. Ed.) / Year: 1983 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. #5: Journal: J.Biomol.Struct.Dyn. / Year: 1983 Title: Crystallographic Study of Mechanism of Ribonuclease T1-Catalysed Specific RNA Hydrolysis Authors: Heinemann, U. / Saenger, W. #6: Journal: Nature / Year: 1982 Title: Specific Protein-Nucleic Acid Recognition in Ribonuclease T1-2'-Guanylic Acid Complex. An X-Ray Study Authors: Heinemann, U. / Saenger, W. #7: Journal: Eur.J.Biochem. / Year: 1980 Title: Crystallization of a Complex between Ribonuclease T1 and 2'-Guanylic Acid Authors: Heinemann, U. / Wernitz, M. / Paehler, A. / Saenger, W. / Menke, G. / Rueterjans, H. #8: Journal: J.Mol.Biol. / Year: 1991 Title: Ribonuclease T1 with Free Recognition and Catalytic Site: Crystal Structure Analysis at 1.5 Angstroms Authors: Martinez-Oyanedel, J. / Choe, H.-W. / Heinemann, U. / Saenger, W. #9: Journal: Biochemistry / Year: 1990 Title: Histidine-40 of Ribonuclease T1Acts as Base Catalyst When the True Catalytic Base, Glutamic Acid 58 is Replaced by Alanine Authors: Steyaert, J. / Hallenga, K. / Wyns, L. / Stanssens, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lra.cif.gz | 32 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lra.ent.gz | 23.7 KB | Display | PDB format |
PDBx/mmJSON format | 1lra.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1lra_validation.pdf.gz | 462.4 KB | Display | wwPDB validaton report |
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Full document | 1lra_full_validation.pdf.gz | 471.1 KB | Display | |
Data in XML | 1lra_validation.xml.gz | 5.5 KB | Display | |
Data in CIF | 1lra_validation.cif.gz | 7.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lr/1lra ftp://data.pdbj.org/pub/pdb/validation_reports/lr/1lra | 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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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO 39 / 2: CIS PROLINE - PRO 55 |
-Components
#1: Protein | Mass: 11036.658 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aspergillus oryzae (mold) / References: UniProt: P00651, EC: 3.1.27.3 |
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#2: Chemical | ChemComp-NA / |
#3: Chemical | ChemComp-2GP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 1.88 Å3/Da / Density % sol: 34.41 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 4.2 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.9 Å / Rmerge(I) obs: 0.069 |
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-Processing
Software | Name: PROFFT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.9→10 Å / σ(F): 1 /
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Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
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Refine LS restraints |
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Software | *PLUS Name: PROFT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 10 Å / Num. reflection obs: 5659 / σ(F): 1 / Rfactor obs: 0.178 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |